Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined
under the first inventor to file provisions of the AIA .
DETAILED ACTION
Claims 1, 26-29, 33, 39, 44, and 46 are pending in the instant application.
A request for continued examination under 37 CFR 1.114, including the fee set forth in 37 CFR 1.17(e), was filed in this application after final rejection. Since this application is eligible for continued examination under 37 CFR 1.114, and the fee set forth in 37 CFR 1.17(e) has been timely paid, the finality of the previous Office action has been withdrawn pursuant to 37 CFR 1.114. Applicant's submission filed on 6/29/2026 has been entered.
Claim Rejections Withdrawn
The rejection to claims 3-4, 6, 9-10, 12, 14, 16, 19, 22-25, and 47-48 are moot in view of claim cancelation.
The rejections to claims 1, 26-29, 33, 39, and 44 under 35 USC §103 are withdrawn in view of claim amendment.
The rejections to claims 1, 26-29, 33, 39, and 44 under Nonstatutory Double Patenting are withdrawn in view of claim amendment.
Claim Status
Applicant’s election without traverse of 1) Group I, claims 1, 3-4, 6, 9-10, 12, 14, 16, 19, 22-29, 33, 39, and 44, drawn to the technical feature of an antibody drug conjugate having a structure of Ab-(L-D)k; and 2) A: the L-D species set forth in claim 25 of:
PNG
media_image1.png
133
555
media_image1.png
Greyscale
and
B: a HCDR 1, a HCDR2 and a HCDR3 set forth in SEQ ID NO: 7, SEQ ID NO: 8 and SEQ ID NO: 9 in the reply filed on 7/14/2025 was addressed and made final in the Non-Final Rejection filed on 11/18/2025. Claim 46 was previously withdrawn in the Non-Final Rejection filed on 11/18/2025 as not containing an elected invention or species.
The elected species is not present in the amended claims.
The Examiner previously included the L-D species of
PNG
media_image2.png
209
558
media_image2.png
Greyscale
Claims 1, 26-27, 29, and 44 read on the Examiner elected species.
The Examiner will further include the antibody anti-TROP-2 antibody PD3, which comprises a VH of SEQ ID NO:29 and a VL of SEQ ID NO:30 present in instant claims 33 and 39. Claims 33 and 39 are rejoined for the second Examiner elected antibody.
Claim 46 remains withdrawn.
Priority
Should applicant desire to obtain the benefit of foreign priority under 35 U.S.C.
119(a)-(d) prior to declaration of an interference, a certified English translation of the
foreign application must be submitted in reply to this action. 37 CFR 41.154(b) and
41.202(e).
Failure to provide a certified translation may result in no benefit being accorded
for the non-English application. The effective priority date is the filing date of
PCT/CN2021/073314 filed on 1/22/2021 in the absence of a certified translation of
CN202010073671.6 filed on 1/22/2020, CN202010114980.3 filed on 2/25/2020, or CN202011153368.3. filed on 10/26/2020.
Claim Rejections Necessitated by Amendment
Claim Rejections - 35 USC § 112(b)
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 33 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Regarding instant claim 33, an antibody is claimed that comprises a heavy chain variable region comprising an HCDR1, HCDR2, and HCDR3 set forth in SEQ ID NO:29 and a light chain variable region comprising an LCDR1, LCDR2, and LCDR3 set forth in SEQ ID NO:30, but the sequence of the CDR regions are not defined. Thus, the metes and bounds are unclear and the claim is indefinite.
Two separate requirements are set forth in 35 U.S.C. 112(b) and pre-AIA 35 U.S.C. 112, second paragraph, namely that:
1) (A) the claims must set forth the subject matter that the inventor or a joint inventor regards as the invention; and
2) (B) the claims must particularly point out and distinctly define the metes and bounds of the subject matter to be protected by the patent grant.
The first requirement is a subjective one because it is dependent on what the inventor or a joint inventor for a patent regards as his or her invention. Note that although pre-AIA 35 U.S.C. 112, second paragraph, uses the phrase "which applicant regards as his invention," pre-AIA 37 CFR 1.41(a) provides that a patent is applied for in the name or names of the actual inventor or inventors.
The second requirement is an objective one because it is not dependent on the views of the inventor or any particular individual, but is evaluated in the context of whether the claim is definite — i.e., whether the scope of the claim is clear to a hypothetical person possessing the ordinary level of skill in the pertinent art.
To promote compact prosecution, the CDR regions will be defined by the Kabat numbering scheme as identified in the instant specification page 79 Table 4, wherein the antibody comprises a heavy chain variable region comprising an HCDR1, HCDR2, and HCDR3 of SEQ ID NO:23, 24, and 25, respectively, and a light chain variable region comprising an LCDR1, LCDR2, and LCDR3 of SEQ ID NO:26, 27, and 28, respectively.
Claim Rejections – 35 USC § 112(a)
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claims 1, 26-27, 29, 33, 39, and 44 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to reasonably convey to one skilled in the relevant art that the inventor or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
Regarding instant claims 1 and 39, a maleimide linker is attached to an antibody for the antibody-drug conjugates and the disclosure teaches antibody conjugation via cysteine residues, but linker conjugates bound to the antibody are claimed as a number, k, between 1 and 10. Cysteine drug conjugates produced via partial reduction of interchain disulfide bonds generate up to eight reactive cysteine thiol groups, thus, only k values 1-8 are available for conjugation. Instant claims 26-27, 29, 33, and 44 are dependent on instant claim 1 without including k as a maximum of 8.
Scope of the claimed genus
Regarding instant claims 1 and 39, antibody-drug conjugates are claimed represented by the following formula
PNG
media_image3.png
174
491
media_image3.png
Greyscale
wherein k is 1 to 10, wherein a maleimide linker is attached to an antibody for the antibody-drug conjugates.
Summary of Species disclosed in the original specification
MPEP § 2163 states that a “representative number of species” means that the species which are adequately described are representative of the entire genus. Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus.
1) The instant specification taught antibody reduction and conjugation of the linker-toxin ADC-3 on page 102 of the instant specification, paragraph 289, wherein TCEP reduction of the antibody would prepare the cysteine residues for coupling to produce a k of about 4. The instant specification does not have examples of antibody drug conjugates wherein the number of conjugates is more than 8.
State of the Relevant Art
The prior art has taught most ADCs are synthesized by conjugating a cytotoxic compound or “payload” to a monoclonal antibody (Behrens CR et al. (Mol. Pharmaceutics 2015, 12, 11, 3986–3998), page 3986, left column, first paragraph). Behrens taught the payloads are conjugated using amino or sulfhydryl specific linkers that react selectively with lysines or cysteines on the antibody surface, wherein a typical antibody contains over 50 lysines and eight interchain cysteines as potential conjugation sites (page 3986, left column, first paragraph). Behrens taught conjugation through antibody cysteines minimizes ADC heterogeneity relative to lysine conjugation because there are fewer potential conjugation sites (page 3986, right column, first paragraph). The process typically involves partial reduction of four antibody interchain disulfide bonds to generate up to eight reactive cysteine thiol groups, followed by conjugation of payloads containing thiol-specific maleimide linkers (page 3986, right column, first paragraph). Behrens taught ADCs with suboptimal DARs are prone to aggregation, poor solubility, and instability, which often lead to increased toxicity and/or inadequate efficacy in vivo (page 3986, left column, first paragraph). Behrens taught the discrepancy between the number of potential conjugation sites and the desired DAR, combined with the use of linkers that lack site-specificity, results in heterogeneous ADCs that vary in both DAR and the conjugation sites (page 3986, left to right column bridging sentence). Behrens taught consequently, most of the ADCs in clinical development for cancer indications contain dozens or more of chemically distinct ADC molecules, each with unique pharmacological properties (page 3986, right column, first paragraph). Thus, linker-drug conjugates would conjugate up to 8 cysteines on the antibody.
Summary
1) Regarding instant claims 1, 26-27, 29, 33, 39, and 44, the instant specification does not have written description of the ligand-drug structure conjugated to an antibody of n values greater than 8.; and
Claim Rejections – 35 USC § 103
In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status.
The following is a quotation of 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action:
A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows:
1. Determining the scope and contents of the prior art.
2. Ascertaining the differences between the prior art and the claims at issue.
3. Resolving the level of ordinary skill in the pertinent art.
4. Considering objective evidence present in the application indicating obviousness or nonobviousness.
Regarding the species of:
PNG
media_image2.png
209
558
media_image2.png
Greyscale
Claims 1, 26-27, 29, and 44 are rejected under 35 U.S.C. 103 as being unpatentable over US 2017/0252458 (Albone EF et al. reference of record), Narayan S et al. (Bioorganic & Medicinal Chemistry Letters 2011 21(6) 1634-1638 reference of record), and WO 2020156439 (Yang C priority to 01/28/2019 reference of record).
Albone taught antibody-drug conjugates (ADC) of ER1159569 conjugated to the antibodies trastuzumab or MORAb009 in a pharmaceutical composition with a pharmaceutically acceptable excipient, wherein the ADCs were dose-dependently effective when administered to cancer cells that expressed the antibody target (page 117, Table 49, Row 3 and 4), wherein ER1159569 had the structure of
PNG
media_image4.png
331
725
media_image4.png
Greyscale
(page 79, Table 46, Row 1), wherein the trastuzumab-ER1159569 had a drug to antibody ratio (DAR) of about 3 and MORAb009-ER1159569 had DAR of about 5 (page 112, Table 47, Rows 7-8)
Albone did not teach ADCs with the structure:
PNG
media_image2.png
209
558
media_image2.png
Greyscale
wherein the D is
PNG
media_image5.png
163
209
media_image5.png
Greyscale
, but this is obvious in view of Narayan and Yang C.
Narayan taught conversion of the C34 hydroxyl (OH) to the methyl ether (OCH3 or OMe) in eribulin analogs was found to enhance potency of the drug in drug resistant cancer cells and lower the fold-resistance ratio (drug resistant cancer cell IC50 value/ cancer cell IC50 value (page 1636-1637, bridging paragraph and Table 1). Narayan taught where present, conversion of the C34 hydroxyl to the methyl ether was found to lower the drug resistance ratio (page 1636, right column, last column). Narayan taught compound 25, which comprised a C34 substituent of OMe, had better pharmacokinetic properties compared to eribulin, which comprised a C34 substituent of OH, wherein area under the curve and clearance were calculated (Table 2). Narayan taught compound 25, which comprised a C34 substituent of OMe, was effective when administered in a pharmaceutical composition with a pharmaceutically acceptable excipient to a subject with cancer (Fig. 6). Narayan taught exchange of the C34 OH present in Compound 16 to OMe in Compound 25 produced an eribulin analog with a more potent IC50 value against drug resistant cancer cells, wherein the IC50 value of Compound 16 was 7.26 nM compared to 1.91 nM for Compound 25 against MES-SA/Dx5-Rx1 cells (Fig. 3 and Table 1).
PNG
media_image6.png
96
110
media_image6.png
Greyscale
PNG
media_image7.png
103
112
media_image7.png
Greyscale
PNG
media_image8.png
95
103
media_image8.png
Greyscale
Thus, individual exchange of a C34 substituent of OH to OMe is expected to be more effective.
Yang C taught mAB015 clone 83B2G2 effectively bound CD79b via ELISA (Fig. 7) and FACS (Fig. 8) and comprised a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 (translated page 12, [149]). Yang C taught mAB015 effectively bound CD79b to a level similar to the positive control SN38 which is the FDA approved antibody-conjugated drug polatuzumab vedotin (translated page 13, [0155]). Yang C taught an anti-CD79B antibody or an antibody-drug conjugate and a pharmaceutical composition thereof, and a method using the same for treating or delaying cancer, especially hematopoietic tumors (translated page 2, [0010]), wherein the ADC comprises an antibody covalently coupled to a drug through a linker, wherein the drug is a cytotoxic agent (translated page 5, [0069]-[0070]). Yang taught diffuse large B-cell lymphoma (DLBCL) is a B-cell lymphoma, wherein the B cell receptor (BCR) complex is the most major molecule on the surface of B cells, wherein the BCR complex comprises Igβ (CD79B) heterodimers that transmit antigen stimulation signals (translated page 2, [0006]).
Regarding instant claims 1, 26-27, 29, and 44, it would have been obvious for a person having ordinary skill in the art to take the effective pharmaceutical composition of an ADC of Albone comprising ER1159569 conjugated to trastuzumab with a DAR of about 3 in a pharmaceutically acceptable excipient – and modify the ADC to:
1) exchange the C34 substituent from -OH to methyl ether (-OCH3 or -OMe) in view of Narayan; and 2) exchange the trastuzumab antibody for mAB015 of Yang C.
PNG
media_image9.png
274
554
media_image9.png
Greyscale
This is obvious because: 1a) Narayan taught conversion of the C34 hydroxyl to the methyl ether was found to enhance potency in drug resistant cancer cells, wherein where present, conversion of the C34 hydroxyl to the methyl ether was found to lower the drug resistance ratio; 1b) Narayan taught compound 25, which comprised a C34 substituent of OMe, was effective at treating cancer cells and had better pharmacokinetic properties compared to eribulin, which comprised a C34 substituent of OH; 1c) Narayan taught exchange of the C34 OH present in Compound 16 to OMe in Compound 25 produced an eribulin analog with a more potent IC50 value against drug resistant cancer cells, wherein the IC50 value of Compound 16 was 7.26 nM compared to 1.91 nM for Compound 25 against MES-SA/Dx5-Rx1 cells. Thus, individual exchange of a C34 substituent of OH to OMe is obvious and expected to be more effective; and 2) mAB015 effectively binds CD79b, which is expressed on cancer cells, and mAB015 binds CD79b as effectively as the antibody for the FDA approved antibody-conjugated drug polatuzumab vedotin as taught by Yang C.
There is a reasonable expectation of success because: 1a) Narayan taught conversion of the C34 hydroxyl to the methyl ether was found to enhance potency in drug resistant cancer cells, wherein where present, conversion of the C34 hydroxyl to the methyl ether was found to lower the drug resistance ratio; 1b) Narayan taught compound 25, which comprised a C34 substituent of OMe, was effective at treating cancer cells and had better pharmacokinetic properties compared to eribulin, which comprised a C34 substituent of OH; 1c) Narayan taught exchange of the C34 OH present in Compound 16 to OMe in Compound 25 produced an eribulin analog with a more potent IC50 value against drug resistant cancer cells, wherein the IC50 value of Compound 16 was 7.26 nM compared to 1.91 nM for Compound 25 against MES-SA/Dx5-Rx1 cells. Thus, individual exchange of a C34 substituent of OH to OMe is expected to be more effective; and 2) mAB015 effectively binds CD79b, which is expressed on cancer cells, and mAB015 binds CD79b as effectively as the antibody for the FDA approved antibody-conjugated drug polatuzumab vedotin as taught by Yang C.
This would produce an ADC of mAB015 as the Ab with a drug conjugate structure of
PNG
media_image2.png
209
558
media_image2.png
Greyscale
wherein k is 3 and D has the structure of:
PNG
media_image10.png
168
212
media_image10.png
Greyscale
, wherein R1a is methyl and R1b is H, in a pharmaceutical composition with a pharmaceutically acceptable excipient and meets the claim limitations of the Examiner elected species present in instant claims 1, 26-27, 29, and 44.
Response to Arguments
Independent claim 1 has been amended.
The updated rejection is above.
Applicant argues in the Final Office Action, the Examiner noted that while the ADC-3 structure demonstrated surprising results, the claims at the time covered a much broader range of L-D structures. By amending the claims to be limited to the specific structure of ADC-3, the Applicants have directly addressed this concern. Under MPEP 716.02(d), objective evidence of nonobviousness is highly persuasive when the evidence is commensurate in scope with the claims. Since the claims are now restricted to the very structure that produced the surprising results acknowledged by the Examiner, the rejection should be withdrawn.
In response, Applicant's arguments filed 6/29/2026 have been fully considered
but they are not persuasive. In the Advisory Action filed 6/16/2026 the Examiner indicated the surprising results encompassed ADC-3, wherein the structure contains a PD3 antibody conjugated to the linker drug, wherein R1 bis hydrogen, and wherein the R1 a group in claim 1 is a methyl. Claim 1 requires conjugation of the PD3 antibody comprising a VH of instant SEQ ID NO:29 and comprising a VL of instant SEQ ID NO:30. MPEP 716.02(d) requires unexpected results to be commensurate in scope with the claimed invention. Whether the unexpected results are the result of unexpectedly improved results or a property not taught by the prior art, the "objective evidence of nonobviousness must be commensurate in scope with the claims which the evidence is offered to support." Thus, the current scope of the claims are not commensurate with the surprising results. The structure of ADC-3 with surprising results is:
PNG
media_image11.png
246
656
media_image11.png
Greyscale
wherein the antibody is PD3. While the Examiner elected species has the same (L-D) as the ADC with surprising results, the instant claims are not commensurate in scope with a single surprising ADC species in the claim.
Applicants respectfully but strongly traverse this rejection. The cited references, whether taken individually or in combination, fail to provide any motivation or a reasonable expectation of success for the specific structural modifications claimed, and the Examiner's rejection relies on impermissible hindsight. Applicants submit the following arguments in response to the Examiner's response presented in the Advisory Action.
Applicant argues:
1. Narayan Discloses Simultaneous Multi-Site Modifications and Fails to Suggest Isolated C34 Methylation. According to pending claims 1 and 39, the drug moiety (-D) possesses a precise eribulin core structure wherein the C34 position is restricted to a methyl ether (-OMe) while the C35 position remains strictly as an unmodified primary amine (-CH2NH2).
The Examiner relies on Compound 25 of Narayan to bridge the gap for the C34 methyl ether. However, as disclosed in Figure 2 and Figure 3 of Narayan, Compound 25 is a second generation analog that was obtained by concurrently changing multiple. distinct chemical variables. Namely, the C34 hydroxyl group was converted to a methyl ether (-OMe) and the primary amine moiety at the C35 position was completely replaced with a bulky morpholine ring.
Narayan provides absolutely no empirical data or comparative analysis for any derivative that contains only the C34 methyl ether while retaining the intact, basic C35 primary amine. Because these multiple structural modifications were introduced simultaneously to achieve the desired effect, the technical data in Narayan cannot isolate, and does not attribute, the observed enhancement in potency or pharmacokinetic profile to the C34 methylation alone. For at least this reason, the rejection should be withdrawn.
2. The Overcoming of P-gp Resistance in Narayan is Driven by Amine Basicity Attenuation, Not C34 Methylation. Furthermore, Applicants submit that the Examiner's technical premise directly contradicts the central therapeutic mechanism taught by Narayan. Specifically, Narayan explicitly states that the primary amine moiety of eribulin is the root cause of its P-glycoprotein (P-gp) efflux liability and subsequent multi-drug resistance (MOR). To solve this, Narayan's explicit design strategy was "attenuation of basicity of the amino group(s) in the C32 side-chain region led to compounds with low susceptibility to Pgp-mediated drug efflux."
The introduction of the morpholine ring at the C35 position in Compound 25 was precisely the structural vehicle used to reduce the basicity of the nitrogen atom, thereby successfully preventing the drug from being pumped out by P-gp. As demonstrated in Table 1 and Figure 4 of Narayan, lowering the Fold-Resistance (FR) is inherently correlated with modifying the amine basicity (e.g., forming morpholines, acyl piperazines, or adding ring strain). The C34 modification was merely an incidental alteration tested within that tertiary amine subgroup.
Therefore, a person having ordinary skill in the art reading Narayan would conclude that the biological efficacy of Compound 25 relies on the attenuation of the amino group's basicity via the morpholine ring. Narayan provides zero incentive, let alone a reasonable expectation of success, that isolated C34 methylation - in the presence of a highly basic C35 primary amine (as required by present claim 1) - would yield any improved performance against resistant tumors. For at least this reason, the rejection should be withdrawn.
3. Control-Variable Analysis of Naravan's Table 1 Proves that Activity Variance is Driven by Amine Structures. Applicants submit that Table 1 of Narayan lists numerous analogs that all possess the C34-methoxy substituent (e.g., Compounds 17 and 19-32). Despite sharing the exact same C34- methoxy feature, these compounds exhibit vastly different pharmacological profiles. Namely, Compound 17 (methoxy-containing) shows an unacceptably high FR of 38.10, and Compound 32 (methoxy-containing) shows a significantly lower FR of 3.99. These data points clearly demonstrate that the structural variations in the amino side chain - and not the methoxy group - are the decisive factors responsible for the observed differences in IC5o and FR values. For at least this reason, the rejection should be withdrawn.
4. Deficiency of Yang C and Lack of Motivation to Combine Three Disparate Systems. Applicants submit that Yang C is deficient to provide any motivation to combine with the other cited references. Specifically, the Examiner further brings in Yang teach the anti-CD79B antibody (mAB015). However, an ADC is an interconnected macromolecular system where the antibody, linker, and payload must be precisely balanced. A/bone discloses a completely different ADC system comprising ER1159569 conjugated to trastuzumab (an anti-HER2 antibody). There is no structural or functional hint in A/bone to modify its payload at the C34 position.
To arrive at the present invention, a PHOSITA would have to: (1) select the specific trastuzumab ADC from A/bone; (2) pluck out the C34 modification from Narayan's multi-variable Compound 25, while ignoring Narayan's primary teaching to modify the C35 amine; and (3) discard A/bone's anti-HER2 antibody system entirely and replace it with Yang C's anti-CD79B antibody. Applicants argue that this multi-step "pick-and-choose" approach across three disparate references could only be performed if the person of ordinary skill in the art had the Applicants' specification in front of them as a blueprint. This is the definition of an impermissible hindsight rejection. For at least this reason, the rejection should be withdrawn.
In response, Applicant's arguments filed 6/29/2026 have been fully considered
but they are not persuasive. The obvious rational is above.
Regarding 1) and 2), Narayan taught conversion of the C34 hydroxyl (OH) to the methyl ether (OCH3 or OMe) was found to enhance potency of the drug in drug resistant cancer cells and lower the fold-resistance ratio (drug resistant cancer cell IC50 value/ cancer cell IC50 value (page 1636-1637, bridging paragraph and Table 1). Narayan taught where present, conversion of the C34 hydroxyl to the methyl ether was found to lower the drug resistance ratio (page 1636, right column, last column). Thus, inclusion of a OMe at C34 is obvious with a reasonable expectation of success. Regarding a bulky morpholine ring, multiple distinct chemical variables, and overcoming resistance: Narayan taught exchange of the C34 OH present in Compound 16 to OMe in Compound 25 produced an eribulin analog with a more potent IC50 value against drug resistant cancer cells, wherein the IC50 value of Compound 16 was 7.26 nM compared to 1.91 nM for Compound 25 against MES-SA/Dx5-Rx1 cells. Thus, individual exchange of a C34 substituent for OH to OMe is obvious and expected to be more effective when the rest of the molecule was held constant and empirical data of changes at the C34 position to OMe. The C34OMe is not an incidental alteration and is taught by Narayan to have an improved effect.
Regarding 3) as described above, Narayan taught exchange of the C34 OH present in Compound 16 to OMe in Compound 25 produced an eribulin analog with a more potent IC50 value against drug resistant cancer cells, wherein the IC50 value of Compound 16 was 7.26 nM compared to 1.91 nM for Compound 25 against MES-SA/Dx5-Rx1 cells. Thus, individual exchange of a C34 substituent for OH to OMe is obvious and expected to be more effective when the rest of the molecule was held constant and empirical data of changes at the C34 position to OMe.
Regarding 4), as described above, it would be obvious with a reasonable expectation of success to exchange the trastuzumab antibody for mAB015 of Yang because Yang taught mAB015 effectively binds CD79b, which is expressed on cancer cells, and mAB015 binds CD79b as effectively as the antibody for the FDA approved antibody-conjugated drug polatuzumab vedotin.
Thus, as indicated above, it would have been obvious for a person having ordinary skill in the art to take the effective pharmaceutical composition of an ADC of Albone comprising ER1159569 conjugated to trastuzumab with a DAR of about 3 in a pharmaceutically acceptable excipient – and modify the ADC to:
1) exchange the C34 substituent from -OH to methyl ether (-OCH3 or -OMe) in view of Narayan; and 2) exchange the trastuzumab antibody for mAB015 of Yang C. The obvious rational is above.
In response to applicant's argument that the examiner's conclusion of obviousness is based upon improper hindsight reasoning, it must be recognized that any judgment on obviousness is in a sense necessarily a reconstruction based upon hindsight reasoning. But so long as it takes into account only knowledge which was within the level of ordinary skill at the time the claimed invention was made, and does not include knowledge gleaned only from the applicant's disclosure, such a reconstruction is proper. See In re McLaughlin, 443 F.2d 1392, 170 USPQ 209 (CCPA 1971).
Applicants respectfully and strongly traverse that ADC-3 is not commensurate in scope with the unexpected results wherein PD3 is necessary for the unexpected results. Under MPEP 716.02(d), objective evidence is legally sufficient and commensurate in scope if the unexpected properties are shown to be a shared characteristic inherent to the structural core common to the claimed genus. Applicants submit that the unexpected results are inherently driven by the novel payload platform, rendering the upper generic scope fully patentable based on the following multi-tiered technical evidence and the fundamental mechanism of ADC therapeutics.
1. The Core Effector Moiety (Free Payload) Possesses Independent Non-Obviousness and Unpredictable PK Advantages. As established in Test Example 1 of the present specification, the specific free payload compound utilized in the present invention (wherein R1 a is methyl and R1 bis hydrogen; "Methyl Eribulin") per se exhibits an extraordinary 4-fold increase in Area Under the Curve (AUC) and a remarkable 8-fold extension in plasma half-life (t1/2) in vivo compared to standard free Eribulin.
In the field of medicinal chemistry, such a drastic, order-of-magnitude leap in metabolic stability resulting from a discrete structural modification (C34 methylation) is entirely unpredictable and represents an independent, significant technical advancement over the prior art (such as Narayan). Consequently, the core payload molecule itself possesses independent nonobviousness based on these unexpected properties. For at least this reason, the rejection should be withdrawn.
2. In ADC Systems, the Cytotoxic Effector (Payload) Dictates the Core Efficacy and Metabolic Superiority.
It is a fundamental axiom in Antibody-Drug Conjugate (ADC) technology that while the antibody serves as the targeted delivery vehicle (the "homing mechanism" to find target cancer cells) and the linker dictates stable circulation, the payload is the ultimate cytotoxic effector that governs intrinsic anti-tumor efficacy and the metabolic footprint once internalized into target cells. Since the specific Methyl-Eribulin core itself possesses independent, non-obvious pharmacological and PK advantages, any ADC incorporating this inventive core will inherently inherit and benefit from these superior traits. Therefore, the structural innovation driving the total conjugate's superiority resides primarily within the payload, rendering the ADC as a whole patentable. Therefore, for at least this reason, the rejection should be withdrawn.
3. Strict Control-Variable Data (ADC-3 vs. ADC-2) Confirms the Decisive Contribution of the Novel Payload.
To conclusively isolate and prove the payload's deterministic contribution within an ADC entity, the specification provides a rigorous, direct parallel comparative study between ADC-3 and ADC-2 in the Examples section. Specifically, the Examples provide identical variables, wherein ADC-3 and ADC-2 share the exact same monoclonal antibody (PD3) and the exact same chemical linker. Furthermore, the Examples demonstrate the sole variable, wherein the only structural difference lies in the payload-ADC-2 utilizes standard Eribulin, whereas ADC-3 utilizes the claimed Methyl-Eribulin.
Applicants submit that the biological data in the specification demonstrate that ADC-3 exhibits significantly superior anti-tumor efficacy and tumor volume control compared to ADC-2. Because all other components (antibody and linker) were held completely constant, this strict parallel comparison provides irrefutable empirical proof that the quantum leap in ADC therapeutic performance is directly, exclusively, and causally driven by the transition from Eribulin to the claimed Methyl-Eribulin payload. For at least this reason, the rejection should be withdrawn.
4. The Surprising Results are a Common Denominator Across the Upper Genus Scope, Supporting the Broad Claims. Because the specification has proven that (i) free Methyl-Eribulin has an independent PK breakthrough (4-fold AUG, 8-fold t112), and (ii) inserting this payload into an ADC (ADC-3) results in a definitive therapeutic superiority over an Eribulin-based ADC (ADC-2) due solely to the payload substitution, it is both scientifically and legally sound that these unexpected results are a shared, inherent characteristic common to the entire genus of claim 1.
Regardless of which standard, tumor-targeting antibody is selected to deliver this payload linker platform, the internal cellular mechanism of action and the enhanced cytotoxicity driven by the Methyl-Eribulin core remain identically superior.
While MPEP 716.02(d) requires objective evidence to be commensurate in scope, it does not require an Applicants to test every single species or antibody variant within a claim. Showing a significant, unexpected improvement on a representative embodiment (ADC-3) that embodies the core inventive feature - that is, the specific C34-methylated eribulin derivative payload conjugated via the specified linker - is legally sufficient to support the non-obviousness of the genus claims containing that identical core feature. Therefore, the objective evidence is fully commensurate in scope with the upper genus claims under MPEP 716.02(d), and the rejection should be withdrawn.
In response, Applicant's arguments filed 6/29/2026 have been fully considered
but they are not persuasive. Regarding 1) - 4) while methyl eribulin has a 4-fold increase in Area Under the Curve (AUC) and a remarkable 8-fold extension in plasma half-life (t/12) in vivo compared to standard free eribulin,
the payloads are present in an ADC and would be internalized into cancer cells for cleavage of the linker and eribulin analog toxicity. This would include ADC-2 with the OH at the C34 position
PNG
media_image12.png
214
590
media_image12.png
Greyscale
as shown in Example 2-15 and ADC-3 with a C34 position OMe. The IC50 values in Table 8 of the instant specification indicate that ADC-2, which comprises: 1) the linker drug of ER1159569; and 2) the same antibody and linker combination as ADC-3, but includes a OMe at ADC-3, is more potent in cancer cell-based assays compared to ADC-3 (page 107, [315]).
PNG
media_image13.png
147
597
media_image13.png
Greyscale
Thus, the cytotoxic payload was more potent in cancer cell-based assays. Further, while the instant specification described that a bystander effect is present for all ADCs tested (page 109, [0322]), which could result in release of free payload, the ADC-2 potency was greater than ADC-3 in the IC50 assays above shown in Table 8. Thus, the effects of a drug administered in the absence of an antibody linker did not reflect the IC50 potency differences in Table 8 above. Thus, the ADC-3 surprising benefits were shown in vivo for Table 11 (specification, page 114, [341]), wherein ADC-3 comprised the PD3 antibody and the linker drug structure, was surprisingly effective when administered to a subject with cancer that expressed TROP-2 in vivo when compared to ADC-2. These disparate in vivo effects are shown to be present in an ADC only with the PD3 antibody attached to the claimed linker drug.
Claims 1, 26-27, 29, and 44 are rejected under 35 U.S.C. 103 as being unpatentable over US 2023/0405138 (Ren W et al.).
Ren taught an effective method of treating cancer in a subject comprising administering a pharmaceutical composition comprising a pharmaceutically acceptable excipient and ADC-1 (Fig 18), wherein ADC-1 comprises a structure of
PNG
media_image14.png
216
627
media_image14.png
Greyscale
conjugated to antibody hAb015-10 with a n of about 3 (page 61, paragraph 494-497), and effectively targets CD79B (page 6, Table 10). Ren taught mAb015 effectively targets CD79B (page 39, Table 2 and Fig. 8), wherein mAb015 comprises a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 (page 40, paragraphs 386-387).
Ren does not describe a single embodiment of the structure of ADC-1 bound to mAb015, but this is obvious in view of Ren’s teaching that mAb015 effectively targets CD79B.
Regarding instant claims 1, 26-27, 29, and 44, it would have been obvious for a person having ordinary skill in the art to take the effective method of treating cancer in a subject comprising administering a pharmaceutical composition comprising a pharmaceutically acceptable excipient and ADC-1, wherein ADC-1 comprises a structure of
PNG
media_image14.png
216
627
media_image14.png
Greyscale
conjugated to antibody hAb015-10 with a n of about 3, wherein hAB015-10 effectively targets CD79B – and:
Exchange the CD79B targeting antibody hAB015-10 for mAb015 which effectively targets CD79B as taught by Ren.
This is obvious because: 1) Ren taught an effective method of treating cancer in a subject comprising administering a pharmaceutical composition comprising a pharmaceutically acceptable excipient and ADC-1, wherein ADC-1 comprises the antibody hAb015-10 which effectively targets CD79B and that mAb015 also effectively targets CD79B.
There is a reasonable expectation of success because: 1) Ren taught an effective method of treating cancer in a subject comprising administering a pharmaceutical composition comprising a pharmaceutically acceptable excipient and ADC-1, wherein ADC-1 comprises the antibody hAb015-10 which effectively targets CD79B and that mAb015 also effectively targets CD79B
This would produce a method of treating cancer in a subject comprising administering a pharmaceutical composition comprising a pharmaceutically acceptable excipient and an ADC comprising mAB015 as the antibody with a drug conjugate structure of
PNG
media_image14.png
216
627
media_image14.png
Greyscale
, wherein n is about 3, wherein mAb015 comprises a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 which comprises a VH comprising instant SEQ ID NO:7-9 and a VL comprising instant SEQ ID NO:10-12, and meets the claim limitations of the Examiner elected species present in instant claims 1, 26-27, 29, and 44.
Double Patenting
The nonstatutory double patenting rejection is based on a judicially created doctrine grounded in public policy (a policy reflected in the statute) so as to prevent the unjustified or improper timewise extension of the “right to exclude” granted by a patent and to prevent possible harassment by multiple assignees. A nonstatutory double patenting rejection is appropriate where the conflicting claims are not identical, but at least one examined application claim is not patentably distinct from the reference claim(s) because the examined application claim is either anticipated by, or would have been obvious over, the reference claim(s). See, e.g., In re Berg, 140 F.3d 1428, 46 USPQ2d 1226 (Fed. Cir. 1998); In re Goodman, 11 F.3d 1046, 29 USPQ2d 2010 (Fed. Cir. 1993); In re Longi, 759 F.2d 887, 225 USPQ 645 (Fed. Cir. 1985); In re Van Ornum, 686 F.2d 937, 214 USPQ 761 (CCPA 1982); In re Vogel, 422 F.2d 438, 164 USPQ 619 (CCPA 1970); In re Thorington, 418 F.2d 528, 163 USPQ 644 (CCPA 1969).
A timely filed terminal disclaimer in compliance with 37 CFR 1.321(c) or 1.321(d) may be used to overcome an actual or provisional rejection based on nonstatutory double patenting provided the reference application or patent either is shown to be commonly owned with the examined application, or claims an invention made as a result of activities undertaken within the scope of a joint research agreement. See MPEP § 717.02 for applications subject to examination under the first inventor to file provisions of the AIA as explained in MPEP § 2159. See MPEP § 2146 et seq. for applications not subject to examination under the first inventor to file provisions of the AIA . A terminal disclaimer must be signed in compliance with 37 CFR 1.321(b).
The filing of a terminal disclaimer by itself is not a complete reply to a nonstatutory double patenting (NSDP) rejection. A complete reply requires that the terminal disclaimer be accompanied by a reply requesting reconsideration of the prior Office action. Even where the NSDP rejection is provisional the reply must be complete. See MPEP § 804, subsection I.B.1. For a reply to a non-final Office action, see 37 CFR 1.111(a). For a reply to final Office action, see 37 CFR 1.113(c). A request for reconsideration while not provided for in 37 CFR 1.113(c) may be filed after final for consideration. See MPEP §§ 706.07(e) and 714.13.
The USPTO Internet website contains terminal disclaimer forms which may be used. Please visit www.uspto.gov/patent/patents-forms. The actual filing date of the application in which the form is filed determines what form (e.g., PTO/SB/25, PTO/SB/26, PTO/AIA /25, or PTO/AIA /26) should be used. A web-based eTerminal Disclaimer may be filled out completely online using web-screens. An eTerminal Disclaimer that meets all requirements is auto-processed and approved immediately upon submission. For more information about eTerminal Disclaimers, refer to www.uspto.gov/patents/apply/applying-online/eterminal-disclaimer.
Regarding the Examiner elected species of
PNG
media_image2.png
209
558
media_image2.png
Greyscale
Claims 1, 26-27, 29, and 44 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-4, 6-8, 11-13, 23-26, 35, 37-39, and 41-42 of copending Application No. 18/018,241. Although the claims at issue are not identical, they are not patentably distinct from each other because:
Regarding instant claims 1, 26-27, 29, and 44, ‘241 claim 13 taught a ligand drug conjugate comprising an anti-CD79B antibody comprising a VH of HCDR1-3 of SEQ ID NO:24-26 (GSSFTSY.*FPRSGN.*GDLGDFDY) and a VL of LCDR1-3 of SEQ ID NO:27, 11, and 12 (RSSQSIVHSDGNTYFE.* KVSNRFS.* FQGSHVPWT) in copending claim 1, which is identical to the Applicant elected antibody of instant SEQ ID NO:7-9 and instant SEQ ID NO:10-12, wherein in copending claim 13 the formula is Pc-(L-D)k wherein
PNG
media_image15.png
363
624
media_image15.png
Greyscale
wherein R1a is methyl and R1b is H, which is identical to the compound structure of instant claim 1, wherein the ligand conjugate comprises
PNG
media_image16.png
104
342
media_image16.png
Greyscale
with a k of 1-10, R1a is methyl and R1b is hydrogen in copending claim 23,
wherein the ligand conjugate is
PNG
media_image17.png
180
556
media_image17.png
Greyscale
in copending claim 37, which is the Examiner elected species, wherein the ligand drug is present in a pharmaceutical composition further comprising a pharmaceutically acceptable excipient and a therapeutically effective amount in copending claim 39, which is identical to instant claim 44.
This meets the claim limitations of the Examiner elected species present in instant claims 1, 26-27, 29, and 44.
This is a provisional nonstatutory double patenting rejection because the patentably indistinct claims have not in fact been patented.
Response to Arguments
Applicants note that the instant application (filed on January 22, 2021) has an earlier effective filing date than both the '241 application (filed on July 27, 2021) and the '721 application (filed on July 22, 2022).
Applicants argue in view of the arguments and amendments provided above; Applicants believe that the rejections under 35 U.S.C. §103 have been fully overcome. Accordingly, the provisional nonstatutory double patenting rejections are now the only rejections remaining in this application.
As correctly noted by the Examiner in the Office Action, MPEP 804 section I.B.1.b.i provides that: "if a provisional nonstatutory double patenting rejection is the only rejection remaining in an application having the earlier patent term filing date, the examiner should withdraw the rejection in the application having the earlier patent term filing date and permit that application to issue as a patent...".
In response, Applicant's arguments filed 6/29/2026 have been fully considered
but they are not persuasive. According to the MPEP 804 section I.B.1.B.i., if a provisional nonstatutory double patenting rejection is the only rejection remaining in an application having the earlier patent term filing date, the examiner should withdraw the rejection in the application having the earlier patent term filing date and permit that application to issue as a patent, thereby converting the provisional nonstatutory double patenting rejection in the other application into a nonstatutory double patenting rejection upon issuance of the patent. While ‘241 has a later effective filing date compared to the instant application, the provisional nonstatutory double patenting rejection is not only rejection remaining in an application.
Claims 1, 26-27, 29, and 44 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-7, 9-13, 15-20, and 22-24 of copending Application No. 18/290,721 in view of WO 2020156439 (Yang C priority to 01/28/2019 reference of record).
‘721 taught an antibody drug conjugate of Formula I of Ab-(L-D)k
PNG
media_image18.png
281
578
media_image18.png
Greyscale
in copending claim 1, wherein k is between 1 and 10 in copending claim 2, wherein the linker contains cleavable peptides in copending claims 2-3 or other moieties in copending claims 5-7, wherein further spacer units are claimed in copending claims 9-13, wherein further linkers are claimed in copending claims 15-16, wherein the ADC further comprises the structure
PNG
media_image19.png
130
386
media_image19.png
Greyscale
and k is between 1 and 10 in copending claim 17, wherein the ADC is present in a pharmaceutical composition further comprising a pharmaceutically acceptable excipient and a therapeutically effective amount in copending claim 22.
The claims of ‘721 do not teach an antibody if instant SEQ ID NO:7-9 and instant SEQ ID NO:10-12, but this is obvious in view of Yang C.
Yang C taught mAB015 clone 83B2G2 effectively bound CD79b via ELISA (Fig. 7) and FACS (Fig. 8) and comprised a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 (translated page 12, [149]). Yang C taught mAB015 effectively bound CD79b to a level similar to the positive control SN38 which is the FDA approved antibody-conjugated drug polatuzumab vedotin (translated page 13, [0155]). Yang C taught an anti-CD79B antibody or an antibody-drug conjugate and a pharmaceutical composition thereof, and a method using the same for treating or delaying cancer, especially hematopoietic tumors (translated page 2, [0010]), wherein the ADC comprises an antibody covalently coupled to a drug through a linker, wherein the drug is a cytotoxic agent (translated page 5, [0069]-[0070]). Yang taught diffuse large B-cell lymphoma (DLBCL) is a B-cell lymphoma, wherein the B cell receptor (BCR) complex is the most major molecule on the surface of B cells, wherein the BCR complex comprises Igβ (CD79B) heterodimers that transmit antigen stimulation signals (translated page 2, [0006]).
Regarding instant claims 1, 26-27, 29, and 44, it would have been obvious for a person having ordinary skill in the art to take the pharmaceutical composition comprising a pharmaceutically acceptable excipient and ADC of copending claims 1, 17, and 22 – and modify the ADC to:
1) exchange the antibody for mAB015 of Yang C.
This is obvious because: 1) mAB015 effectively binds CD79b, which is expressed on cancer cells, and mAB015 binds CD79b as effectively as the antibody for the FDA approved antibody-conjugated drug polatuzumab vedotin as taught by Yang C.
There is a reasonable expectation of success because: 1) mAB015 effectively binds CD79b, which is expressed on cancer cells, and mAB015 binds CD79b as effectively as the antibody for the FDA approved antibody-conjugated drug polatuzumab vedotin as taught by Yang C.
This meets the claim limitations of the Examiner elected species present in instant claims 1, 26-27, 29, and 44.
This is a provisional nonstatutory double patenting rejection.
Response to Arguments
Applicants note that the instant application (filed on January 22, 2021) has an earlier effective filing date than both the '241 application (filed on July 27, 2021) and the '721 application (filed on July 22, 2022).
Applicants argue in view of the arguments and amendments provided above; Applicants believe that the rejections under 35 U.S.C. §103 have been fully overcome. Accordingly, the provisional nonstatutory double patenting rejections are now the only rejections remaining in this application.
As correctly noted by the Examiner in the Office Action, MPEP 804 section I.B.1.b.i provides that: "if a provisional nonstatutory double patenting rejection is the only rejection remaining in an application having the earlier patent term filing date, the examiner should withdraw the rejection in the application having the earlier patent term filing date and permit that application to issue as a patent...".
In response, Applicant's arguments filed 6/29/2026 have been fully considered
but they are not persuasive. According to the MPEP 804 section I.B.1.B.i., if a provisional nonstatutory double patenting rejection is the only rejection remaining in an application having the earlier patent term filing date, the examiner should withdraw the rejection in the application having the earlier patent term filing date and permit that application to issue as a patent, thereby converting the provisional nonstatutory double patenting rejection in the other application into a nonstatutory double patenting rejection upon issuance of the patent. While ‘721 has a later effective filing date compared to the instant application, the provisional nonstatutory double patenting rejection is not only rejection remaining in an application.
Claims 1, 26-27, 29, and 44 are provisionally rejected on the ground of nonstatutory double patenting as being unpatentable over claims 1-3, 5-7, 9-13, 15-20, and 22-24 of copending Application No. 19/661,397 in view of WO 2020156439 (Yang C priority to 01/28/2019 reference of record).
‘397 taught anti-CD79B conjugates and method of treatment of proliferative disorder of cancer in copending claims 1-4, 6-8, 11-13, 23-26, 35, 37-39, and 41-42.
‘397 taught an antibody-drug conjugate with the structure:
PNG
media_image20.png
193
564
media_image20.png
Greyscale
, wherein Pc is an anti-CD79B antibody comprising a VH of HCDR1-3 of SEQ ID NO:24-26, respectively and a VL of LCDR1-3 of SEQ ID NO:27, 11, and 12, respectively, and wherein n is 1 to 10 in copending claims 1 and 37. ‘397 taught an anti-CD79B for a ligand-drug conjugate comprising a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 in copending claim 4. ‘397 taught a pharmaceutical composition comprising a pharmaceutically acceptable excipient and a therapeutically effective amount of an anti-CD79B drug conjugate in copending claim 39.
‘397 does not describe a single embodiment of the structure of ADC-1 bound to an anti-CD79B with the instantly claimed HCDR1-3 and LCDR1-3 of the elected species, but this is obvious in view of ‘397 teaching an antibody that CD79B and contains the instantly claimed HCDR1-3 and LCDR1-3 of the elected species.
Regarding instant claims 1, 26-27, 29, and 44, it would have been obvious for a person having ordinary skill in the art to combine copending claims 1, 4, 37, and 39 to produce an antibody-drug conjugate with the structure:
PNG
media_image20.png
193
564
media_image20.png
Greyscale
, wherein Pc is an anti-CD79B antibody comprising the VH of SEQ ID NO:3 and the VL of SEQ ID NO:4, wherein n is 1 to 10 in a pharmaceutical composition comprising a pharmaceutically acceptable excipient and a therapeutically effective amount of an anti-CD79B drug conjugate.
This is obvious with a reasonable expectation of success because: 1a) the claimed CD79B antibody comprising a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 is taught to be in an antibody-drug conjugate that targets the same target of CD79B; and 1b) a pharmaceutical composition comprising a pharmaceutically acceptable excipient and the ADC above would allow the pharmaceutical composition to be administered as a treatment.
This would produce a pharmaceutical composition comprising a pharmaceutically acceptable excipient and an ADC comprising ADC-1 as the antibody with a drug conjugate structure of
PNG
media_image14.png
216
627
media_image14.png
Greyscale
, wherein n is about 3, wherein Pc comprises a VH of SEQ ID NO:3 and a VL of SEQ ID NO:4 which comprises a VH comprising instant SEQ ID NO:7-9 and a VL comprising instant SEQ ID NO:10-12, and meets the claim limitations of the Examiner elected species present in instant claims 1, 26-27, 29, and 44.
Conclusion
No claims are allowed.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to JOHN J SKOKO III whose telephone number is (571)272-1107. The examiner can normally be reached M-F 8:30 - 5:00.
Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Julie Z Wu can be reached at (571)272-5205. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/J.J.S./Examiner, Art Unit 1643
/Karen A. Canella/Primary Examiner, Art Unit 1643
Prosecution Insights