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 .
Information Disclosure Statement
The information disclosure statement filed February 9, 2021 fails to comply with 37 CFR 1.98(a)(2), which requires a legible copy of each cited foreign patent document; each non-patent literature publication or that portion which caused it to be listed; and all other information or that portion which caused it to be listed. It has been placed in the application file, but the information referred to therein has not been considered.
This objection refers to the Non-Patent Literature document 7.
Status of Claims
Claims 1-12 were pending.
Claims 1, 3, 5, 8, and 10-12 are amended.
Claims 1-12 are examined herein.
Claim Objections
Claim 1 is objected to because:
Claim 1 recites “antibody-FcRn-interaction” (step c), should be “antibody-FcRn interaction”.
Appropriate correction is required.
Withdrawn Rejections
The objection to the specification is withdrawn in view of specification amendments.
The objections to claims 3, 5, 8, and 10 are withdrawn in view of claims amendments.
The rejection of claims 1-12 under 35 U.S.C. 112(b) is withdrawn in view of claims 1, 5, and 12 amendments.
The rejection of claim 5 under 35 U.S.C. § 112(d) is withdrawn in view of Applicant argument.
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.
Claim 11 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
Claim 11 recites the branched glucan, of which the solid surface is free, is dextran. It is unclear what the limitation means because claim 1 already recites “the solid surface is free of branched glucan”. That also means the solid surface is free of all branched glucans including dextran.
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 11 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 11 recites the branched glucan, of which the solid surface is free, is dextran. It is unclear what the limitation means because parent claim 1 recites “the solid surface is free of branched glucan”, which means it is free of any species of the branched glucan genus, including dextran. Adding a species to an excluded genus does not further limit claim 1.
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 § 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:
Determining the scope and contents of the prior art.
Ascertaining the differences between the prior art and the claims at issue.
Resolving the level of ordinary skill in the pertinent art.
Considering objective evidence present in the application indicating obviousness or nonobviousness.
This application currently names joint inventors. In considering patentability of the claims the examiner presumes that the subject matter of the various claims was commonly owned as of the effective filing date of the claimed invention(s) absent any evidence to the contrary. Applicant is advised of the obligation under 37 CFR 1.56 to point out the inventor and effective filing dates of each claim that was not commonly owned as of the effective filing date of the later invention in order for the examiner to consider the applicability of 35 U.S.C. 102(b)(2)(C) for any potential 35 U.S.C. 102(a)(2) prior art against the later invention.
Claims 1-2, 4, 6, and 8-11 are rejected under 35 U.S.C. 103 as being unpatentable over Rossi et al. (IDS; WO2013181087), GEHealthcare-2012 (Biacor Assay Handbook, 2012), and Jonsson et al. (J Androl. 2010 Nov-Dec;31(6):560-5), and as evidenced by GEHealthcare-2005 (Biacore Sensor Surface Handbook, 2005), for reasons of record which are reiterated herein below.
Regarding claims 1-2 and 4, Rossi teaches a method for measuring binding affinity (Kd) of bispecific hexavalent antibodies to the neonatal Fc receptor (FcRn) by surface plasmon resonance ([0223]), wherein the FcRn is a soluble single-chain FcRn immobilized onto a biosensor chip using an amine coupling kit ([0211]).
Solutions comprising antibodies at different concentrations were applied to the biosensor chip – “test articles were diluted with pH 6.0 running buffer [50 mM NaPO4, 150 mM NaCl, and 0.05% (v/v) Surfactant 20] to 400, 200, 100, 50, and 25 nM and bound to the immobilized scFcRn” ([0211]).
Rossi does not specifically teach determining the association rate constant and the dissociation rate constant for each concentration as recited in step b) of claim 1. However, the reference teaches the final step c) determining with the rates obtained in step b) the KD-value of the antibody-FcRn interaction – “To determine FcRn binding affinity (KD) at pH 6.0, the data from all five concentrations were used simultaneously to fit a two-state reaction model” ([0211]). Binding affinity calculations necessarily use measurements of the association and the dissociation rate constants.
Additionally, Rossi teaches the immobilized FcRn is a monomeric FcRn – specifically, “soluble single-chain FcRn was generated following the methods of Feng” ([0211]), meeting the limitation of claim 4 reciting the FcRn is a single chain FcRn.
Rossi teaches “scFcRn was immobilized onto a CM5 biosensor chip using an amine coupling kit” ([0211]), but does not specifically teach the monomeric FcRn is immobilized using functional groups that are directly attached to said solid surface; the solid surface is free of branched glucan; and the immobilization of the FcRn is at a pH value of from pH 7 to pH 8 and at a pH value of about pH 7.4.
Regarding claims 1-2, GEHealthcare-2012 teaches different sensor surface types available for immobilization of binding molecules for surface plasmon resonance measurements (Table 3-1, pg. 18-19). Specifically, the reference teaches C1 sensor chip having no dextran matrix, with carboxyl groups directly attached to the surface (Table 3-1, pg. 18). The C1 sensor chip meets the limitation of claim 1 reciting the solid surface is free of branched glucan.
Rossi and GEHealthcare-2012 do not specifically teach immobilization of the FcRn at a pH value of from pH 7 to pH 8 and at a pH value of about pH 7.4.
Regarding claims 1-2, Jonsson teaches a method for surface plasmon resonance study of semenogelin protein binding (Title and Abstract). Jonsson also teaches immobilization of ligands for surface plasmon resonance at a pH value of about pH 7.4.
Specifically, Jonsson teaches the flow buffer during the immobilization comprised 10 mM HEPES, pH 7.4 (pg. 561, col. 2, par. 3), meeting the limitations of claims 1 and 2 reciting immobilization at a pH value of from pH 7 to pH 8 and at a pH value of about pH 7.4.
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Rossi by employing a glucan free sensor as taught by GEHealthcare-2012 (C1 sensor, pg. 18) as an obvious matter of simple substitution of one known element (C1 sensor) for another (CM5 sensor) to obtain predictable results.
One skilled in the art would have a reasonable expectation of success using C1 sensor instead of CM5 sensor, because GEHealthcare-2012 teaches using both sensors for surface plasmon resonance studies.
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to have modified the method of Rossi and GEHealthcare-2012 by immobilizing FcRn on the sensor surface at a pH value of about pH 7.4 as taught by Jonsson as an obvious matter of combining prior art elements (the SPR method of Rossi and GEHealthcare-2012 with immobilization conditions of Jonsson) according to known methods to yield predictable results.
One skilled in the art would have a reasonable expectation of success using a pH value of about pH 7.4 during immobilization of FcRn on the sensor surface because GEHealthcare-2012 teaches the pH of the ligand solution should be above the pKa (3.5) of carboxyl groups on the surface so that the surface is negatively charged” (pg. 19, last par.) and Jonsson has demonstrated successful immobilization at a pH value of about pH 7.4.
Regarding claim 6, Rossi teaches “scFcRn was immobilized onto a CM5 biosensor chip using an amine coupling kit” ([0211]), meeting the limitation of claim 6 reciting amine coupling.
Regarding claim 8, Rossi, GEHealthcare-2012, and Jonsson teach the immobilization buffer comprising 10 mM HEPES, pH 7.4 (Jonsson, pg. 561, col. 2, par. 3), meeting the corresponding pH limitation of claim 8.
Additionally, GEHealthcare-2005 provides evidence that ligand concentrations during immobilization step vary depending on the isoelectric point of the ligand, the type of sensor surface, and the requirements of the application “ligand solutions for immobilization are usually quite dilute (typically 10–50 µg/ml for most proteins) provided that efficient pre-concentration can be achieved. Higher concentrations may be needed for proteins that for reasons of low isoelectric point or other factors do not pre-concentrate efficiently on the surface. The best concentration will vary according to the nature of the ligand, the type of sensor surface and the requirements of the application” (pg. 35, col. 1, par. 2).
Since Applicant has not disclosed that the claimed FcRn immobilization concentration of about 250 µg/ml is for any particular purpose or solves any stated problem and the prior art teaches that ligand concentrations vary (see par. above), absent unexpected results, it would have been obvious for one of ordinary skill to discover the optimum workable ranges of FcRn concentration by normal optimization procedures known in the art.
Regarding claim 9, Rossi, GEHealthcare-2012, and Jonsson teach the solution of the antibody applied to the immobilized FcRn comprises 150 mM NaCl. Specifically, Jonsson teaches “the flow buffer during all experiments comprised … 150 mM NaCl” (pg. 561, col. 2, last par.).
Regarding claim 10, Rossi, GEHealthcare-2012, and Jonsson teach the solution of the antibody applied to the immobilized FcRn in step b) comprises 10 mM HEPES, 150 mM NaCl, 0.05 % P-20 at a pH value of pH 7.4. Specifically, Jonsson teaches the flow buffer during the immobilization comprises of 10 mM HEPES, 150 mM NaCl, and 0.05% Tween 20 (pH 7.4) (pg. 561, col. 2, par. 3).
Jonsson does not specifically teach P-20. However, GEHealthcare-2012 teaches P-20 as an equivalent to Tween-20 “Inclusion of non-ionic detergent (0.05% Surfactant P20, Tween™ or equivalent) in all buffers is recommended to minimize deposition of protein and other biomolecules in the flow system” (pg. 24, par. 1).
The limitation “optionally 20 % (w/w) ethylene glycol” is not given patentable weight (see Claim Interpretation above).
Regarding claim 11, Rossi teaches “scFcRn was immobilized onto a CM5 biosensor chip using an amine coupling kit” ([0211]). The CM5 biosensor chip is a dextran-coated chip as evidenced by GEHealthcare-2012 (pg. 17, Fig. 3-1), meeting the limitation of the claim reciting the branched glucan is dextran.
Claims 3 and 7 are rejected under 35 U.S.C. 103 as being unpatentable over Rossi, GEHealthcare-2012, and Jonsson, as applied to claims 1-2 above, in view of Douzi (Methods in Molecular Biology, vol 1615, 2017. Humana Press, New York, NY, pp 257–275), for reasons of record which are reiterated herein below.
The teachings of Rossi, GEHealthcare-2012, and Jonsson have been set forth above.
Regarding claim 7, Jonsson teaches that for immobilization the ligand (SgI protein) was injected at 20 µg/mL concentration to reach 2000 resonance units (RU) (pg. 561, col. 2, par. 3).
Rossi, GEHealthcare-2012, and Jonsson do not specifically teach a density of 50-150 RU and a density of about 50-150 pg/mm2.
Regarding claims 3 and 7, Douzi teaches a surface plasmon resonance method to study protein–protein interactions (Title and Abstract). Douzi also teaches a density of 50-150 RU. Specifically, the reference teaches “kinetic measurements require a small amount of ligand immobilization (Rmax between 50 and 150 RUs)” (pg. 267, par. 4). Claim 1 recites determining the KD-value of the antibody-FcRn interaction by determining the association rate constant and the dissociation rate constant, which are the kinetic measurements.
The protein concentration taught by Jonsson as 20 µg/mL to reach 2000 resonance units (RU) translates into a density of 50-150 pg/mm2 to reach 50-150 RU as taught by Douzi.
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Rossi, GEHealthcare-2012, and Jonsson by employing a density of 50-150 RU as taught by Douzi and a corresponding density of 50-150 pg/mm2 as taught by Jonsson, in order to measure the KD-value of the antibody-FcRn interaction using kinetic measurements. One having ordinary skill in the art would have been motivated to make such a change because the density of Douzi is selected for kinetic measurements disclosed in instant application and Jonsson teaches a calculation to translate RU density into mass density in pg/mm2. The use of such combination would have been desirable for those of ordinary skill in the art to run SPR experiments in optimal conditions.
One having ordinary skill in the art would have had a reasonable expectation of success in combining the prior art references because Douzi and Jonsson teach RU and mass densities for SPR method of Rossi, GEHealthcare-2012, and Jonsson.
Claim 5 is rejected under 35 U.S.C. 103 as being unpatentable over Rossi, GEHealthcare-2012, and Jonsson, as applied to claims 1-2 above, in view of Feng et al. (Protein Expr Purif. 2011 Sep;79(1):66-71), Cytiva (Sensor Chip C1, 2026), Boucher et al. (J Mol Recognit. 2013 Oct;26(10):496-500), and Zhang et al. (Sci Rep. 2020 Apr 10;10(1):6239), for reasons of record which are reiterated herein below.
The teachings of Rossi, GEHealthcare-2012, and Jonsson have been set forth above.
Regarding claim 5, Rossi teaches a method for measuring binding affinity using soluble single-chain FcRn immobilized onto a surface plasmon biosensor chip ([0211]), wherein the single-chain FcRn is a fusion polypeptide of beta-2-microglobulin and human FcRn generated by following the methods of Feng et al. (2011, Protein Expr. Purif. 79:66-71).
Rossi, GEHealthcare-2012, and Jonsson do not specifically teach wherein the fusion scFcRn comprises an (GGGGS)4-peptidic linker, and a C-terminal Avi-tag.
Regarding claim 5, Feng teaches “Design, expression and characterization of a soluble single-chain functional human neonatal Fc receptor” (Title). Specifically, the reference teaches a fusion polypeptide between beta-2-microglobulin and FcRn (Abstract) with a (GGGGS)3 linker (Fig. 1A). Additionally, the fusion polypeptide comprises a His6 affinity tag at the C-terminus (pg. 67, col. 2, par. 1 and pg. 68, col. 2, par. 1).
Feng does not specifically teach (GGGGS)4 linker and a C-terminal Avi-tag.
Regarding claim 5, Zhang teaches designing protein fusions between two polypeptides connected by a GGGGS-linker (Abstract). Zhang also teaches (GGGGS)4 linker.
Specifically, Zhang teaches that fusing two polypeptides together can cause tension between the polypeptides if a linker is too short or decrease the stability of the fusion if the linker is too long (pg. 2, par. 5). The reference teaches using linkers of different sizes GGGGS4, GGGGS5 and GGGGS6 to find properly optimized protein fusion (pg. 2, last par.).
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Rossi, GEHealthcare-2012, and Jonsson by employing a GGGGS-linker as taught by Feng, and optimize the size of the linker as taught by Zhang, in order to connect beta-2-microglobulin and FcRn moieties in the fusion with the linker of optimal size. One having ordinary skill in the art would have been motivated to make such a change because Zhang teaches that linker size is important for the protein fusion stability (pg. 2, par. 5). The use of such combination would have been desirable to those of ordinary skill in the art for the reasons mentioned above.
One having ordinary skill in the art would have had a reasonable expectation of success in combining the prior art references because Feng teaches fusing beta-2-microglobulin and FcRn moieties with the GGGGS-linker, and Zhang teaches optimizing the size of the GGGGS-linker.
Feng and Zhang do not specifically teach a C-terminal Avi-tag.
Avi-tag is an affinity tag for immobilizing proteins in mild conditions. Feng teaches an alternative to the Avi-tag - a His6 affinity tag at the C-terminus of the fusion protein (pg. 67, col. 2, par. 1 and pg. 68, col. 2, par. 1).
Regarding claim 5, Boucher teaches a method for immobilizing polypeptide ligands on a surface plasmon resonance chip surface using in vivo biotinylation of the Avi-tag incorporated into the ligand sequence (Abstract and Fig. 1A-B). Both His-tag and biotin-tags covalently attached to a protein are known in the art for immobilization of peptides and proteins. Both tags can be used interchangeably. Both tags can be located at either terminus of the protein or inside the protein sequence as long as the tags are available for interaction with the chip surface.
GEHealthcare-2012 teaches different sensor surface types available for immobilization of binding molecules, including both an NTA sensor chip with nitrilotriacetic acid covalently attached for capture of histidine-tagged ligands, such as the His6 affinity tagged fusion protein of Feng, and a SA sensor chip with streptavidin covalently attached for capture of biotinylated molecules (GEHealthcare-2012, Table 3-1, pg. 19). The SA sensor chip is not free of branched glucan as claim 1 requires.
However, Cytiva, the manufacturer of these chips, teaches that the C1 sensor chip (see GEHealthcare-2012 Table 3-1, pg. 18), which is free of the dextran matrix can be used for ligand immobilization when “there is a need to avoid dextran on the surface” (pg. 1, par. 1). Immunoglobulins are glycoproteins containing covalently attached carbohydrate structures (glycans).
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Rossi, GEHealthcare-2012, Jonsson, Feng, and Zhang by employing the Avi-tag as taught by Boucher, in order to immobilize the soluble single-chain FcRn of Rossi on the surface plasmon resonance chip surface, as an obvious matter of simple substitution of one known affinity tag for another to obtain predictable results.
One having ordinary skill in the art would have had a reasonable expectation of success in combining the prior art references because both His-tag and biotin-tag are well-known in the art as reliable and interchangeable affinity handles. The His-tag of Feng located at the C-terminus of the fusion protein was successfully used for purification of the scFcRn on a Ni-chelating HiTrap
column (pg. 67, col. 2, last par.), therefore it is readily accessible for interaction with the chip surface. One would have had a reasonable expectation of success with the C-terminal Avi-tag.
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Rossi, GEHealthcare-2012, Jonsson, Feng, Zhang, and Boucher by employing a dextran-free matrix as taught by Cytiva, in order to immobilize the soluble single-chain FcRn and avoid potential interference of dextran on the surface of the chip with the glycans normally attached to immunoglobulins.
One having ordinary skill in the art would have had a reasonable expectation of success of using the dextran-free matrix instead of dextran-modified matrix because both kinds of matrices are produced by Cytiva for surface plasmon resonance experiments (GEHealthcare-2012, Table 3-1, pg. 19).
Claim 12 is rejected under 35 U.S.C. 103 as being unpatentable over Rossi, GEHealthcare-2012, and Jonsson, as applied to claims 1-2 above, in view of Qureshi et al. (Sci Rep. 2017 Dec 6;7(1):17049), for reasons of record which are reiterated herein below.
The teachings of Rossi, GEHealthcare-2012, and Jonsson have been set forth above.
Rossi, GEHealthcare-2012, and Jonsson do not specifically teach wherein the Fab-FcRn interaction as well as the Fc-region-FcRn interaction are divided and visualized using a 2- or 3-dimensional diagram.
Regarding claim 12, Qureshi teaches a method for analysis of Fc-receptor binding data generated in SPR experiments (pg. 13, par. 6). Specifically, the reference teaches analysis of hexameric-Fc-FcRn interaction using the same software TraceDrawer and the Interaction Map (pg. 13, par. 7) as disclosed in the specification. Two-dimensional diagrams with stability on the x-axis and the recognition on the y-axis were used in visualization (Fig. 2A-B), meeting the corresponding limitation of the claim reciting the Fc-region-FcRn interaction are divided and visualized using a 2- or 3-dimensional diagram.
It would have been obvious to one having ordinary skill in the art before the effective filing date of the claimed invention to modify the method of Rossi, GEHealthcare-2012, and Jonsson by employing software analysis methods as taught by Qureshi, in order to visualize the interaction data. One having ordinary skill in the art would have been motivated to make such a change because the software analysis methods taught by Qureshi are designed for analysis of binding data generated by the method of Rossi, GEHealthcare-2012, and Jonsson. The use of such combination would have been desirable to those of ordinary skill in the art for the reasons mentioned above.
One having ordinary skill in the art would have had a reasonable expectation of success in combining the prior art references because Qureshi teaches the software analysis methods directly applicable to binding data generated in SPR experiments of Rossi, GEHealthcare-2012, and Jonsson.
Although Qureshi does not specifically teach analysis of the Fab-FcRn interaction, such limitation is drawn to intended use of the analysis method of Qureshi and therefore the prior art only needs to be capable of performing the recited intended use. So long as the analysis software of Qureshi is capable of analysis of the Fc-region-FcRn interaction, it can be used for analysis of the Fab-FcRn interaction. Therefore, the software reads on the claim.
Response to Arguments
Applicant's arguments filed July 7, 2026 have been fully considered.
Claim 5 was rejected under 35 U.S.C. § 112(d). The rejection is withdrawn in view of Applicant argument.
Claims 1-2, 4, 6, and 8-11 were rejected under 35 U.S.C. § 103 as being unpatentable over the cited prior art. Applicant disagrees (section “Rejections Under 35 U.S.C. § 103”, pg. 10-13), but the arguments are not persuasive:
Applicant argues that the limitation of claim 1 reciting “immobilization of the FcRn is at a pH value of from pH 7 to pH 8” is not addressed (pg. 11, par. 1-2). Specifically, Applicant correctly cites a passage from the non-final OA (mailed April 6, 2026) “The Office Action then relies on Jonsson, stating that "Jonsson teaches the flow buffer during the immobilization comprised 10 mM HEPES, pH 7.4 (pg. 561, col. 2, par. 3), meeting the limitations of claims I and 2 reciting immobilization at a pH value of from pH 7 to pH 8 and at a pH value of about pH 7 .4," (Office Action, page 7)” (pg. 11, par. 3) that addresses the limitation.
Then Applicant cites Jonsson conditions for activation of the chip “Jonsson actually states that the "flow cells of a CM3 sensor chip were activated with 20 mL of 0.2 M l-ethyl-3-(3-dimethylaminopropyl) carbodiimide and 0.05 M N-hydroxysulphosuccinimide at a flow rate of 5 mL/min, and then albumin and Sgl (both at 20 mglmL in 10 mM sodium acetate [pH 5.0])” (pg. 11, par. 4) and incorrectly concludes that these were immobilization conditions. The cited passage clearly says, "flow cells of a CM3 sensor chip were activated”. Activation is a separate step from immobilization and indeed requires an acidic pH. The actual immobilization step was performed at pH 7.4 as presented in the paragraph above, meeting the limitation “a pH value of from pH 7 to pH 8”.
As such, the conclusion made by Applicant “Jonsson, just like Rossi and GEHEalthcare-2012, teaches immobilizing the ligand onto the solid surface (e.g., SPR chip) at a pH below 7” (pg. 12, par. 1) is incorrect.
Additionally, Applicant describes why a pH value from pH 7 to pH 8 was chosen for immobilization (pg. 12, par. 2) but fails to overcome the rejection because Jonsson teaches pH 7.4 falling within this range.
Applicant argues that “Jonsson is completely silent on the use of FcRn as the ligand and provides no teaching or suggestion of how pH effects FcRn heterodimerization” (pg. 12, last par.). The argument is not persuasive because Applicant is arguing limitations which are not claimed.
In response to applicant’s argument that the references fail to show certain features of the invention, it is noted that the features upon which applicant relies (i.e., how pH effects FcRn heterodimerization) are not recited in the rejected claim(s). Although the claims are interpreted in light of the specification, limitations from the specification are not read into the claims. See In re Van Geuns, 988 F.2d 1181, 26 USPQ2d 1057 (Fed. Cir. 1993).
Finally, Applicant’s argument “The remaining cited references GEHealthcare-2005, Douzi, Feng, Cytivia, Boucher, Zhang, and Qureshi fail to cure the deficiencies of Rossi, GEHealthcare-2012, and Jonsson, as the combined disclosures fail to teach or even suggest a method for determining antibody-FcRn interaction by immobilizing FcRn on a solid at a pH value of from pH 7 to pH 8” (pg. 13, par. 1) is incorrect in view of Jonsson’s teaching that " the flow buffer during the immobilization comprised 10 mM HEPES, pH 7.4” (pg. 561, col. 2, par. 3) discussed above.
Conclusion
THIS ACTION IS MADE FINAL. Applicant is reminded of the extension of time policy as set forth in 37 CFR 1.136(a).
A shortened statutory period for reply to this final action is set to expire THREE MONTHS from the mailing date of this action. In the event a first reply is filed within TWO MONTHS of the mailing date of this final action and the advisory action is not mailed until after the end of the THREE-MONTH shortened statutory period, then the shortened statutory period will expire on the date the advisory action is mailed, and any nonprovisional extension fee (37 CFR 1.17(a)) pursuant to 37 CFR 1.136(a) will be calculated from the mailing date of the advisory action. In no event, however, will the statutory period for reply expire later than SIX MONTHS from the date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to Alexander Volkov whose telephone number is (571) 272-1899. The examiner can normally be reached M-F 9:00AM-5:00PM (EST).
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/ALEXANDER ALEXANDROVIC VOLKOV/Examiner, Art Unit 1677
/REBECCA M GIERE/Primary Examiner, Art Unit 1677
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