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 .
The Group and/or Art Unit of your application has changed. To aid in correlating any papers for this application, all further correspondence regarding this application should be directed to Group Art Unit 1671, Examiner Foley.
Applicant’s amendments to the claims have overcome the claim objections and rejections under 35 USC § 112(b).
An updated search identified pertinent prior art. Prosecution is reopened.
Specification
The use of the terms “TWEEN-20” and “TRITON-100”, which are a trade name or a mark used in commerce, has been noted in this application. The term should be accompanied by the generic terminology; furthermore the term should be capitalized wherever it appears or, where appropriate, include a proper symbol indicating use in commerce such as ™, SM , or ® following the term.
Although the use of trade names and marks used in commerce (i.e., trademarks, service marks, certification marks, and collective marks) are permissible in patent applications, the proprietary nature of the marks should be respected and every effort made to prevent their use in any manner which might adversely affect their validity as commercial marks.
It is noted that two copies of the specification have been filed with the amendment on November 27, 2024. At the top of page 8 of applicant’s remarks, applicant states that trademark names have been properly annotated, i.e. "Tween® 20 (polyethylene glycol sorbitan monolaurate)" and “TRITONX®l00 (2-[4-(2,4,4- trimethylpentan-2-yl) phenoxy] ethanol)” in the amended specification. However, neither specification received reflects these changes. A substitute specification excluding the claims is required pursuant to 37 CFR 1.125(a) because the proprietary nature of the trademarks, Tween® 20 and TRITONX® l00, should be valued by proper annotation.
The disclosure is objected to because of the following informalities: antibody identification is not consistent in paragraphs [0084, 0086, 0087, 0093, and 0095]. For example, paragraph [0086] of the instant published disclosure, USPgPub 2022/0252614, refers to antibody “140-1”, which does not appear in the table presented under paragraph [0084]; antibody “6F-76” listed under paragraph [0087] may be intended to be listed as “6F-78” under paragraph [0084] or vice versa; and antibody “14C-TT” recited in the table under paragraph [0093] is probably intended to be, “14C-77”, as recited in paragraph [0084] and in the table under paragraph [0095]. Applicant is requested to review the instant disclosure for any other discrepancies not identified herein and correct them accordingly. Appropriate correction is required.
A substitute specification must not contain new matter. The substitute specification must be submitted with markings showing all the changes relative to the immediate prior version of the specification of record. The text of any added subject matter must be shown by underlining the added text. The text of any deleted matter must be shown by strike-through except that double brackets placed before and after the deleted characters may be used to show deletion of five or fewer consecutive characters. The text of any deleted subject matter must be shown by being placed within double brackets if strike-through cannot be easily perceived. An accompanying clean version (without markings) and a statement that the substitute specification contains no new matter must also be supplied. Numbering the paragraphs of the specification of record is not considered a change that must be shown.
Claim Objections
In claim 18, the primary and/ or secondary antigen list is separated by commas or semicolons. Applicant should choose a single punctuation mark to separate the antigens for consistency.
Claim 21 recites the limitation "the hepatitis C virus" in line 1. There is insufficient antecedent basis for this limitation in the claim. It is presumed that the "the hepatitis C virus" is intended to further limit the “pathological” material recited in claim 10, from which claim 21 depends. An appropriate amendment correlating "the hepatitis C virus" with the “pathological” material recited in claim 10 would ameliorate this issue.
Claim Rejections - 35 USC § 112
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.
Claims 9, 18, and 20 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 applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 20 and line 3 of claim 9 require that the lysis solution contains a “protective protein”. A definition or genus describing these terms is not provided in the instant disclosure and it is not clear what protein material is intended to be claimed. Paragraph [0116] of the instant published disclosure characterizes (bovine serum albumin) “BSA” as a protective protein. Applicant is encouraged to exchange “protective protein” with “bovine serum albumin, BSA”, or language similar to this to overcome this rejection.
Lines 4-5 of claim 18 recites:
“a 7th-21st amino acid sequence and 29th-48th amino acid sequence from the hepatitis C virus core antigen;”
It is not clear whether the two antigen regions recited in lines 4-5 are intended to be a single antigen comprising two regions, or, if the two amino acid regions recited are intended to be separate antigens listed since all of the other antigen amino acid regions listed are separated by a comma or a semicolon. In the interest of compact prosecution, the antigens recited have been interpreted to mean two separate regions.
Claim Rejections - 35 USC § 112
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 1-11, 16-18, and 20-23 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. This is a written description rejection.
The instant claims require a primary antibody directed against an epitope in a 95th-117th amino acid sequence of the hepatitis C virus core antigen (HCVcAg) and a secondary antibody a directed against an epitope in a 55th-72nd amino acid sequence of the HCVcAg. The instant disclosure does not adequately describe the antibodies claimed. Example 2 of the instant published disclosure, USPgPub 2022/0252614, describe fusion protein C175-A and non-fusion protein C175-B as possessing reactivity to HCV+ serum in paragraph [0064], but because C175-B is more reactive, it is used to immunize to mice and prepare a hybridoma. Paragraphs [0081-0084] describe epitope mapping of the monoclonal antibodies (Mabs) and core antigen binding regions. Paragraphs [0086-0096] describe screening antibody pairs to identify highly sensitive and compatible Mab combination: 11C-13 paired with 14C-77, characterized as “superior…in sensitivity and specificity” in paragraph [0096].
The instant claims require a primary antibody directed against an epitope in residues 95-117 and a secondary antibody directed against an epitope in residues 55-72 of the HCV core antigen used to detect HCV in a subject’s sample. However, the instant specification only teaches one pair of antibodies: 11C-13 that binds to HCV core epitope residues 95-117 paired with 14C-77 that binds to HCV core epitope residues 55-72 that have the maximum detection rate and requisite sensitivity and specificity to detect HCV in a subject’s sample. The specification does not describe the genus of antibodies that are directed against an epitope in residues 95-117 and a secondary antibody directed against an epitope in residues 55-72 of the HCV core antigen.
As taught in Greenspan et al (Nature Biotechnology. 1999; 17:936-937) defining epitopes is not as easy as it seems (page 937). Epitopes have been defined in terms of the spacial organization of residues that make contact with a ligand and the structural characterization of the molecular interface for the binding of the molecules to define the epitope boundaries (page 937 middle of page). The epitope defined in this manner will likely include residues that contact the ligand but are energetically neutral or even destabilizing to binding. “In addition, a priori it will not include any residue that makes no contact with a ligand but whose substitution may profoundly affect ligand recognition through influence on the stability of the free form of the macromolecule, or participation in long-range allosteric effects”. “Even when the residues making contacts with ligands are known with certainty, say from the crystal structure of the complex, the question remains with regard to the energetic involvement of each residue (page 936 right column, first paragraph). Therefore, “amino acids should be recognized to have multiple ways of contributing to a noncovalent interaction” (page 937, middle of page). While the instant disclosure lists several Mabs that bind to residues 95-117 and 55-72 of HCVcAg in the table under paragraph [0084], it is not evident that the antibodies do in fact bind the same epitope. As evidenced by Greenspan et al a number of factors not primarily related to the contours of the contacts of the molecules contribute to the free energy change, sometimes profoundly.
While one may be able to assay whether an antibody “competes” with the recited monoclonal antibody, it is apparent that the degree to which an antibody competes with another antibody is a relative or subjective expression, and the requisite degree to which the claimed antibody competes with a monoclonal antibodies cannot be ascertained from the disclosure.
Contrary to the assertion in the specification that such a binding assay determines whether two antibodies bind to the same antigenic determinant (i.e., epitope), competing antibodies do not necessarily bind the same epitopes. For example, “competing” antibodies may bind spatially overlapping but discrete epitopes. Simply because two antibodies cannot simultaneously occupy the same space, such an antibody, once bound to the antigen, sterically hinders or blocks binding of another such antibody. As another example, a “competing” antibody might not necessarily bind to the same epitope of an antigen as another antibody, if one of the antibodies induces conformational shifts in the three-dimensional structure of the antigen upon binding, which prevents binding of the other antibody to the antigen because the epitope to which it would otherwise bind is unrecognizable as a consequence of the structural change.
In addition, it is recognized that the degree of binding of an antibody, which is observed in a competitive binding assay, will depend upon the concentration of the detectably labeled antibody and the unlabeled competing antibody. Typically, the higher the concentration of the unlabeled competitor, the lower the percentage of binding of the labeled antibody. So, at high concentrations, any antibody might be deemed capable of “competing” for binding to an antigen with any other antibody, regardless of whether or not the different antibodies bind to the same, or even overlapping epitopes.
George et al. (Circulation. 1998; 97: 900-906) describe different antibodies, which do not bind to the same epitope of an antigen, but are nevertheless capable of competing with one another for binding to the antigen; see entire document (e.g., page 903, paragraph bridging columns 1 and 2). More particularly, George et al. describes three antibodies, which bind decidedly different, non-cross-reactive epitopes on 2GPI; yet, George et al. teaches each is able to “compete” by a measurable extent with any of the others for binding to the antigen (page 903, paragraph bridging columns 1 and 2). George et al. teaches monoclonal antibody ILA-4 competed with itself for binding to the antigen (% inhibition = 90 ± 11%), but George et al. discloses, despite its binding a non-overlapping epitope, monoclonal antibody ILA-1 also “competed”, with monoclonal antibody ILA-4 for binding to the antigen (% inhibition = 9 ± 4%). Accordingly, George et al. illustrates the capricious and arbitrary nature of determinations that different antibodies bind to the same or different epitopes, which are based upon the results of competitive binding assays, such as the assay exemplified in the specification.
The Court has indicated in Amgen Inc vs Sanofi ( 2017-1480, Fed Cir, 2017) that the disclosure of a well characterized antigen is insufficient for an adequate written description of the antibody that binds the antigen. The Court stated that “an adequate written description must contain enough information about the actual makeup of the claim products – a precise definition such as by structure, formula, chemical name, physical properties, or other properties, of species falling within the genus sufficient to distinguish the genus from other material,” which may be present in “function “terminology “when the art has established a correlation between structure and function” (page 17, 1st paragraph). The Court went on to indicate that knowledge of the chemical structure of an antigen does not tell you anything about the structure of the antibody (Id).
The guidelines for the Examination of Patent Applications Under the 35 U.S.C. 112, § (a) "Written Description" Requirement make clear that if a claimed genus does not show actual reduction to practice for a representative number of species, then the Requirement may be alternatively met by reduction to drawings, 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 genus (Federal Register, Vol. 66, No. 4, pages 1099-1111, Fri. January 5, 2001, see especially page 1106 column 3).
The specification does not provide adequate written description of the claimed invention. The legal standard for sufficiency of a patent's (or a specification's) written description is whether that description "reasonably conveys to the artisan that the inventor had possession at that time of the. . .claimed subject matter", Vas-Cath, Inc. V. Mahurkar, 19 USPQ2d 1111 (Fed. Cir. 1991).
In the instant case, the specification does not convey to the artisan that applicant had possession at the time of invention of the claimed invention, i.e., the genus of antibodies that specifically bind to an epitope in residues 95-117 and a secondary antibody directed against an epitope in residues 55-72 of the HCV core antigen, as asserted by the instant claims. The genus of antibodies are claimed by function, binding to residues 95-117 and 55-72 of HCVcAg. Several Mabs that bind to residues 95-117 and 55-72 of HCVcAg are listed in the table under paragraph [0084], including preferred antibodies 11C-13 and 14C-77. However, no structural information for any of the antibodies is provided. The Federal Circuit in University of California v. Eli Lilly and Co., 119 F.3d 1559, 43 USPQ2d 1398 (Fed. Cir. 1997) stated that “[a] written description of an invention involving a chemical genus, like a description of a chemical species, requires a precise definition, such as by structure, formula, [or] chemical name, of the claimed subject matter sufficient to distinguish it from other materials.” Id. At 1567, 43 USPQ2d at 1405. The court concluded that “naming a type of material generally known to exist, in the absence of knowledge as to what that material consists of, is not a description of that material.” Id.
The state of the prior art is such that it is well established in the art that the formation of an intact antigen-binding site of antibodies routinely requires the association of the complete heavy and light chain variable regions of a given antibody, each of which consists of three CDRs or hypervariable regions, which provide the majority of the contact residues for the binding of the antibody to its target epitope (Paul, Fundamental Immunology, 3 rd Edition, 1993, pp. 292-295, under the heading “Fv Structure and Diversity in Three Dimensions”). The amino acid sequences and conformations of each of the heavy and light chain CDRs are critical in maintaining the antigen binding specificity and affinity, which is characteristic of the immunoglobulin. It is expected that all of the heavy and light chain CDRs in their proper order and in the context of framework sequences which maintain their required conformation, are required in order to produce a protein having antigen-binding function and that proper association of heavy and light chain variable regions is required in order to form functional antigen binding sites (Paul, page 293, first column, lines 3-8 and line 31 to column 2, line 9 and lines 27-30). Even minor changes in the amino acid sequences of the heavy and light variable regions, particularly in the CDRs, may dramatically affect antigen-binding function as evidenced by Rudikoff et al (Proc. Natl. Acad. Sci. USA, 79:1979-1983, March 1982). Rudikoff et al. teach that the alteration of a single amino acid in the CDR of a phosphocholine-binding myeloma protein resulted in the loss of antigen-binding function. Colman P. M. (Research in Immunology, 145:33-36, 1994) teaches that even a very conservative substitution may abolish binding or may have very little effect on the binding affinity (see pg. 35, top of left column and pg. 33, right column). Thus, without the full sequence set of light and heavy chain CDR specific sequences in their respective order, the scope of antibodies claimed adequate lack written description.
The Federal Circuit clarified that a molecule can be adequately described without disclosing its complete structure. See Enzo Biochem, Inc. V. Gen-Probe Inc., 296 F.3d 1316, 63 USPQ2d 1609 (Fed. Cir. 2002). The Enzo court adopted the standard that the written description requirement can be met by “show[ing] that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics ....i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. “ Id. At 1324, 63 USPQ2d at 1613 (emphasis omitted, bracketed material in original). However, no such information is provided in the instant disclosure regarding the instantly claimed antibodies.
Furthermore The Board in Ex Parte Kubin found that the written description of 35 USC 112 was not met, stating:
Without a correlation between structure and function, the claim does little more than define the claimed invention by function. That is not sufficient to satisfy the written description requirement. See Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406 (“definition by function … does not suffice to define the genus because it is only an indication of what the gene does, rather than what it is”).
The Board in Ex Parte Kubin further stated on page 16:
Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features. See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
The court in In re Alonso (Fed. Cir. 2008) citing In re Enzo, 323 F.3d at 969:
[F]or purposes of satisfying the written description requirement, it is not enough merely to disclose a method of making and identifying compounds capable of being used to practice the claimed invention.
In AbbVie v. Janssen Biotech and Centocor Biologics (Fed. Cir. 2014) Judge Lourie focuses particularly on the alleged infringing antibodies and notes:
[While] AbbVie’s patents need not describe the allegedly infringing [compound] in exact terms . . . [t]he patents must at least describe some species representative of antibodies that are structurally similar to [the accused compound]. Because the patent document lacked any such structural description, the court confirmed that the corresponding claims were invalid under 112(a). In discussing the case, Judge Lourie was clear that one problem here is that the invention was described in terms of its function rather than its structure. Lourie writes: Functionally defined genus claims can be inherently vulnerable to invalidity challenge for lack of written description support, especially in technology fields that are highly unpredictable, where it is difficult to establish a correlation between structure and function for the whole genus or to predict what would be covered by the functionally claimed genus.
In this case, the specification does not describe the genus antibodies that are directed against an epitope in residues 95-117 and a secondary antibody directed against an epitope in residues 55-72 of the HCV core antigen and therefore, does not satisfy either the Lilly nor Enzo standards. The specification does disclose the genus of antibodies claimed.
There are insufficient structural features common to all members of the genus of antibodies. The Board in Kubin indicated that possession may not be shown by merely describing how to obtain possession of members of the claimed genus. The antibodies are claimed by function, binding to an epitope in residues 95-117 and an epitope in residues 55-72 of the HCV core antigen. However, the specification does not disclose sufficient information on the structural function relationship to identify the claimed genus of antibodies. One of ordinary skill in the art would not be able to identify the broad claimed genus of antibodies with specific binding to an epitope in residues 95-117 and an epitope in residues 55-72 of the HCV core antigen.
The specification does not provide an adequate written description of the broad genus of antibodies that bind an epitope in residues 95-117 and an epitope in residues 55-72 of the HCV core antigen that are required to practice the claimed invention. Applicants have not described the genus of antibodies sufficiently to show they had possession of the claimed genus. Since the disclosure fails to provide sufficient relevant identifying characteristics, and because the genus is highly variant, one of skill in the art would reasonably conclude that the disclosure fails to provide an adequate written description or disclose a representative number of species to describe the genus of antibodies claimed.
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.
(a)(2) the claimed invention was described in a patent issued under section 151, or in an application for patent published or deemed published under section 122(b), in which the patent or application, as the case may be, names another inventor and was effectively filed before the effective filing date of the claimed invention.
Claims 1-7, 10, 11, 13, 16-18, 22, and 23 are rejected under 35 U.S.C. 102(a)(1)/(a)(2) as being anticipated by Shah et al. (USPgPub 2003/0108858).
Figure 3, paragraphs [0013, 0015, 0017, 0036, 0042, 0106-0107], and claims 12 and 13 of Shah et al. anticipate a kit comprising at least one HCV antigen and at least one HCV antibody for the simultaneous detection of HCV antigens and antibodies, as required by instant claim 1. Antibodies C11-3 or C11-7 listed in Table III and claims 1, 3, 8, and 10 in the kit of Shah et al. are directed against HCV core antigen epitopes within 104-110, 112-124, anticipating the instant antibody directed against an epitope within 95-117 amino acids of the HCV core antigen. Antibodies 14-153-462; 14-726-217; 14-178-125; 14-1269-281; 14-947-104 14-188-104 and 14-1708-269 listed in Table III and claims 1, 3, 8, and 10 in the kit of Shah et al. are directed against HCV core antigen epitopes within 50-64, anticipating the instant antibody directed against an epitope within 55-72 amino acids of the HCV core antigen. The antibodies of Shah et al. anticipate the antibodies listed in claims 1 and 11. Figure 3 and claims 1, 3, 4, 7-13, 16, and 17 of Shah et al. require that at least one capture antibody and at least one antigen bound to a solid phase of magnetic particles, latex particles or microtiter plated (paragraphs [0029 and 0038]) and labeled with acridinium, and a biotin-labeled (secondary) avidin antibody, see Figure 3, paragraphs [0018, 0030, 0046, 0088, 0089], and claims 14 and 15, anticipating instant claims 2-7, 16, and 22. Paragraphs [0123 and 0127] of Shah et al. teach using positive (HCV-infected) and negative (healthy) plasma, anticipating instant claim 10. Shah et al. prepare the Mabs by immunizing mice with HCV core antigen amino acids 1-150 in paragraphs [0093-0096], anticipating the HCV core antigen comprising 55-72 and 95-117 residues, anticipating instant claim 13. Claims 2 and 9 of Shah et al. require that the at least one HCV antigen coated on the solid phase is selected from the core, NS3, NS4, NS5, and portions thereof, anticipating instant claim 17. Paragraphs [0070-0073, 0075] list recombinant protein portions, selected from a core antigen containing residues 1-150; NS3 containing residues 1192-1457; and NS4 containing residues 1569-1961, anticipating the residues contained by the antigens listed in instant claims 18 and 23.
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.
Claim 21 is rejected under 35 U.S.C. 103 as being unpatentable over Shah et al. supra, as applied to claims 1-7, 10, 11, 13, 16-18, 22, and 23 above, and further in view of Hoffman et al. (Hepatology. 1995; 21 (3): 632-638), as evidenced by Zein (Clinical Microbiology Reviews. 2000; 13 (2): 223-235).
See the teachings of Shah et al. above. Shah et al. do not teach the HCV genotypes/ subtypes listed in instant claim 21 for detection.
In Figure 3, Hoffman et al. list HCV core peptides various infected subjects react to, including patient 2, reacting to residues 153-172 and patients 9 and 11, reacting to residues 55-74. Table 2 of Hoffman et al. identifies the genotype these patients are infected with according to Simmonds et al. (see the * next to Genotype in the Table and the corresponding * notation under the Table). Table 2 identifies patients 2 and 11 as infected with genotype 1a and patient 9 as infected with genotype 1b. Table 1 of Zein correlate the various classification HCV types. Zein show that genotypes 1a and 1b of Simmonds et al. correspond to Okamoto et al. or Cha et al. types I and II.
One of ordinary skill in the art prior to the instant effective filing date would have been motivated to have detected specific genotypes the subject is infected with to administer an appropriate treatment regimen. One of ordinary skill in the art prior to the instant effective filing date would have had a reasonable expectation of success for detecting specific genotypes with the HCV core materials of Shah et al. because the core residue epitopes of Shah et al. comprising 104-110, 112-124, and 50-64, would have detected at least genotype I/1a recited in instant claim 21, as evidenced by Hoffman et al. and Zein.
Claims 8, 9, and 20 are rejected under 35 U.S.C. 103 as being unpatentable over Shah et al. as applied to claims 1-7, 10, 11, 13, 16-18, 22, and 23 above, and further in view of Pomerantz et al. (USPgPub 2003/0091590, of record) and Grodzki et al. (Methods Mol Biol. 2010; 588: 15-26, of record).
See the teachings of Shah et al. above. Shah et al. do not teach a lysis buffer, as required by claim 8 or a lysis buffer comprising the components recited in instant claims 9 and 20.
Paragraph [0171] of Pomerantz et al. teach a lysis buffer comprising Tris, a NP-40 (surfactant), SDS (denaturant), and a protease inhibitor cocktail (protective protein).
Pomerantz et al. do not teach including ammonium sulfate and ethanol in the lysis buffer, but Grodzki et al. do, see pages 16-17, second paragraph +.
Grodzki et al. teaches that a small amount of ammonium sulfate can be added in the purification process of antibodies to first precipitate the less soluble impurities from a sample (e.g. sera or ascites; see page 16), which are then removed by centrifugation. Grodzki et al. further teach that water miscible solvents, including ethanol, can be used to differentially
precipitate out proteins; see page 17, paragraph 4.
It would have been obvious for one of ordinary skill in the art prior to the effective filing date to prepare a lysis buffer as described by Pomerantz and further incorporate
ammonium sulfate and ethanol of Grodski et al., wherein the lysis buffer is incorporated as a component of the kit. One would have been motivated to do so for the advantage of optimizing a
successful lysis buffer of the prior art in order to precipitate less soluble impurities and
differentially precipitate out proteins as described by Grodzki et al. to purify antibodies. Further, one would have been motivated to substitute one buffer, including Tris for PBS. One would
have been motivated to do so for the advantage of optimizing the buffer solution by incorporating a buffer that is stable at different ranges of pH values. There would have been a reasonable expectation of success, given the underlying materials and methods are widely known, commonly used and successfully demonstrated as evidenced by the teachings of the prior art.
Allowable Subject Matter
Claim 24 is objected to as being dependent upon a rejected base claim, but would be allowable if rewritten in independent form including all of the limitations of the base claim and any intervening claims.
The prior art does not teach or suggest SEQ ID NOs: 1 or 2.
Conclusion
Any inquiry concerning this communication or earlier communications from the examiner should be directed to SHANON A FOLEY whose telephone number is (571)272-0898. The examiner can normally be reached M-F, generally 5:30 AM-5 PM, flexible.
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/Shanon A. Foley/Primary Examiner, Art Unit 1671