Prosecution Insights
Last updated: April 19, 2026
Application No. 17/934,700

METHODS FOR ENVIRONMENTAL CHITIN QUANTIFICATION

Non-Final OA §103
Filed
Sep 23, 2022
Examiner
HAQ, SHAFIQUL
Art Unit
1678
Tech Center
1600 — Biotechnology & Organic Chemistry
Assignee
Arizona Board of Regents
OA Round
1 (Non-Final)
64%
Grant Probability
Moderate
1-2
OA Rounds
3y 8m
To Grant
99%
With Interview

Examiner Intelligence

Grants 64% of resolved cases
64%
Career Allow Rate
599 granted / 928 resolved
+4.5% vs TC avg
Strong +56% interview lift
Without
With
+56.1%
Interview Lift
resolved cases with interview
Typical timeline
3y 8m
Avg Prosecution
27 currently pending
Career history
955
Total Applications
across all art units

Statute-Specific Performance

§101
2.5%
-37.5% vs TC avg
§103
36.9%
-3.1% vs TC avg
§102
13.8%
-26.2% vs TC avg
§112
29.9%
-10.1% vs TC avg
Black line = Tech Center average estimate • Based on career data from 928 resolved cases

Office Action

§103
Notice of Pre-AIA or AIA Status The present application is being examined under the pre-AIA first to invent provisions. DETAILED ACTION Response to Election/Restrictions Applicant’s election with traverse of Group II (claims 11-17) is acknowledged. Applicant’s traversal is on the ground that any prior art searched for one group is applicable to the other group and hence, there would not be a serious search and/or examination burden. The above arguments have fully been considered but are not found persuasive. As described in items 3-5 of the restriction requirements mailed August 12, 2025, each of the groups are distinct and there would be a serious search and/or examination burden if restriction were not required. Non-coextensive searches of the patent and non-patent literature would be necessary. As for example, claim 1 (Group I) would require search for conversion of conversion of Chitin to Chitosan with heating in alkaline solution, which is not required from claim 11 process as conversion with enzyme would fulfil the process step and moreover, the process steps of Group II and distinct from the process of Group I invention and each, would require distinct prior art searches. Therefore, the restriction requirement deemed proper and is made FINAL. Therefore, claims 1-10 and 18-20 are withdrawn from further consideration as being directed to a non-elected invention. See 37 CFR 1.142(b) and MPEP § 821.03. Applicants preserve their right to file a divisional on the non-elected subject matter. Claims 11-17 are examined on merits in this office action. Claim Rejections - 35 USC § 103 In the event the determination of the status of the application as subject to AIA 35 U.S.C. 102 and 103 (or as subject to pre-AIA 35 U.S.C. 102 and 103) is incorrect, any correction of the statutory basis (i.e., changing from AIA to pre-AIA ) for the rejection will not be considered a new ground of rejection if the prior art relied upon, and the rationale supporting the rejection, would be the same under either status. The following is a quotation of pre-AIA 35 U.S.C. 103(a) which forms the basis for all obviousness rejections set forth in this Office action: (a) A patent may not be obtained though the invention is not identically disclosed or described as set forth in section 102, if the differences between the subject matter sought to be patented and the prior art are such that the subject matter as a whole would have been obvious at the time the invention was made to a person having ordinary skill in the art to which said subject matter pertains. Patentability shall not be negated by the manner in which the invention was made. Claims 11-17 are rejected under pre-AIA 35 U.S.C. 103(a) as being unpatentable over Ayliffe et al in view of Laine et al (US 5,914,239). In regards to claims 11 and 12, Ayliffe teaches quantitative assay of Chitin in fungal biomass (environmental sample) wherein wheat germ agglutinin conjugated to a fluorophore is utilized in the detection process (Abstract). Ayliffe teaches that the process includes autoclaving the sample in 1M KOH , neutralized in 50mM Tris (pH 7.0), stained with WGA-FITC, washed to remove unbound stain prior to quantifying fluorescence (1st column on page 659) and measuring output of the chitosan sample to a standardized curve (Fig.1). The process of autoclaving the sample in 1M KOH would encompass the process of converting chitin in the environmental sample to chitosan because Ayliffe teaches that the process would include fragmentation of chitin particles and some chitin deacetylation (page 660). Ayliffe teaches that increase of chitin staining in KOH/autoclaved sample which is likely due to fragmentation of the chitin particles during autoclaving providing a greater surface area of exposed chitin (page 660, lines 12-14 of 2nd col.). The process of staining includes adding of WGA-FITC (i.e. chitin binding agent conjugated to a reporter). Therefore, the process of Ayliffe differ from the process of instant claim 11 by not utilizing substrate surface comprising chitin binding agent disposed thereon for immobilizing chitin in the sample on the substrate surface. That is, Ayliffe does not disclose adding chitosan mixture to a substrate comprising a first chitin binding agent disposed thereon and incubating the chitosan mixture. Laine is directed to diagnosis of fungal infection utilizing chitin-binding lectin (Title). Laine teaches that chitovibrin (a chitin binding lectin) has a strong affinity for chitin and is useful for detection of the presence of chitin, particularly in diagnosing fungal infections in humans, animal and plant material (Abstract). Laine teaches ELISA based detection with the chitin binding lectin and the process comprises contacting sample with immobilized chitovibrin, rinsing unbound sample away, binding adherent chitin to enzyme-linked chitovibrin (for example, a chitovibrin linked to horseradish peroxidase), washing away of the unbound enzyme-linked chitovibrin and detecting chitin by detecting the linked enzyme with a suitable substrate Col. 5, 2nd para and claim 1-5). Therefore, from the description in mind of Laine, one of ordinary skilled in the art can easily envisage including immobilization step of adding autoclaved neutralized mixture of Ayliffe on a substrate comprising chitin binding agent (as for example, WGA or chitovibrin) with the expectation of immobilizing chitin from the sample for carrying out detection with a solid phase-based system. On or ordinary skilled in the art would understand that immobilization would facilitate washing of unbound substances and since Ayliffe teaches washing of unbound stains prior to quantifying, one of ordinary skilled in the art would easily envisage alternative embodiment of detection utilizing solid-phase based system. From the description in mind of Laine, one of ordinary skilled in the art can easily envisage immobilizing chitin binding agent WGA or Chitovibrin on a substrate surface for utilizing the substrate for binding of chitin from the chitosan mixture for the solid phase-based system (ELISA) with a reasonable expectation of success. In regards to claim 13, as described above, Laine teaches ELISA based detection with the chitin binding lectin and the process comprises contacting sample with immobilized chitin binding agent and rinsing unbound sample away, which removes any unbound substances and the combination of Ayliffe and Laine provides obviousness of the method steps. In regards to claim 14, both Ayliffe and Laine teaches chitin binding lectin wherein Ayliffe teaches chitin binding lectin Wheat Germ Agglutinin (WGA) and Laine teaches chitin binding lectin Chitovibrin. In regards to claim 15, as described above, Ayliffe teaches chitin binding lectin which is Wheat Germ Agglutinin (WGA). In regards to claims 16 and 17, Ayliffe teaches chitin binding lectin comprising a fluorescent reporter alexa488 or fluorescein isothiocyanate (FITC) and Laine teaches the chitin binding lectin comprising a fluorescent reporter or an enzyme reporter wherein the enzyme reporter is horseradish peroxidase. Laine teaches that Chitovibrin may be coupled to fluorescein isothiocyanate (FITC) or an enzyme linked system such as horseradish peroxidase, alkaline phosphatase or β-galactosidase. Thus, various reporter system including fluorescent reporter and enzyme reporter with chitin binding lectin would be obvious to one or ordinary skilled in the art. Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to SHAFIQUL HAQ whose telephone number is (571)272-6103. The examiner can normally be reached on Mon-Fri 8-4:30. 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. If attempts to reach the examiner by telephone are unsuccessful, the examiner’s supervisor, Gregory S. Emch can be reached on 571-272-8149. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300. Information regarding the status of an application may be obtained from the Patent Application Information Retrieval (PAIR) system. Status information for published applications may be obtained from either Private PAIR or Public PAIR. Status information for unpublished applications is available through Private PAIR only. For more information about the PAIR system, see http://pair-direct.uspto.gov. Should you have questions on access to the Private PAIR system, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative or access to the automated information system, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000. /SHAFIQUL HAQ/Primary Examiner, Art Unit 1678
Read full office action

Prosecution Timeline

Sep 23, 2022
Application Filed
Jan 13, 2026
Non-Final Rejection — §103 (current)

Precedent Cases

Applications granted by this same examiner with similar technology

Patent 12590953
METHODS FOR SCREENING CEREBLON MODIFYING COMPOUNDS
2y 5m to grant Granted Mar 31, 2026
Patent 12590120
MATERIALS AND METHODS FOR ISOLATING SELF-ANTIGEN POLYPEPTIDES
2y 5m to grant Granted Mar 31, 2026
Patent 12577266
PROTEIN PROXIMITY ASSAY IN FORMALIN FIXED PARAFFIN EMBEDDED TISSUE USING CAGED HAPTENS
2y 5m to grant Granted Mar 17, 2026
Patent 12565680
CANCER NEOANTIGENS AND THEIR UTILITIES IN CANCER VACCINES AND TCR-BASED CANCER IMMUNOTHERAPY
2y 5m to grant Granted Mar 03, 2026
Patent 12559511
PROTEIN PROXIMITY ASSAY IN FORMALIN FIXED PARAFFIN EMBEDDED TISSUE USING CAGED HAPTENS
2y 5m to grant Granted Feb 24, 2026
Study what changed to get past this examiner. Based on 5 most recent grants.

AI Strategy Recommendation

Get an AI-powered prosecution strategy using examiner precedents, rejection analysis, and claim mapping.
Powered by AI — typically takes 5-10 seconds

Prosecution Projections

1-2
Expected OA Rounds
64%
Grant Probability
99%
With Interview (+56.1%)
3y 8m
Median Time to Grant
Low
PTA Risk
Based on 928 resolved cases by this examiner. Grant probability derived from career allow rate.

Sign in with your work email

Enter your email to receive a magic link. No password needed.

Personal email addresses (Gmail, Yahoo, etc.) are not accepted.

Free tier: 3 strategy analyses per month