DETAILED ACTION
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 .
Application Status
The claims filed June 14, 2023 are acknowledged. Claims 1-20 are pending and under examination herein.
Claim Rejections - 35 USC § 112(d)
The following is a quotation of 35 U.S.C. 112(d):
(d) REFERENCE IN DEPENDENT FORMS.—Subject to subsection (e), a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
The following is a quotation of pre-AIA 35 U.S.C. 112, fourth paragraph:
Subject to the following paragraph [i.e., the fifth paragraph of pre-AIA 35 U.S.C. 112], a claim in dependent form shall contain a reference to a claim previously set forth and then specify a further limitation of the subject matter claimed. A claim in dependent form shall be construed to incorporate by reference all the limitations of the claim to which it refers.
Claim 18 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 18 recites the method of claim 13, which comprised the steps of “obtaining a sample from an individual and determining the level of QSOX1 in the sample using an antibody according to claim 1”, “wherein a level of QSOX1 greater than 5,000 ng/mL correlates with cancer in the subject”. The wherein clause provided in claim 18 does not further limit the method of claim 13 because the claim does not require additional steps to be performed (e.g., a diagnosis of cancer in the subject). Rather, an inherent property (i.e., a correlation between QSOX1 expression and cancer) is stated.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
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 1-5 and 8-20 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.
“[T]he purpose of the written description requirement is to ‘ensure that the scope of the right to exclude, as set forth in the claims, does not overreach the scope of the inventor’s contribution to the field of art as described in the patent specification.’” Ariad Pharm., Inc. v. Eli Lilly & Co., 598 F.3d 1336, 1353-54 (Fed. Cir. 2010) (en banc) (quoting Univ. of Rochester v. G.D. Searle & Co., 358 F.3d 916, 920 (Fed. Cir. 2004)). To satisfy the written description requirement, the specification must describe the claimed invention in sufficient detail that one skilled in the art can reasonably conclude that the inventor had possession of the claimed invention. Vas-Cath, Inc. v. Mahurkar, 935 F.2d 1555, 1562-63, 19 USPQ2d 1111 (Fed. Cir. 1991).
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 it may be satisfied by the 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. “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).
For a claim to a genus, a generic statement that defines a genus of substances by only their functional activity does not provide an adequate written description of the genus. Reagents of the University of California v. Eli Lilly, 43 USPQ2d 1398 (CAFC 1997). “[A] sufficient description of a genus . . . requires the disclosure of either a representative number of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can ‘visualize or recognize’ the members of the genus.” Ariad, 598 F.3d at 1350 (quoting Eli Lilly, 119 F.3d at 1568-69). A “representative number of species” means that those species that are adequately described are representative of the entire genus. AbbVie Deutschland GMBH v. Janssen Biotech, 111 USPQ2d 1780, 1790 (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. For example, the Federal Circuit has found that possession of a mouse antibody heavy and light chain variable regions provides a structural "stepping stone" to the corresponding chimeric antibody, but not to human antibodies. Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1875 (Fed. Cir. 2011).
The claimed invention. The nature and scope of the claimed invention at issue is an anti-QSOX1 antibody comprising three heavy chain variable region (VH) complementarity determining regions (CDRs) and three light chain variable region (VL) CDRs as set forth in claim 1 and its dependent claims 2-5 and 8-20. The antibody recited in claim 1 fails to satisfy the written description requirement in part because the claim sets forth that each of the CDRs can be “mixed and matched” to form at least 64 (2×2×2×2×2×2) possible combinations of antibodies comprising three VH CDRs and three VL CDRs, exclusive of all the additional possible CDR sequences that meet the limitation of “a sequence having at least 87% identity to SEQ ID NO: 1 or SEQ ID NO: 7”, “a sequence having at least 85% identity to SEQ ID NO: 2 or SEQ ID NO: 8”, etc. However, Applicant’s disclosure does not provide a showing that each of these possible combinations of VH and VL CDRs have the ability to bind specifically to QSOX1 as instantly claimed. Furthermore, the claim language reciting “a sequence having at least 87% identity to SEQ ID NO: 1 or SEQ ID NO: 7”, “a sequence having at least 85% identity to SEQ ID NO: 2 or SEQ ID NO: 8”, etc., does not satisfy the written description requirement because these limitations allow for unpredictable variability in the VH CDR1, VH CDR2, VH CDR3, VL CDR1, and/or VL CDR3, which would be expected to impact the specificity of the instantly claimed anti-QSOX1 antibody for its cognate antigen as understood based on the teachings of the prior art. In order to satisfy the written description requirement, the claims must define a complete structure of the antigen-binding domain by sequence (i.e., a complement of three heavy chain CDRs and three light chain CDRs) that has a demonstrated ability to bind specifically to QSOX1 as presently claimed.
Claim 2 requires that the instantly claimed antibody is capable of binding to human QSOX1 with a dissociation constant (KD) less than 10-6 M. However, one of ordinary skill in the art cannot readily predict or visualize which anti-QSOX1 antibodies are capable of binding to human QSOX1 with a dissociation constant (KD) less than 10-6 M without knowing the corresponding structural elements of the antibody that are responsible for conferring this function.
Claims 3-4 recite similar language to claim 1 stating that the instantly claimed antibody may comprise variability within one or more of the CDR sequences. Claim 5 recites that the VH and VL amino acid sequences may be “mixed and matched” and/or that said sequences may comprise “at least 90% identity” to the sequences of SEQ ID NO: 13 or 15 (for the VH) or to SEQ ID NO: 14 or 16 (for the VL), while the CDRs (as set forth in independent claim 1) are not expressly defined. Together, these claims still fail to define a complete structure that would be expected to correlate with the presently claimed function of binding to QSOX1.
Of note, claims 6-7 (which are not included in this rejection) recite an antibody having a completely defined structure (comprising three defined heavy chain CDRs and three defined light chain CDRs) that would be expected to correlate with the instantly claimed function of binding specifically to QSOX1 based on what is understood in the art and in view of Applicant's disclosure.
State of the prior art. It is well established in the art that the formation of an intact antigen-binding site in an antibody usually requires the association of the complete heavy and light chain variable regions of a given antibody, each of which comprises three CDRs (or hypervariable regions) that provide the majority of the contact residues for the binding of the antibody to its target epitope. See Almagro (Frontiers in Immunology (2018) 8: 1751), “The IgG Molecule” (page 3) and Figure 1. Sela-Culang (Frontiers in Immunology (2013) 4: 302) further teaches, “A major focus in analyzing the structural basis for [antigen] recognition has been in identifying the exact boundaries of the CDRs in a given [antibody]. It is a common practice to identify paratopes through the identification of CDRs” (page 3).
Although the prior art teaches some understanding of the structural basis of antigen-antibody recognition, it is aptly noted that the art is characterized by a high level of unpredictability, since the skilled artisan still cannot accurately and reliably predict the consequences of amino acid substitutions, insertions, and deletions in the antigen-binding domains. Ni (The Protein Journal (2024) 43: 683-696) teaches, “Mutations, even one mutation, introduced in the CDRs through [somatic hypermutation] can change the binding properties and repertoire of antibodies. However, how just one-point mutation can dramatically change the recognition profiles of the antibody is still unclear” (Introduction). Furthermore, while affinity maturation techniques can result in differences in the CDRs of the antibody compared to its parental antibody, those techniques involve trial-and-error testing and the changes that maintain or improve affinity are not predictable a priori (Almagro, pages 3 and 6-7).
Gershoni (Biodrugs (2007) 21(3): 145-156) teaches that antibody binding to the same antigen, or even the same epitope on that antigen, can be accomplished with an impressively wide variety of antibody structures, even when the antibodies are limited to those from a particular source (page 146, Section 1.1). The skilled artisan therefore understands that antibodies from a variety of different sources may bind the same antigen and even mediate the same functional effects, but differ widely in the details of the structure of their antigen-binding sites, particularly in the amino acid sequence.
Antibodies that specifically bind to QSOX1, having structurally defined antigen-binding domains comprising a complement of three heavy chain CDRs and three light chain CDRs, have previously been described in the art. See, e.g., Fass (US 2018/0273639 A1; cited in IDS) and Fass (US 2021/0292437 A1).
Scope of species disclosed in original specification. The Examples disclose the complete structures of two antibody clones, “2F1” and “3A10”, for which the amino acid sequences of the corresponding VH and VL domains (and their corresponding CDRs) are summarized in Table 1 (pages 19-20).
Antibody 2F1 has a VH comprising the amino acid sequence of SEQ ID NO: 13 (with three CDRs comprising the amino acid sequences of SEQ ID NO: 1, 2, and 3, respectively) and a VL comprising the amino acid sequence of SEQ ID NO: 14 (with three CDRs comprising the amino acid sequences of SEQ ID NO: 4, 5 (“SAS”), and 6, respectively).
Antibody 3A10 has a VH comprising the amino acid sequence of SEQ ID NO: 15 (with three CDRs comprising the amino acid sequences of SEQ ID NO: 7, 8, and 9, respectively) and a VL comprising the amino acid sequence of SEQ ID NO: 16 (with three CDRs comprising the amino acid sequences of SEQ ID NO: 10, 11 (“WAS”), and 12, respectively).
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. As summarized above, the specification only discloses two antibodies for which the complete structure (comprising three heavy chain CDRs and three light chain CDRs) responsible for its antigen-binding function are defined. These two embodiments cannot be said to be broadly representative of the 64+ possible antibodies encompassed in the scope of the presently claimed invention.
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. As illustrated by the state of the prior art, the corresponding CDR structures (amino acid sequences) in the VH and the VL domains are critical determinants of antigen binding function. Only those antibodies for which these structures have been defined in Applicant's disclosure (i.e., the combinations set forth above for clone 2F1 and 3A10 and summarized in Table 1) satisfy the written description requirement. Applicant's disclosure does not set forth which residue(s) in any of the CDRs can be modified (e.g., substituted or deleted) while retaining the ability of the antibody to specifically bind to QSOX1 as required by the instant claims.
Conclusion. For all of the reasons presented above, one of skill in the art would not know which of the countless other anti-QSOX1 antibodies encompassed by the highly general structural requirements of the claims would also possess the required functional activity. 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, the Applicant did not possess the full genus of anti-QSOX1 antibodies as broadly claimed at the time the application was filed.
Claim Rejections - 35 USC § 101
35 U.S.C. 101 reads as follows:
Whoever invents or discovers any new and useful process, machine, manufacture, or composition of matter, or any new and useful improvement thereof, may obtain a patent therefor, subject to the conditions and requirements of this title.
The 2019 Patent Subject Matter Eligibility Guidance (“Guidance”) provides a means of
determining whether a particular claim is patent eligible under 35 U.S.C. 101. See MPEP 2106.
The Guidance requires an analysis of multiple steps, Steps 1, 2A, and 2B:
Step 1 - Following a determination of the broadest reasonable interpretation of a claim, is the claim drawn to a process, machine, article of manufacture, or composition of matter? If the answer to this inquiry is “Yes,” the analysis moves on to step 2A.
Step 2A - A two-prong analysis. For prong one, does the claim recite an abstract idea, law of nature, or natural phenomenon? If “Yes,” the analysis proceeds to prong two, which asks whether the claim recites additional elements that integrate the judicial exception into a practical application.
Step 2B - Does the claim recite additional elements that amount to significantly more than the judicial exception? If “No,” the claim is not eligible subject matter under 35 U.S.C. 101.
Claim 18 is rejected under 35 U.S.C. 101 because the claimed invention is directed to a judicial exception (i.e., a naturally occurring phenomenon) without significantly more. Laws of nature and natural phenomena, as identified by the courts, include naturally occurring principles/relations and nature-based products that are naturally occurring or that do not have markedly different characteristics compared to what occurs in nature. See MPEP § 2106.04(b).
Claim 18 recites the limitation that “a level of QSOX1 greater than 5,000 ng/mL correlates with cancer in the subject”. This limitation is drawn to a naturally occurring phenomenon as evidenced by Applicant (e.g., Figure 2), and thus the claim is drawn to a judicial exception because this type of correlation is a consequence of natural processes. A claim that focuses on judicial exception(s) can be shown to recite something “significantly more” than the judicial exception(s) by reciting a meaningful limitation beyond the judicial exceptions. However, in the instant case, the claims do not include additional elements that are sufficient to amount to significantly more than the judicial exception because the additional elements are limited to well-understood, routine and conventional activities which are not enough to qualify the claimed method as reciting something “significantly more” than the judicial exceptions. Obtaining a sample to perform a method of detecting protein expression is well-understood, routine and conventional activity for those in the art. Further, the step is recited at a high level of generality such that it amounts to insignificant pre-solution activity, e.g., a mere data gathering step necessary to use the correlation. Claim 18 recites that the determination step of the claimed method is performed using an antibody according to claim 1. However, anti-QSOX1 antibodies meeting the generic structural limitations recited in claim 1 are known in the art. By way of example, consider the “2F1.14” and “3A10.6” antibody clones disclosed by Koelbel (Masters Thesis: “Characterization of Monoclonal Antibodies Against Quiescin Sulfhydryl Oxidase 1”, Arizona State University, Published May 2019), which are shown to bind to rQSOX1 (e.g., Figure 5) and which could be used to detect QSOX1 in biological samples (e.g., Discussion). Thus, the present claim does not recite “significantly more” than the judicial exception because the claim does not recite in this step a meaningful limitation, such as a particular or unconventional antibody, that distinguishes it from well-understood, routine, and conventional data gathering activity engaged in by scientists prior to the filing date of Applicant's invention.
Claim Rejections - 35 USC § 102
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.
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.
Claims 1-8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Koelbel (Masters Thesis: “Characterization of Monoclonal Antibodies Against Quiescin Sulfhydryl Oxidase 1”, Arizona State University, Published May 2019).
Koelbel describes the generation and characterization of monoclonal antibodies against QSOX1. Regarding claims 1 and 3-8, Koelbel illustrates an alignment of high-producing anti-QSOX1 antibody clones “2F1.14” and “3A10.6” against the Fass group’s scFv 492.1 mAb. The antibody clone “2F1.14” comprises a VH having an amino acid sequence that shares 100% sequence identity to instant SEQ ID NO: 13 (with corresponding CDRs having amino acid sequences that share 100% sequence identity to instant SEQ ID NO: 1-3, respectively) and a VL having an amino acid sequence that shares 100% sequence identity to instant SEQ ID NO: 14 (with corresponding CDRs having amino acid sequences that share 100% sequence identity to instant SEQ ID NO: 4-6, respectively) (page 20, Figure 6). The antibody clone “3A10.6” comprises a VH having an amino acid sequence that shares 100% sequence identity to instant SEQ ID NO: 15 (with corresponding CDRs having amino acid sequences that share 100% sequence identity to instant SEQ ID NO: 7-9, respectively) and a VL having an amino acid sequence that shares 100% sequence identity to instant SEQ ID NO: 16 (with corresponding CDRs having amino acid sequences that share 100% sequence identity to instant SEQ ID NO: 10-12, respectively) (pages 20-21, Figure 6).
Regarding claim 2, products of identical composition cannot have mutually exclusive properties. A chemical composition and its properties are inseparable. In re Spada 15 USPQ2d 1655, 1658 (Fed. Cir. 1990). See MPEP § 2112.01. Accordingly, absent a showing otherwise, the 2F1.14 and 3A10.6 clones disclosed by Koelbel would be expected to be capable of binding human QSOX1 with a KD of less than 10-6 M.
Claim Rejections - 35 USC § 103
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.
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.
Claims 1 and 9-20 are rejected under 35 U.S.C. 103 as being unpatentable over Koelbel (Masters Thesis, Arizona State University, Published May 2019; supra) as applied to claims 1-8 above, further in view of Fass (US 2018/0273639 A1; cited in IDS).
The teachings of Koelbel are recited in the 35 U.S.C. § 102 rejection above. Additionally, Koelbel teaches that elevated expression of QSOX1 is observed in the plasma of pancreatic ductal adenocarcinoma (PDA) patients and has also been observed in breast, lung, and kidney cancers, among others (e.g., Abstract). Koelbel further teaches, “QSOX1 expression is associated with cell proliferation and invasion in vitro and tumor growth in vivo. Additionally, the enzymatic activity of QSOX1 in the extracellular matrix (ECM) is important for cell invasion in vitro. Small molecule inhibitors of QSOX1 have been shown to have antitumorigenic properties in vitro and in vivo” (Abstract). Koelbel further provides that the antibody clones 2F1.14 and 3A10.6 suppressed tumor invasion in a 3D invasion model (e.g., Abstract; Results, pages 24-26; Figure 9), relevant to claim 12. Koelbel further sets forth that another use of the antibody’s clones “is detecting QSOX1 in biological samples to investigate QSOX1 as a potential biomarker of cancer or cancer progression” (Discussion, page 30), relevant to claims 13-20.
However, Koelbel does not expressly teach that the 2F1.14 or 3A10.6 antibody clones comprise an Fc portion of a human or humanized antibody. Koelbel also does not expressly teach methods of treating cancer or determining or detecting the level of QSOX in a plasma sample as set forth in claims 12-20.
Fass describes anti-QSOX1 antibodies, as well as pharmaceutical compositions and methods of use thereof (e.g., Abstract; Examples 1, ¶ 0331-0333). In specific embodiments, Fass discloses an antibody “Mab492.1” which binds to human QSOX1 and a modified version (“Mab492gen”) in which point mutations were introduced to render the antibody capable of binding to the mouse QSOX1 ortholog (e.g., ¶ 0079). Relevant to claim 9, Fass teaches that purified Mab492gen comprising human constant regions (Fc) was used for inhibition assays (e.g., ¶ 0313-0314). Relevant to claims 10-11, Fass discloses embodiments in which the antibody of the invention is immobilized to a solid support such as the well of an assay plate or is attached to a detectable moiety in order to enable detection of the antibody (e.g., ¶ 0037-0038, 0274-0284; claims 1 and 8).
Relevant to claim 12, Fass discloses a method of treating a laminin-associated disease or condition (a cancerous tumor) that comprises administering an antibody of the invention to a subject in need thereof (e.g., ¶ 0043-0046, 0203-0216, 0262-0271; claims 1, 10-11, and 14).
Relevant to claims 13-18, Fass discloses methods comprising obtaining a biological sample from an animal (e.g., plasma) and analyzing the sample for QSOX1 levels using an antibody of the invention conjugated to a detectable moiety and/or with detection methods known in the art such as ELISA or enzyme-linked chemiluminescence assay (CLIA) (¶ 0272-0283). (As discussed in the 35 U.S.C. § 112(d) rejection above, claim 18 includes the limitations of the method of claim 13 and does not further limit the claimed method.) Relevant to claims 10 and 19-20, Fass teaches that the antibody of the invention can be used for in vitro or ex vivo applications such as detecting QSOX1 levels in biological samples, wherein the antibody is immobilized on a solid support such as an assay plate well (e.g., ¶ 0283-0287).
In view of the teachings of Fass, it would have been obvious to one of ordinary skill in the art, before the filing date of the instantly claimed invention, to use one or both of the antibody clones disclosed by Koelbel in a method of treating cancer or of determining or detecting the level of QSOX1 in a biological sample. The skilled artisan would have been motivated to administer one or both of antibody clones 2F1.14 and 3A10.6 in a method of treating cancer because Koelbel teaches that these antibodies suppressed tumor invasion in a 3D invasion model. One would further have been motivated to use the antibodies in methods of detecting QSOX1 expression because the antibodies specifically bind to QSOX1, and Koelbel provides that the disclosed antibody clones “can serve as tools in furthering the characterization of QSOX1 and its role in cancer”. There would have been a reasonable expectation of success because those of ordinary skill in the art would recognize that the antibodies disclosed by Koelbel and by Fass are functional equivalents known for the same purpose (i.e., anti-QSOX1 antibodies that inhibit QSOX1 activity) and could be substituted in one method for the other to achieve the same desired outcome.
Conclusion
No claims are allowed.
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/ELIZABETH A SHUPE/Examiner, Art Unit 1643
/Brad Duffy/Primary Examiner, Art Unit 1643