Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
1. Applicant’s election of Group II (claims 3-6 & 12-20) with traverse in the reply filed on 6/26/26 is acknowledged.
2. In traversing the Unity of Invention Applicants argue – “Applicant submits the actual technical problem solved by the present invention is how to effectively immobilize Amine Dehydrogenase (AmDH) and Formate Dehydrogenase (FDH) to achieve high catalytic activity and operational stability, which cannot be achieved by traditional glutaraldehyde-activated carriers or other activation methods (e.g., hexamethylene diisocyanate or p-benzoquinone) as evidenced by Comparative Examples 1-4 in the specification.
The distinguishing technical features are not limited to the use of cyanuric chloride alone. Rather, they comprise a specific immobilization process including: 1) activation with Cyanuric Chloride: Using cyanuric chloride to activate the amino resin; and 2) PEI Post-Modification: The crucial step of post-modifying the initially immobilized enzyme with Polyethyleneimine (PEI).
Therefore, Applicant submits the instant claims involve an inventive step for the following reasons.
A. No Motivation to Combine D1 and D2 (US Patent No. 5,780,260A):
1. Conflict in Activation Medium (Aqueous vs. Organic Solvent)
Applicant submits D1 relies on glutaraldehyde activation, which is performed in an
aqueous buffer (e.g., phosphate buffer, pH 7.5) (D1, Example 1, Paragraph [0106]). The entire immobilization process of D1 is conducted in an aqueous environment, which is standard for glutaraldehyde cross-linking.
Applicant submits D2 explicitly states that the activation of amino groups is "preferably carried out by reaction with dialdehydes... This method is particularly easy to carry out even in an aqueous medium. By this means it is possible to avoid the use of toxic compounds and organic solvents" (D2, Column 4, Lines 30-35). While D2 mentions cyanuric chloride as one option among many (D2, Column 4, Lines 15-20), Applicant submits the preferred embodiment and the general teaching of D2 lean towards aqueous compatibility and explicitly discourage the use of organic solvents.
Applicant submits the claimed method of the present application critically requires
dispersing the amino carrier in a polar organic solvent (e.g., acetone, THF) and reacting with cyanuric chloride in a low-water/anhydrous environment (Claims 4-5). This "dry" activation is essential because cyanuric chloride hydrolyzes rapidly in the presence of water, rendering it ineffective for the specific activation of amino resins in the manner claimed.
Applicant submits there is no motivation for a person skilled in the art to replace the
aqueous glutaraldehyde system of D1 with an organic solvent-based cyanuric chloride system. Such a change would contradict D2's preference for aqueous conditions and its explicit teaching to avoid organic solvents. Furthermore, combining Dl's aqueous enzyme solution with D2's cyanuric chloride activation would likely cause the immediate hydrolysis of cyanuric chloride, failing to achieve the intended activation. Thus, D1 and D2 do not suggest the specific "organic solvent activation" step of the instant application.
2. D1 Does Not Teach or Suggest PEI Post-Modification for Stability
Regarding the use of PEI, Applicant submits in D1, PEI is primarily used for non- covalent adsorption to immobilize sensitive coenzymes (like FDH) or as a secondary layer for a second enzyme (D1, Example 2, Method 2, Paragraph [0119]). D1 does not disclose using PEI to covalently cross-link or protect enzymes that have already been covalently bound to a carrier. Specifically, D1 uses PEI before or during the adsorption of the secondary enzyme, not as a post- immobilization treatment for the primary enzyme.
Applicant submits the claimed method of the present invention involves modifying the initially immobilized enzyme (which is covalently bound to the cyanuric chloride-activated carrier) with PEI after the immobilization step (Claim 6). This specific sequence creates a polymer-bonded protective layer that significantly enhances the operational stability of the water-soluble AmDH/FDH system.
Applicant submits neither D1 nor D2 suggests or teaches this specific post- immobilization PEI modification step in the context of cyanuric chloride-activated carriers. D1 uses PEI for adsorption, while D2 does not use PEI at all. There is no teaching in the cited references to apply PEI post-modification to covalently bound AmDH/FDH to solve the problem of stability.
B. The Combination of D1 and D2 Does Not Yield the Claimed Solution
Applicant submits even if one were to assume a motivation to use cyanuric chloride, the combination of D1 and D2 fails to teach the critical sequence of steps required by the instant method. D1 teaches glutaraldehyde activation in water + PEI adsorption for coenzymes. D2 teaches cyanuric chloride activation (generally in water or unspecified solvent, but preferring avoidance of organic solvents) for different enzymes (Penicillin G Amidase, etc.).
The instant application is directed to a specific combination of: 1) Organic Solvent
Activation: Cyanuric chloride activation in acetone/THF (dry environment); 2) Buffer Wash: Replacing organic solvent with buffer before enzyme addition; 3) Covalent Binding: Binding AmDH/FDH; and 4) PEI Post-Modification: Using low molecular weight PEI (1.8-10 KDa) to cross-link/protect the immobilized enzymes.
The specific combination is not suggested by D1 or D2. The step of washing away the
organic solvent and then performing PEI post-modification on the covalently bound enzyme is a unique sequence not found in the cited references. The cited references offers no guidance on how to combine these specific chemical treatments to achieve the results of the instant application.
C. Unexpected Technical Results
Applicant submits the data in the present application (Embodiments 1-4 vs. Comparative Examples 1-5) clearly demonstrate the necessity and unexpected benefit of the claimed combination:
Glutaraldehyde: Activity drops drastically (55% to 6% over 5 cycles) (Comp. Ex. 1).
Cyanuric Chloride WITHOUT PEI: Activity drops significantly (98% to 13% over 5
cycles) (Comp. Ex. 4).
Cyanuric Chloride WITH PEI (Present Invention): Activity remains high (99% to
91% over 5 cycles) (Ex. 1).
Applicant submits this demonstrates that the PEI post-modification step is critical to the success of the cyanuric chloride activation for AmDH. The cited references do not suggest this specific synergy. D1 uses glutaraldehyde (no CC, no PEI post-mod for stability). D2 uses CC (no PEI). Neither teaches the combination for AmDH.
Therefore, the technical solution is non-obvious and constitutes a special technical feature. The data demonstrates that the specific sequence of cyanuric chloride activation in organic solvent combined with PEI post-modification is not obvious. Merely using cyanuric chloride (without PEI post-modification) is insufficient (13% vs 91%). Merely using PEI post- modification on a different activation method (glutaraldehyde) is ineffective (6% vs 91%). Only the specific combination claimed in the instant application achieves high stability and activity.
D1 uses PEI for adsorption, not for post-modification of covalently bound enzymes. D2 uses cyanuric chloride, but not for this enzyme system, nor with PEI post-modification. The synergy between the specific activation chemistry (cyanuric chloride in organic solvent) and the specific post-treatment (PEI) provides a technical effect (enhanced stability of water-soluble AmDH/FDH) that is not suggested by the prior art.
Therefore, claims 3-6 and 12-20 involve are patentable over the cited references.
3. Applicants arguments are considered and the lack of unity requirement is withdrawn.
4. All pending claims 1-20 are under consideration in this examination.
5. Drawings
The drawings filed on 6/28/24 are acknowledged.
6. IDS filed 7/12/24, 4/10/25 & 12/16/25 are considered.
7. Specification
The specification has not been checked to the extent necessary to determine the presence of all possible minor errors. Applicant's cooperation is requested in correcting any errors of which applicant may become aware in the specification.
8. Written Description
Claims 1, 3-9, 12-17 & 19-20 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112, first paragraph, as containing 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(s), at the time the application was filed, had possession of the claimed invention.
Claims 1-20 of the instant application are drawn to the following genus claims.
1. An immobilized enzyme, wherein the immobilized enzyme is a Polyethyleneimine (PEI)-modified immobilized enzyme, and comprises: an enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) and/or a Formate Dehydrogenase (FDH); and a carrier, wherein the carrier is a cyanuric chloride-activated amino carrier.
2. The immobilized enzyme according to claim 1, wherein the AmDH comprises an AmDH as shown in SEQ ID NO: 1; preferably, the FDH comprises a FDH as shown in SEQ ID NO: 2; preferably, the amino carrier comprises ECR8409, LX-1000HA, or LX-1000EPHA; and preferably, the molecular weight of PEI is 1.8-10 KDa.
3. A method for preparing an immobilized enzyme, comprising: activating an amino carrier with cyanuric chloride to obtain an activated carrier; and mixing and incubating an enzyme and the activated carrier for immobilization, and then modifying the immobilized product with Polyethyleneimine (PEI) to obtain the immobilized enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) and/or a Formate Dehydrogenase (FDH).
4. The method according to claim 3, wherein activating the amino carrier with the cyanuric chloride to obtain the activated carrier comprises: dispersing the amino carrier in an organic solvent to obtain a carrier suspension; and reacting the cyanuric chloride with the carrier suspension to activate the amino carrier, so as to obtain the activated carrier.
5. The method according to claim 4, wherein before immobilization, the method further comprises washing the activated carrier with a buffer solution to replace the organic solvent.
6. The method according to claim 3, wherein mixing and incubating the enzyme and the activated carrier for immobilization, and then modifying the immobilized product with the PEI to obtain the immobilized enzyme comprises: mixing and incubating the enzyme and the activated carrier for immobilization to obtain an initial immobilized enzyme; and post-modifying on the initial immobilized enzyme with the PEI, so as to obtain the immobilized enzyme.
7. A method for using immobilized enzyme according to claim 1 in a continuous reaction.
8. The method according to claim 7, wherein the continuous reaction comprises performing the continuous reaction in a packed bed reactor; preferably, the packed bed reactor is made by packing the immobilized enzyme into an empty chromatography column or a stainless steel chromatography column; preferably, a volume of the packed bed reactor is 5-50 mL; and preferably, a method for packing the packed bed reactor is wet packing.
9. The method according to claim 8, wherein the continuous reaction comprises: pumping a substrate-containing reaction system into the packed bed reactor from bottom to top, and re-mixing a reaction product in the reaction system, wherein a pump is a constant flow pump, and preferably, a pressure of the constant flow pump is less than or equal to 20 MPa; and preferably, a flow rate of the continuous reaction is 0.01-10 mL/min.
10. The method according to claim 9, wherein the immobilized enzyme comprises an immobilized AmDH, or a co-immobilization system of AmDH and FDH; preferably, the AmDH comprises an AmDH as shown in SEQ ID NO: 1; preferably, the FDH comprises a FDH as shown in SEQ ID NO: 2; preferably, the reaction system comprises a substrate or comprises a mixture of the substrate and the FDH; and preferably, the immobilized enzyme is the immobilized AmDH, and the reaction system comprises the mixture of the substrate and the FDH.
11. The method according to claim 10, wherein the immobilized enzyme is the immobilized AmDH, and the reaction system comprises the mixture of the substrate and the FDH.
12. The method according to claim 4, wherein the organic solvent is a polar organic solvent; preferably, the polar organic solvent comprises any one or more of tetrahydrofuran, acetone, dimethyl formamide, or dimethyl sulfoxide.
13. The method according to claim 4, wherein a temperature for activation is 0-30° C., and more preferably, 0-5° C.; preferably, a time for activation is 2-5 h.
14. The method according to claim 4, wherein, after activation, the activated carrier is washed with the organic solvent to remove unreacted cyanuric chloride; preferably, after washing, the method further comprises drying the activated carrier with nitrogen in a blowing manner.
15. The method according to claim 4, wherein the amino carrier is a dry carrier; preferably, the amino carrier comprises ECR8409, LX-1000HA, or LX-1000EPHA.
16. The method according to claim 5, wherein the enzyme is prepared using the buffer solution; preferably, the buffer solution comprises a phosphate buffer solution, a glycine buffer solution, or a borax buffer solution; preferably, a concentration of the phosphate buffer solution is 20-50 mM; preferably, a pH of the phosphate buffer solution is 6.5-9.0.
17. The method according to claim 5, wherein a temperature for immobilization is 0-30° C., and more preferably, 4-30° C.; and preferably, a time for immobilization is 2-5 h.
18. The method according to claim 5, wherein the AmDH comprises an AmDH as shown in SEQ ID NO: 1; preferably, the FDH comprises a FDH as shown in SEQ ID NO: 2.
19. The method according to claim 6, wherein post-modifying on the initial immobilized enzyme by adding a PEI solution to the initial immobilized enzyme; preferably, a molecular weight of the PEI is 1.8-10 KDa; preferably, a pH of the PEI solution is 5-8; preferably, a final concentration of the added PEI is 0.5-3% W/V.
20. The method according to claim 6, wherein a temperature for post-modification is 0-30° C., preferably, 10-30° C.; and preferably, a time for post-modification is 8-24 h.
The purpose of the written description requirement is to ensure that the inventor had possession, at the time the invention was made, of the specific subject matter claimed. For a broad generic claim, the specification must provide adequate written description to identify the genus of the claim.
“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." Fiers, 984 F.2d at 1171, 25 USPQ2d 1601; In re Smythe, 480 F.2d 1376, 1383, 178 USPQ 279, 284985 (CCPA 1973) (“In other cases, particularly but not necessarily, chemical cases, where there is unpredictability in performance of certain species or subcombinations other than those specifically enumerated, one skilled in the art may be found not to have been placed in possession of a genus.”). Regents of the University of California v. Eli Lilly & Co., 119, F.3d 1559, 1568, 43 USPQ2d 1398, 1405 (Fed. Cir. 1997).
MPEP § 2163 further states that if a biomolecule is described only by a functional characteristic, without any disclosed correlation between function and structure of the biomolecule, it is "not sufficient characteristic for written description purposes, even when accompanied by a method of obtaining the claimed biomolecule.”
“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 …, 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 claimed genus.” MPEP 2163.
Furthermore, 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. The disclosure of only one species encompassed within a genus adequately describes a claim directed to that genus only if the disclosure ‘indicates that the patentee has invented species sufficient to constitute the gen[us].’ See Enzo Biochem, 323 F.3d at 966, 63 USPQ2d at 1615; Noelle v. Lederman, 355 F.3d 1343, 1350, 69 USPQ2d 1508, 1514 (Fed. Cir. 2004) (Fed. Cir. 2004) (‘[A] patentee of a biotechnological invention cannot necessarily claim a genus after only describing a limited number of species because there may be unpredictability in the results obtained from species other than those specifically enumerated.’). ‘A patentee will not be deemed to have invented species sufficient to constitute the genus by virtue of having disclosed a single species when … the evidence indicates ordinary artisans could not predict the operability in the invention of any species other than the one disclosed.’ In re Curtis, 354 F.3d 1347, 1358, 69 USPQ2d 1274, 1282 (Fed. Cir. 2004).” MPEP 2163.
In University of California v. Eli Lilly & Co., 43 USPQ2d 1938, the Court of Appeals for the Federal Circuit has held 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”. As indicated in MPEP § 2163, 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, 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 that Applicant was in possession of the claimed genus. In addition, 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.
The factors considered in the Written Description requirement are (1) level of skill and knowledge in the art, (2) partial structure, (3) physical and/or chemical properties, (4) functional characteristics alone or coupled with a known or disclosed correlation between structure and function, and the (5) method of making the claimed invention. Disclosure of any combination of such identifying characteristics that distinguish the claimed invention from other materials and would lead one of skill in the art to the conclusion that the applicant was in possession of the claimed species is sufficient." MPEP § 2163.
In claims 1, 3-9, 12-17 & 19-20 broadly drawn to: An immobilized enzyme, wherein the immobilized enzyme is a Polyethyleneimine (PEI)-modified immobilized enzyme, and comprises: an enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) and/or a Formate Dehydrogenase (FDH); and a carrier, wherein the carrier is a cyanuric chloride-activated amino carrier (See claim 1 for example), or the method claims drawn to: A method for preparing an immobilized enzyme, comprising: activating an amino carrier with cyanuric chloride to obtain an activated carrier; and mixing and incubating an enzyme and the activated carrier for immobilization, and then modifying the immobilized product with Polyethyleneimine (PEI) to obtain the immobilized enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) and/or a Formate Dehydrogenase (FDH) (See claim 3, for example); there is no structure associated with function with regard to the members of genus claims.
No information, beyond the characterization of: An immobilized enzyme, wherein the immobilized enzyme is a Polyethyleneimine (PEI)-modified immobilized enzyme, and comprises: an enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) of SEQ ID NO: 1 and/or a Formate Dehydrogenase (FDH) of SEQ ID NO: 2; and an amino carrier ECR8409, LX-1000HA, or LX-1000EPHA; and where in the PEI has a molecular weight of 1.8-10 KDa.
The genus of AmDH or FDH polypeptides, amino carrier and PEI MW required in the claimed invention is an extremely large structurally and functionally variable genus. While the argument can be made that the recited genus of polypeptides is adequately described by the disclosure of the structures of SEQ ID NO: 1, 2, with specific structures amino carrier and PEI having the associated function/activity, since one could use structural homology to isolate those polypeptides and amino carrier and PEI MW recited in the claims to make the immobilized enzyme. The art clearly teaches the “Practical Limits of Function Prediction”:
(a) Devos et al., (Proteins: Structure, Function and Genetics, 2000, Vol. 41: 98-107), teach that the results obtained by analyzing a significant number of true sequence similarities, derived directly from structural alignments, point to the complexity of function prediction. Different aspects of protein function, including (i) enzymatic function classification, (ii) functional annotations in the form of key words, (iii) classes of cellular function, and (iv) conservation of binding sites can only be reliably transferred between similar sequences to a modest degree. The reason for this difficulty is a combination of the unavoidable database inaccuracies and plasticity of proteins (Abstract, page 98) and the analysis poses interesting questions about the reliability of current function prediction exercises and the intrinsic limitation of protein function prediction (Column 1, paragraph 3, page 99) and conclude that “Despite widespread use of database searching techniques followed by function inference as standard procedures in Bioinformatics, the results presented here illustrate that transfer of function between similar sequences involves more difficulties than commonly believed. Our data show that even true pair-wise sequence relations, identified by their structural similarity, correspond in many cases to different functions (column 2, paragraph 2, page 105). Our data show that even true pair-wise sequence relations, identified by their structural similarity, correspond in many cases to different functions (column 2, paragraph 2, page 105). Applicants’ are respectfully directed to the problems associated EC Classification in the section “Transferring the EC Classification enzyme to Non-Enzyme Comparisons”; pages 101-102 and Fig. 2a)-b), highlighting the structural and functional heterogeneity based on EC Classification numbers; as the stereo-specificity, substrate-specificity and catalytic properties vary widely.
(b) Whisstock et al., (Quarterly Reviews of Biophysics 2003, Vol. 36 (3): 307-340) also highlight the difficulties associated with “Prediction of protein function from protein sequence and structure”; “To reason from sequence and structure to function is to step onto much shakier ground”, closely related proteins can change function, either through divergence to a related function or by recruitment for a very different function, in such cases, assignment of function on the basis of homology, in the absence of direct experimental evidence, will give the wrong answer (page 309, paragraph 4), it is difficult to state criteria for successful prediction of function, since function is in principle a fuzzy concept. Given three sequences, it is possible to decide which of the three possible pairs is most closely related. Given three structures, methods are also available to measure and compare similarity of the pairs. However, in many cases, given three protein functions, it would be more difficult to choose the pair with most similar function, although it is possible to define metrics for quantitative comparisons of different protein sequences and structures, this is more difficult for proteins of different functions (page 312, paragraph 5), in families of closely related proteins, mutations usually conserve function but modulate specificity i.e., mutations tend to leave the backbone conformation of the pocket unchanged but to affect the shape and charge of its lining, altering specificity (page 313, paragraph 4), although the hope is that highly similar proteins will share similar functions, substitutions of a single, critically placed amino acid in an active-site residue may be sufficient to alter a protein’s role fundamentally (page 323, paragraph 1).
(c) This finding is reinforced in the following scientific teachings for specific proteins in the art that suggest, even highly structurally homologous polynucleotides and encoded polypeptides do not necessarily share the same function. For example, Witkowski et al., (Biochemistry 38:11643-11650, 1999), teaches that one conservative amino acid substitution transforms a b-ketoacyl synthase into a malonyl decarboxylase and completely eliminates b-ketoacyl synthase activity.
As stated above, No information, beyond the characterization of: An immobilized enzyme, wherein the immobilized enzyme is a Polyethyleneimine (PEI)-modified immobilized enzyme, and comprises: an enzyme, wherein the enzyme comprises an Amine Dehydrogenase (AmDH) of SEQ ID NO: 1 and/or a Formate Dehydrogenase (FDH) of SEQ ID NO: 2; and an amino carrier ECR8409, LX-1000HA, or LX-1000EPHA; and where in the PEI has a molecular weight of 1.8-10 KDa, which would indicate that they had possession of the claimed genus of polypeptides, amino carrier and PEI to assemble a Polyethyleneimine (PEI)-modified immobilized enzyme. As the claimed genera of polypeptides having widely variable structures and associated function, since minor changes in structure may result in changes affecting function and no additional information (species/variant/mutant) correlating structure with function has been provided. Furthermore, “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).
Therefore, one skilled in the art cannot reasonably conclude that applicant had possession of the claimed invention at the time the instant application was filed. Applicants are referred to the revised guidelines concerning compliance with the written description requirement of U.S.C. 112, first paragraph, published in the Official Gazette and also available at www.uspto.gov.
9. Claim Rejections - 35 USC § 112 (second paragraph)
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 2 & 8-20 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 pre-AIA the applicant regards as the invention.
Claims 2, 8-10 & 12-20 recite - the expression “preferably” (28 occurrences) which attempts to give both broad and narrow meaning to the scope of the above claims. These claims are unclear.
Claim 11 is included in the rejection for failing to correct the defect present in the base claim(s).
10. No claim is allowed.
11. Any inquiry concerning this communication or earlier communications from the examiner should be directed to TEKCHAND SAIDHA whose telephone number is (571)272-0940. The examiner can normally be reached on M-F 8.00-5.30. Examiner interviews are available via telephone, in-person, and video conferencing using a USPTO supplied web-based collaboration tool. To schedule an interview, applicant is encouraged to use the USPTO Automated Interview Request (AIR) at http://www.uspto.gov/interviewpractice.
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/TEKCHAND SAIDHA/
Primary Examiner, Art Unit 1652
Recombinant Enzymes, Hoteling
Telephone: (571) 272-0940
Fax: (571) 273-0940
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