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
2. The election without traverse filed 01/27/2026 in response to the Office Action of 11/28/2025 is acknowledged and has been entered.
Applicant has elected Group I, claims 1-2, 4, 7, 9, 31, 34, 36, 39, 42 and 53, drawn to an isolated anti-Ryk antibody or antibody derivative.
3. Claims 1, 2, 4, 7, 9, 12, 15, 31, 34, 36, 39, 42, 47, 53, 54, 66, 67, 69, 74, 85 and 109 are pending in the application. Claims 12, 15, 47, 54, 66, 67, 69, 74, 85 and 109 have been withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to nonelected inventions, there being no allowable generic or linking claim. Election was made without traverse in the reply filed on 01/27/2026.
Claims 1-2, 4, 7, 9, 31, 34, 36, 39, 42 and 53 are currently under prosecution.
Priority
5. Applicant’s claim under 35 U.S.C. §§ 119(e) and/or 365(c) for benefit of the earlier filing date of applications, is acknowledged.
Drawings
6. The drawing set forth as Figures 1-4 and 7 are objected to because the figures depict amino acid sequences, which are not identified by sequence identification numbers, either in the figure or in the brief description of figures at pages 8-9 of the specification. Sequences appearing in the specification and/or drawings must be identified by a sequence identifier in accordance with 37 C.F.R. 1.821(d); sequence identifiers for sequences appearing in the drawings may appear in the drawings or in the brief description of the drawings.
A replacement drawing sheet, including the correction, is required, if the drawings are objected to. See 37 CFR 1.121(d). However, this ground of objection would be withdrawn, so that a replacement drawing would not be required, if Applicant were to amend the brief description of the figures at pages 8-9 of the specification to include sequence identification numbers.
Appropriate correction is required.
Specification
7. The disclosure is objected to for the following reason: Figures 1-4 and 7 depict an amino acid sequence that is not identified, see, e.g., pages 8-9 of the specification.
Claim Objections
8. Claims 1 and 39 are objected to because claims recite, “WO 2017/172733 A1”. Claims must, under modern claim practice, stand alone to define invention, and incorporation into claims by express reference to specification and/or drawings is not permitted except in very limited circumstances. See Ex parte Fressola, 27 USPQ2d 1608 (BPAI, 1993). See M.P.E.P. § 2173.05(s), which states:
“Where possible, claims are to be complete in themselves. Incorporation by reference to a specific figure or table “is permitted only in exceptional circumstances where there is no practical way to define the invention in words and where it is more concise to incorporate by reference than duplicating a drawing or table into the claim. Incorporation by reference is a necessity doctrine, not for applicant's convenience.” Ex parte Fressola, 27 USPQ2d 1608, 1609 (Bd. Pat. App. & Inter. 1993) (citations omitted).
Appropriate correction is required.
Claim Rejections - 35 USC § 112
9. 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.
10. 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.
11. Claims 1 and 31 are 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 pre-AIA the applicant regards as the invention.
Regarding claims 1 and 31, the phrase "e.g." renders the claim indefinite because it is unclear whether the limitation(s) following the phrase are part of the claimed invention. See MPEP § 2173.05(d).
12. The following is a quotation 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.
13. The following is a quotation of 35 U.S.C. 112 (pre-AIA ), first paragraph:
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.
14. Claims 1-2, 4, 7, 9, 31, 34, 36, 39, 42 and 53 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 claims contain 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 pre-AIA the inventors, at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
1) MPEP § 2163 states that the written description requirement for a claimed genus may be satisfied through sufficient description of a representative number of species by actual reduction to practice, or by disclosure of relevant, identifying characteristics, i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. A “representative number of species” means that the species which are adequately described are representative of the entire genus. See, e.g., AbbVie Deutschland GMBH v. Janssen Biotech, 759 F.3d 1285, 111 USPQ2d 1780 (Fed. Cir. 2014). Thus, when there is substantial variation within the genus, one must describe a sufficient variety of species to reflect the variation within the genus to provide a "representative number” of species. The “structural features common to the members of the genus” needed for one of skill in the art to ‘visualize or recognize’ the members of the genus takes into account the state of the art at the time of the invention. “Functional” terminology may be used “when the art has established a correlation between structure and function” but “merely drawing a fence around the outer limits of a purported genus is not an adequate substitute for describing a variety of materials constituting the genus and showing one has invented a genus and not just a species. Ariad Pharmaceuticals Inc. v. Eli Lilly & Co., 598 F3d 1336, 94 USPQ2d 1161, 1171 (Fed Cir. 2010).
On 22 February 2018, the USPTO provided a Memorandum clarifying the Written Description Guidelines for claims drawn to antibodies, which can be found at www.uspto.gov/sites/default/files/documents/amgen_22feb2018.pdf. That Memorandum indicates that, in compliance with recent legal decisions, the disclosure of a full characterized antigen no longer is sufficient written description of an antibody to that antigen. Accordingly, the instant claims have been re-evaluated in view of that guidance.
Scope of the claimed genus
Claims 1, 31, 34, 36, 39, 42, 53 are drawn to an isolated anti-Ryk antibody binds to SEQ ID NO: 19, 24, or 25.
State of the Relevant Art
SEQ ID NO: 19, 24, or 25 is a fragment of receptor tyrosine kinase-related protein (ryk), it is known in the art; see below sequence alignment 1.
As was well-known in the antibody art, antibodies as a class share an overall structure generally comprising two heavy chain polypeptides that each comprises a heavy chain variable region (VH) and a heavy chain constant region made up of several domain (CH1, hinge, CH2, CH3, and for some antibodies, a CH4). Each of the heavy chains pairs with a light chain polypeptide that comprises a light chain variable region (VL) and a constant region. But while this overall structure is shared amongst antibodies from a wide variety of sources (human, rat, mouse, rabbit), the structure each antibody uses to bind its particular epitope on an antigen is structurally distinct and is formed by a recombination event that results in high variability at the amino acid sequence level. By the time the invention was made, it is well established in the art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). Chimeric antibodies comprise the heavy and light chain variable regions of a rodent antibody linked to human constant regions and preserve the entirety of the VH and VL of the parent antibody. Id. at 1619-20. Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4. Almagro provides a detailed discussion regarding various methods of humanization, including rationale design approaches and empirical approaches based on random screening. Almagro, Sections 4 and 5.
Examples of antigen binding domains comprising only a VH (or less commonly, a VL) that in turn comprise only three CDRs certainly do exist in the literature, but those antibodies generally comprise unique structures such as CDR1 and CDR3’s that are elongated in length and that are often disulfide linked. E.g., De Genst et al., Dev Comp Immunol 2006; 30:187-98. “Shuffling” of the VL (or less commonly the VH) had also been used to improve affinity of a parent antibody in certain instances. But the procedure generally required a "dominant" VH (i.e., a VH that is primarily responsible for antigen specificity). E.g., Yoshinaga et al., J. Biochem 2008; 143: 593-601.
Overall, at the time the invention was made, the level of skill for preparing antibodies and then selecting those antibodies with desired functional properties was high. However, even if a selection procedure was, at the time of the invention, sufficient to enable the skilled artisan to identify antibodies with the recited functional properties, the written description provision of 35 U.S.C § 112 is severable from its enablement provision. Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011) (“The fact that a fully-human antibody could be made does not suffice to show that the inventors of the '775 patent possessed such an antibody.”) Absent the conserved structure provided by all six CDRs of a parental antibody in the context of appropriate VH and VL framework sequences, the skilled artisan generally would not be able to visualize or otherwise predict, a priori, what an antibody with a particular set of functional properties would look like structurally.
Summary of Species disclosed in the original specification
Although the specification teaches SEQ ID NO: 19, 24, or 25 (see [0030-0031] and [0183] of the published application); however, the specification does not provide a representative number of species to which the claimed a genus of antibodies that specifically binds to the SEQ ID NO: 19, 24, or 25.
Are the disclosed species representative of the claimed genus?
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.
However, the specification does not provide a representative number of species to which the claimed a genus of antibodies that specifically binds to the SEQ ID NO: 19, 24, or 25.
Identifying characteristics and structure/function correlation
In the absence of a representative number of species, the written description requirement for a claimed genus may be satisfied by disclosure of relevant, identifying characteristics; i.e., structure or other physical and/or chemical properties, by functional characteristics coupled with a known or disclosed correlation between function and structure, or by a combination of such identifying characteristics, sufficient to show the applicant was in possession of the claimed genus. To meet this requirement in the instant case, the specification must describe structural features that convey the claimed binding activity, a prerequisite for utility in the recited composition.
As noted above, the art generally accepted that the combination of the CDRs within the VH and VL pair of an antibody were essential for binding specificity. But the specification does not describe what residues within the CDRs confer the binding activity claimed. Accordingly, the skilled artisan would not be able to discern a structure/function correlation for antibodies other than those comprising either all six CDRs (in the context of VH and VL regions) of one parental antibody, or the VH and VL of one parental antibody.
Further, the specification does not show that either the VH or the VL is “dominant” and could be paired with other VH or VL to form a new antibody that still bound the same antigen. It is again acknowledged that the skilled artisan possessed the methodology needed to “shuffle” the VL and/or VH and screen for binders. But that methodology did not allow the skilled artisan to visualize the structure of the alternate VH/VL chains prior to the step of screening. Accordingly, absent supporting evidence of a “dominant” VH or VL, the recitation of only a VH or only a VL does not provide a structure that the skilled artisan would consider to correlate with binding function.
For all of the reasons presented above, one of skill in the art would not know which of the countless other antibodies that meet the highly general structural requirements of the claims would also be able to specifically bind the SEQ ID NO: 19, 24, or 25. And none of the dependent claims provide sufficient additional structure or a structure/function correlation to provide an adequate written description of the genera claimed. Therefore, the skilled artisan would not reasonably conclude that the inventors, at the time the application was filed, had full possession of antibodies as broadly claimed. Given the lack of shared structural properties that provide the claimed binding activity, the limited number of species described, and the fact that the species that were described cannot be considered representative of the broad genus, Applicant was not in possession of the invention as claimed.
2) Turning to a new issue, claims 1-2 and 4 are directed to a genus of anti-Ryk antibodies which only comprises one CDR.
Although the specification teaches Ab5.5 which comprises six CDRs (see Figures 1-2); however, the specification does not teach that the claimed genus of anti-Ryk antibodies only comprises one CDR would have or retain the activity or function of the antibody.
It is well established in the antibody art that the formation of an intact antigen-binding site in an antibody usually required the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three “complementarity determining regions” (“CDRs”) which provide the majority of the contact residues for the binding of the antibody to its target epitope. E.g., Almagro & Fransson, Frontiers in Bioscience 2008; 13:1619-33 (see Section 3 “Antibody Structure and the Antigen Binding Site” and Figure 1). Chimeric antibodies comprise the heavy and light chain variable regions of a rodent antibody linked to human constant regions and preserve the entirety of the VH and VL of the parent antibody. Id. at 1619-20. Humanized antibodies comprise only the CDRs, or in some cases an abbreviated subset of residues within the CDRs, of a parental rodent antibody in the context of human framework sequences. Id. at Section 4. All of the CDRs of the heavy and light chain, in their proper order of CDR1, then 2, then 3, and in the context of framework sequences which maintain their required conformation are generally required to produce a humanized antibody in which the heavy and light chains associate to form an antigen-binding region that binds the same antigen as the parental rodent antibody. Id. at Section 4. Almagro provides a detailed discussion regarding various methods of humanization, including rationale design approaches and empirical approaches based on random screening. Almagro, Sections 4 and 5.
Given the teachings of the antibody art and the specification, the skilled artisan would not be able to predict that the claimed anti-Ryk antibody which only comprises one CDR would have or retain the activity or function of the antibody.
3) Turning to another issue, the claims 1-2, 4, 7, 9, 31, 34, 36, 39, 42 and 53 is drawn to an anti-Ryk antibody or antibody derivative comprising VL or VH have at least 85% sequence identity to the sequence of SEQ ID NOs: 11-18.
Thus, the claim is drawn to a genus of antibodies or antibody derivative comprise an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18.
Although the specification teaches SEQ ID NOs: 11-18 (see page 27 of the published application); however, the specification does not teach that an anti-Ryk antibody or antibody derivative comprises an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18 would have or retain the activity or function of SEQ ID NOs: 11-18.
Given the fact that the claims are drawn to a genus of antibodies or antibody derivative comprise an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18, which have no particular function or activity, there is no correlation between any one particularly identifying structural feature and any one particularly identifying functional feature. Consequently, it is submitted that the skilled artisan could not immediately envision, recognize or distinguish at least a substantial number of the genus of antibodies or antibody derivative comprise an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18 to which the claim is directed.
Although the specification teaches SEQ ID NOs: 11-18, the SEQ ID NOs are not reasonably representative of the genus of antibodies or antibody derivative comprise an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18. This is largely because each amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18 has substantially varying structure and need not have any particular function or activity.
Guidelines states, “[p]ossession may be shown in a variety of ways including description of an actual reduction to practice, or by showing the invention was ‘ready for patenting’ such as by disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention” (Id. at 1104). “Guidelines” further states, “[f]or inventions in an unpredictable art, adequate written description of a genus which embraces widely variant species cannot be achieved by disclosing only one species within the genus” (Id. at 1106); accordingly, it follows that an adequate written description of a genus cannot be achieved in the absence of a disclosure of at least one species within the genus. Moreover, because the claim encompass a genus of antibodies or antibody derivative comprise an amino acid sequence that has at least 85% identical to SEQ ID NOs: 11-18, which vary both structurally and functionally, an adequate written description of the claimed invention must include sufficient description of at least a representative number of species by actual reduction to practice, reduction to drawings, or by disclosure of relevant, identifying characteristics sufficient to show that Applicant was in possession of the claimed genus. In this instance, factual evidence of an actual reduction to practice has not been disclosed by Applicant in the specification; Applicant has not shown the invention was “ready for patenting” by disclosure of drawings or structural chemical formulas that show that the invention was complete; and Applicant has not described distinguishing identifying characteristics sufficient to show that Applicant was in possession of the claimed invention at the time the application was filed.
Thus, it is submitted that the instant claims, and the disclosure describing the claimed subject matter, fails to satisfy the written description requirement set forth under 35 U.S.C. § 112, first paragraph.
15. 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 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.
Claim Rejections - 35 USC § 102
16. The following is a quotation of the appropriate paragraphs of 35 U.S.C. 102 that form the basis for the rejections under this section made in this Office action:
A person shall be entitled to a patent unless –
(a)(1) the claimed invention was patented, described in a printed publication, or in public use, on sale or otherwise available to the public before the effective filing date of the claimed invention.
17. Claims 1, 31, 34, 36, 39, 42 and 53 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Macheda et al (US 20160053022, published on 02/25/2016, IDS).
Claims 1, 31, 34, 36, 39, 42 and 53 are herein drawn to an isolated anti-Ryk antibody specifically binds to an epitope within a region of the ectodomain of Ryk, amino-acids 26-227 of human Ryk (SEQ ID NO:25).
Macheda et al teach an antibody or antigen-binding fragment thereof, binds specifically to the WIF domain of human RYK (SEQ ID NO: 44); see entire document, e.g., abstract, [0009], claims 1-13, pages 45-47.
SEQ ID NO: 44 of Macheda et al is 100% identical with the instant claimed SEQ ID NO: 25; see below sequences alignment 2.
For claim 31, Macheda et al teach that the antibody is a humanized monoclonal antibody; see claim 12.
For claim 34, Macheda et al teach that the anti-RYK antibody inhibit the binding of Wnt5a; see abstract, [0011].
For claim 36, the anti-RYK antibody of Macheda et al binds to SEQ ID NO: 44, which comprising the instant claimed SEQ ID NO: 19; see below sequences alignment 3.
For claim 39, Macheda et al teach poor immunogenicity of the anti-RYK antibody; see [0008].
For claim 42, Macheda et al teach that KD of the anti-RYK antibody is less than 10−8 M; see claim 7.
For claim 53, Macheda et al teach that the anti-RYK antibody can be used to modulate the interaction of Wnts with RYK; see abstract.
18. Claims 1 and 9 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Zou et al. (US 20190119386, published on 04/25/2019).
Claims 1 and 9 are herein drawn to an anti-RYK antibody comprises a heavy chain variable region comprising at least about 85% sequence identity to SEQ ID NO:14.
Zou et al. teach anti-Ryk antibody has a heavy chain variable region with the amino acid sequence set forth in SEQ ID NO: 8; see entire document, e.g., [0144].
The SEQ ID NO: 8 of Zou et al. is 91.3% identical with the instant claimed SEQ ID NO:14; see below sequence alignment 4.
Conclusion
19. No claim is allowed.
20. Any inquiry concerning this communication or earlier communications from the examiner should be directed to YAN XIAO whose telephone number is (571)270-3578. The examiner can normally be reached M-F 8-5 EST.
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If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Samira Jean-Louis can be reached on 571-270-3503. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
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/YAN XIAO/Primary Examiner, Art Unit 1642
Sequence alignment 1
receptor tyrosine kinase-related protein - mouse
C;Species: Mus musculus (house mouse)
C;Date: 26-Jul-1996 #sequence_revision 26-Jul-1996 #text_change 05-Oct-2004
C;Accession: I56248; I52575
R;Simoneaux, D.K.; Fletcher, F.A.; Jurecic, R.; Shilling, H.G.; Van, N.T.; Patel, P.; Belmont, J.W.
J. Immunol. 154, 1157-1166, 1995
A;Title: The receptor tyrosine kinase-related gene (ryk) demonstrates lineage and stage-specific expression in hematopoietic cells.
A;Reference number: I56248; MUID:95123066; PMID:7822791
A;Accession: I56248
A;Status: preliminary; translated from GB/EMBL/DDBJ
A;Molecule type: mRNA
A;Residues: 1-594 <RES>
A;Cross-references: UNIPROT:Q01887; UNIPARC:UPI0000029464; GB:L38394; NID:g598328; PIDN:AAA67060.1; PID:g598329
R;Yee, K.; Bishop, T.R.; Mather, C.; Zon, L.I.
Blood 82, 1335-1343, 1993
A;Title: Isolation of a novel receptor tyrosine kinase cDNA expressed by developing erythroid progenitors.
A;Reference number: I52575; MUID:93357492; PMID:8394755
A;Accession: I52575
A;Status: preliminary; translated from GB/EMBL/DDBJ
A;Molecule type: mRNA
A;Residues: 1-19,21-315,'GSH' <RE2>
A;Cross-references: UNIPARC:UPI0000044DC1; GB:L21707; NID:g309443; PIDN:AAA02913.1; PID:g309444
C;Genetics:
A;Gene: ryk; MRK
F;315-590/Domain: protein kinase homology <KIN>
Query Match 100.0%; Score 3068; Length 594;
Best Local Similarity 100.0%;
Matches 594; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 MRAGRGGVPGSGGLRAPPPPLLLLLLAMLPAAAPRSPALAAAPAGPSVSLYLSEDEVRRL 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MRAGRGGVPGSGGLRAPPPPLLLLLLAMLPAAAPRSPALAAAPAGPSVSLYLSEDEVRRL 60
Qy 61 LGLDAELYYVRNDLISHYALSFNLLVPSETNFLHFTWHAKSKVEYKLGFQVDNFVAMGMP 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 LGLDAELYYVRNDLISHYALSFNLLVPSETNFLHFTWHAKSKVEYKLGFQVDNFVAMGMP 120
Qy 121 QVNISAQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSSKNFTVLNFKRRKMCYK 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 QVNISAQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSSKNFTVLNFKRRKMCYK 180
Qy 181 KLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMK 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 KLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVIFLVAIILAVLHLHSMK 240
Qy 241 RIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSSSGYPTLRIEKNDLRSVTL 300
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 RIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSSSGYPTLRIEKNDLRSVTL 300
Qy 301 LEAKAKVKDIAISRERITLKDVLQEGTFGRIFHGILVDEKDPNKEKQTFVKTVKDQASEV 360
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 LEAKAKVKDIAISRERITLKDVLQEGTFGRIFHGILVDEKDPNKEKQTFVKTVKDQASEV 360
Qy 361 QVTMMLTESCKLRGLHHRNLLPITHVCIEEGEKPMVVLPYMNWGNLKLFLRQCKLVEANN 420
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 QVTMMLTESCKLRGLHHRNLLPITHVCIEEGEKPMVVLPYMNWGNLKLFLRQCKLVEANN 420
Qy 421 PQAISQQDLVHMAIQIACGMSYLARREVIHRDLAARNCVIDDTLQVKITDNALSRDLFPM 480
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 PQAISQQDLVHMAIQIACGMSYLARREVIHRDLAARNCVIDDTLQVKITDNALSRDLFPM 480
Qy 481 DYHCLGDNENRPVRWMALESLVNNEFSSASDVWAFGVTLWELMTLGQTPYVDIDPFEMAA 540
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 DYHCLGDNENRPVRWMALESLVNNEFSSASDVWAFGVTLWELMTLGQTPYVDIDPFEMAA 540
Qy 541 YLKDGYRIAQPINCPDELFAVMACCWALDPEERPKFQQLVQCLTEFHAALGAYV 594
||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 YLKDGYRIAQPINCPDELFAVMACCWALDPEERPKFQQLVQCLTEFHAALGAYV 594
Sequence alignment 2
US-14-781-195-42
Filing date in PALM: 2015-09-29
Sequence 42, US/14781195
Publication No. US20160053022A1
GENERAL INFORMATION
APPLICANT: Peter MacCallum Cancer Institute
APPLICANT: Macheda, Maria Luisa
APPLICANT: Halford, Michael Maurice
APPLICANT: Stacker, Steven
APPLICANT: Parish, Clare Louise
APPLICANT: Nice, Edouard Collins
TITLE OF INVENTION: ANTIBODIES AGAINST HUMAN RYK AND USES THEREFOR
FILE REFERENCE: 951579
CURRENT APPLICATION NUMBER: US/14/781,195
CURRENT FILING DATE: 2015-09-29
PRIOR APPLICATION NUMBER: AU 2013901150
PRIOR FILING DATE: 2013-04-03
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 42
LENGTH: 610
TYPE: PRT
ORGANISM: Homo sapiens
Query Match 99.6%; Score 3127.5; Length 610;
Best Local Similarity 99.5%;
Matches 607; Conservative 0; Mismatches 0; Indels 3; Gaps 1;
Qy 1 MRGAARLGRPGRSCLPGARGLRAPPPPPLLLLLALLPLLPAPGAAAAPAPRPPELQSASA 60
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 1 MRGAARLGRPGRSCLPGARGLRAPPPPPLLLLLALLPLLPAPGAAAAPAPRPPELQSASA 60
Qy 61 GPSVSLYLSEDEVRRLIGLDAELYYVRNDLISHYALSFSLLVPSETNFLHFTWHAKSKVE 120
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 61 GPSVSLYLSEDEVRRLIGLDAELYYVRNDLISHYALSFSLLVPSETNFLHFTWHAKSKVE 120
Qy 121 YKLGFQVDNVLAMDMPQVNISVQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSS 180
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 121 YKLGFQVDNVLAMDMPQVNISVQGEVPRTLSVFRVELSCTGKVDSEVMILMQLNLTVNSS 180
Qy 181 KNFTVLNFKRRKMCYKKLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVI 240
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 181 KNFTVLNFKRRKMCYKKLEEVKTSALDKNTSRTIYDPVHAAPTTSTRVFYISVGVCCAVI 240
Qy 241 FLVAIILAVLHLHSMKRIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITS--- 297
|||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 241 FLVAIILAVLHLHSMKRIELDDSISASSSSQGLSQPSTQTTQYLRADTPNNATPITSSLG 300
Qy 298 YPTLRIEKNDLRSVTLLEAKGKVKDIAISRERITLKDVLQEGTFGRIFHGILIDEKDPNK 357
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 301 YPTLRIEKNDLRSVTLLEAKGKVKDIAISRERITLKDVLQEGTFGRIFHGILIDEKDPNK 360
Qy 358 EKQAFVKTVKDQASEIQVTMMLTESCKLRGLHHRNLLPITHVCIEEGEKPMVILPYMNWG 417
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 361 EKQAFVKTVKDQASEIQVTMMLTESCKLRGLHHRNLLPITHVCIEEGEKPMVILPYMNWG 420
Qy 418 NLKLFLRQCKLVEANNPQAISQQDLVHMAIQIACGMSYLARREVIHKDLAARNCVIDDTL 477
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 421 NLKLFLRQCKLVEANNPQAISQQDLVHMAIQIACGMSYLARREVIHKDLAARNCVIDDTL 480
Qy 478 QVKITDNALSRDLFPMDYHCLGDNENRPVRWMALESLVNNEFSSASDVWAFGVTLWELMT 537
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 481 QVKITDNALSRDLFPMDYHCLGDNENRPVRWMALESLVNNEFSSASDVWAFGVTLWELMT 540
Qy 538 LGQTPYVDIDPFEMAAYLKDGYRIAQPINCPDELFAVMACCWALDPEERPKFQQLVQCLT 597
||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Db 541 LGQTPYVDIDPFEMAAYLKDGYRIAQPINCPDELFAVMACCWALDPEERPKFQQLVQCLT 600
Qy 598 EFHAALGAYV 607
||||||||||
Db 601 EFHAALGAYV 610
Sequence alignment 3
US-14-781-195-44
Filing date in PALM: 2015-09-29
Sequence 44, US/14781195
Publication No. US20160053022A1
GENERAL INFORMATION
APPLICANT: Peter MacCallum Cancer Institute
APPLICANT: Macheda, Maria Luisa
APPLICANT: Halford, Michael Maurice
APPLICANT: Stacker, Steven
APPLICANT: Parish, Clare Louise
APPLICANT: Nice, Edouard Collins
TITLE OF INVENTION: ANTIBODIES AGAINST HUMAN RYK AND USES THEREFOR
FILE REFERENCE: 951579
CURRENT APPLICATION NUMBER: US/14/781,195
CURRENT FILING DATE: 2015-09-29
PRIOR APPLICATION NUMBER: AU 2013901150
PRIOR FILING DATE: 2013-04-03
NUMBER OF SEQ ID NOS: 46
SEQ ID NO 44
LENGTH: 607
TYPE: PRT
ORGANISM: Homo sapiens
Query Match 100.0%; Score 42; Length 607;
Best Local Similarity 100.0%;
Matches 8; Conservative 0; Mismatches 0; Indels 0; Gaps 0;
Qy 1 SRTIYDPV 8
||||||||
Db 211 SRTIYDPV 218
Sequence alignment 4
US-16-086-958-8
(NOTE: this sequence has 1 duplicate in the database searched.
See complete list at the end of this report)
Sequence 8, US/16086958
Publication No. US20190119386A1
GENERAL INFORMATION
APPLICANT: THE REGENTS OF THE UNIVERSITY OF CALIFORNIA
TITLE OF INVENTION: ANTI-RYK ANTIBODIES AND METHODS OF USING THE SAME
FILE REFERENCE: 20378-201389
CURRENT APPLICATION NUMBER: US/16/086,958
CURRENT FILING DATE: 2018-09-20
PRIOR APPLICATION NUMBER: 62/314,025
PRIOR FILING DATE: 2016-03-28
NUMBER OF SEQ ID NOS: 13
SEQ ID NO 8
LENGTH: 440
TYPE: PRT
ORGANISM: Artificial Sequence
FEATURE:
OTHER INFORMATION: Description of Artificial Sequence: Synthetic
polypeptide
Query Match 91.3%; Score 569; Length 440;
Best Local Similarity 89.7%;
Matches 104; Conservative 7; Mismatches 5; Indels 0; Gaps 0;
Qy 1 EVQLVESGGGLVQPGGSLRLSCAASGFTFSSYTMSWIRQAPGKGLEWVAYISNGGGGTYY 60
||:|||||| ||||||||:|||||||||||||||||||| | | ||||||||||||||||
Db 1 EVKLVESGGDLVQPGGSLKLSCAASGFTFSSYTMSWIRQTPEKRLEWVAYISNGGGGTYY 60
Qy 61 PDSVKGRFTISRDNAKNTLYLQMNSLRAEDTAVYYCTRHGDNGDYWGHGSLVTVSS 116
||:|||||||||||||||||||||||::||||:||||||||||||||||| :||||
Db 61 PDTVKGRFTISRDNAKNTLYLQMNSLKSEDTAMYYCTRHGDNGDYWGHGSTLTVSS 116
Prosecution Insights