DETAILED ACTION In application filed on 09 / 1 8 /202 3 , Claims 1 -10 are pending. The claim set submitted on 09/18/2023 is considered because this is the most recent claim set . Claims 1 -10 are considered in the current office 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. Drawings The drawings are objected to because certain reference characters in figures, not limited to Figures 1-2 are not legible. Drawings with improved resolution should be provided. Corrected drawing sheets in compliance with 37 CFR 1.121(d) are required in reply to the Office action to avoid abandonment of the application. Any amended replacement drawing sheet should include all of the figures appearing on the immediate prior version of the sheet, even if only one figure is being amended. The figure or figure number of an amended drawing should not be labeled as “amended.” If a drawing figure is to be canceled, the appropriate figure must be removed from the replacement sheet, and where necessary, the remaining figures must be renumbered and appropriate changes made to the brief description of the several views of the drawings for consistency. Additional replacement sheets may be necessary to show the renumbering of the remaining figures. Each drawing sheet submitted after the filing date of an application must be labeled in the top margin as either “Replacement Sheet” or “New Sheet” pursuant to 37 CFR 1.121(d). If the changes are not accepted by the examiner, the applicant will be notified and informed of any required corrective action in the next Office action. The objection to the drawings will not be held in abeyance. Specification The use of the term “BioStab Antibody Stabilizer” (See specification, Para 0027), which is 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. Claim Rejections - 35 USC § 112 Claims 1-10 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 1 recites the limitation "the liquid " in line 7; and “the reaction” in line 11. There is insufficient antecedent basis for this limitation in the claim. For the purpose of expedited prosecution, the limitation "the liquid " in line 7; and “the reaction” in line 11 is interpreted by the Examiner as " a liquid "; and “ a reaction ”. Moreover, Claims 2-10 are rejected by virtue of dependency on claim 1. Claim s 3-4 recites the limitation " the condition of incubating temperature ". There is insufficient antecedent basis for this limitation in the claim. For the purpose of expedited prosecution, the limitation "the condition of incubating temperature" is interpreted by the Examiner as " a condition of incubating temperature". Claim 5 recites the limitation " the main wavelength " in line 2; and “the reference wavelength” in line 3 . There is insufficient antecedent basis for this limitation in the claim. For the purpose of expedited prosecution, the limitation s " the main wavelength " in line 2; and “the reference wavelength” in line 3 are interpreted by the Examiner as " a main wavelength "; and “ a reference wavelength". Claim 6 recites the limitation " heat-dried 96-well plate" in line 20 . There is insufficient antecedent basis for this limitation in the claim. For the purpose of expedited prosecution, the limitation "heat-dried 96-well plate" is interpreted by the Examiner as " the 96-well plate". Moreover, Claims 7 -10 are rejected by virtue of dependency on claim 6 . Claim Rejections - 35 USC § 102 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 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 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. Claims 1-5 are rejected under 35 U.S.C. 102 (a) (1) as being anticipated by Niu et al. (CN114740205A) . Regarding Claim 1, Niu teaches a method for performing simplified ELISA operation, characterized by comprising the following steps: S1, preparing standards of a target protein (See Abstract… Dispase II) with gradient dilutions (See Page 3… Dispase II standard is diluted with diluent to 50ng/mL,25ng/mL, 12.5ng/mL, 6.25ng/mL, 3.125ng/mL, 1.56ng/mL) , and pre-diluting test samples (See Page 8 … The Dispase II antigen standard was serially diluted to 1.56-150ng/mL with different sample diluents, placed at 37°C for 3 days and 5 days, and the stability was determined, thereby teaching “ pre-diluting test samples” ) ; S2, setting up wells for standards and wells for test samples on an ELISA plate, adding 100 µ l of diluted standards and 100 µl of test samples into their respective wells (See Page 4 , 9 … add 100 µl of sample diluent to blank wells, add 100 µl of sample to be tested to sample wells) incubating , discarding the liquid, drying, and washing (See Page 4… for incubating, discarding the liquid, drying, and washing) ; S3, adding 100 µl of TMB chromogenic substrate (See Page 6… color developing solution B is TMB; See Page 4… Color development: Add 100 µl/well of pre-configured color developing solution to the ELISA plate, mix well, and incubate at 37°C for 15 minutes in the dark; equal volume mixing ) into each well of the standards / test samples, incubating at room temperature, adding 100 µl of stop solution to terminate the reaction in each well (See Page 6…Stop solution: 2mol/L concentrated H2SO4; See Page 4… Stop: Add stop solution at 100 µl/well) ; S4, placing the ELISA plate into an ELISA reader for dual-wavelength detection, reading test results based on the standards (See Page 4… Reading: Put the microplate plate into the microplate reader to measure the absorbance at dual wavelength 450/630nm (or single wavelength 450nm), and the reading is completed within 20min) , plotting OD curve of the standards, and calculating the concentration of the target substance in the samples (See Page 4…(9)Result processing: The average OD value of each standard product minus the OD value of the blank well is used as the correction value, the OD (OD450nm-OD630nm) value of the standard product is used as the dependent variable Y, and the standard product concentration is used as the independent variable X to make a curve; use Four-parameter Logistic mathematical model fitting equation: Y=((A-D)/(1+(x/C)^B))+D, the content of Dispase II in the sample is calculated by substituting the absorbance value of the sample OD (OD450nm- OD630nm) into the formula). Regarding Claim 2 , Niu teaches that in S1, the gradient dilutions comprise dilutions of 6 different concentrations (See Page 3…the dispase II standard is in the following concentrations: 50ng/mL, 25ng/mL, 12.5ng/mL, 6.25ng/mL, 3.125ng /mL, 1.56ng/mL series standard solution). Niu does not teach that the gradient dilutions comprise dilutions of 6 different concentrations. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including the number of data points for the standards in an ELISA calibration curve improves accuracy, precision, and the ability to fit complex, non-linear curves like 4-Parameter Logistic (4PL) or 5PL. Thus, the gradient dilutions comprising dilutions of 7 different concentrations is a result effective variables. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method where the gradient dilutions comprise dilutions of 7 different concentrations, for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page5). Regarding Claim 3, Niu teaches that in S2, the incubating is under the condition of incubating temperature at 37 °C, for 1 hour (See Page 4… and place at 37°C. Incubate 30-120min… incubate at 37°C for 30-120min; See Page 9… then place at 37°C Incubate for 1 h); and 1 X PBS-T solution is used as washing solution during the washing (See Page 3… After washing with PBST; Washing solution: 1×PBS with pH=7.4, containing 0.05% Tween-20). Regarding Claim 4 , Niu teaches that wherein in S3, the incubating is under the condition of incubating temperature at room temperature, for 5 - 15 minutes (See Page 4…Add 100 µl/well of pre-configured color developing solution to the ELISA plate, mix well, and incubate at 37°C for 15 minutes in the dark; equal volume mixing…the incubation time of the color developing solution was 15 min) ; and the stop solution is a sulfuric acid solution with a concentration of 2 M (See Page 3, 6, 9 and 13…The stop solution was 2mol/L concentrated H2SO4) . Niu does not teach that the stop solution is a sulfuric acid solution with a concentration of 1 M. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including the concentration of the stop solution which is a sulfuric acid solution affects speed at which the reaction is terminated, where a concentration of 0.5M to 2M is typical, with higher concentrations (e.g., 2M) ensuring a faster, more complete stop, whereas lower concentrations (0.18M–0.5M) might result in slower inhibition. Thus, the stop solution is a sulfuric acid solution with a concentration of 1 M is a result effective variable. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method where the concentration of 1 M of the stop solution which is a sulfuric acid solution , for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page 5). Regarding Claim 5 , Niu teaches that wherein in S4, the main wavelength for dual-wavelength detection is 450 nm (‘450nm’) , and the reference wavelength is 570 nm or 630 nm (‘630 nm’) (See Page 4…absorbance at dual wavelength 450/630nm (or single wavelength 450nm) … the OD (OD450nm-OD630nm)). 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 35 U.S.C. 103 which forms the basis for all obviousness rejections set forth in this Office action: A patent for a claimed invention may not be obtained, notwithstanding that the claimed invention is not identically disclosed as set forth in section 102, if the differences between the claimed invention and the prior art are such that the claimed invention as a whole would have been obvious before the effective filing date of the claimed invention to a person having ordinary skill in the art to which the claimed invention pertains. Patentability shall not be negated by the manner in which the invention was made. The factual inquiries for establishing a background for determining obviousness under 35 U.S.C. 103 are summarized as follows: 1. Determining the scope and contents of the prior art. 2. Ascertaining the differences between the prior art and the claims at issue. 3. Resolving the level of ordinary skill in the pertinent art. 4. Considering objective evidence present in the application indicating obviousness or nonobviousness. 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 6-9 are rejected under 35 U.S.C. 103 as being unpatentable over by Niu et al. (CN114740205A) in view of Peng et al. (CN107167590A). Regarding Claim 6, Niu teaches that the preparing method of the ELISA plate comprising the following steps: Step 1, diluting the capturing antibodies of the target protein to a working concentration (‘(See Page 7… ‘ concentrations, namely 1ug/ml, 2ug/ml,’) by using PBS buffer, adding 50 µl of the PBS buffer per well into a 96-well plate (See Page 7…coating plate; See Page 4…The 96-well microtiter plate) , and incubating overnight at 4 o C so as to coat (See Page 7… Dilute the purified coated antibody with coating solution to 2 concentrations, namely 1ug/ml, 2ug/ml, 100µl per well, 4 ℃ after being washed with PBST overnight) ; Step 2, discarding the excess liquid, drying, (See Page 9…after washing the plate, put the ELISA plate upside down on clean absorbent paper, and pat to remove the residual washing liquid) and adding 300 µ l of 5% BSA solution to each well, placing at room temperature for 2 hours ( See Page 3…After washing with PBST, the blocking solution also contains 1% (v/v) BSA…add 200 µl/well of blocking solution to block and incubate at 37°C for 120 min; See Page 9…Blocking: after washing the plate, add 200 µl of blocking solution to each well, seal the plate with a sealing film, and incubate at 37°C for 2 hours ; See Page 7…after washing with PBST, 200ul of different blocking solutions were added to block ); Step 3, discarding the liquid, drying, adding water solution containing sucrose, trehalose, and gelatin (See Page 7… containing 2% gelatin ) to each well, placing at room temperature for a time , discarding the excess liquid, tap-drying (See Page 9…After washing the plate, add 200 µl of stabilizer to each well, seal the plate with a sealing film, and incubate at room temperature for 2 hours. Spin dry the stabilizer, blow dry for 5h, and vacuum and plastic seal; See Page 3…add 200 μl/well of stabilizer to incubate at room temperature for 120 min; 5h, vacuum and plastic seal ; See Page 8…after washing, add stabilizer to stand at room temperature for 2hours, spin dry the stabilizer, and blast dry for 4 hours; See Page 9…Stabilizer 1:5% sucrose solution; Stabilizer 2: 5% trehalose solution ) ; Step 4, diluting detecting antibodies of a target protein to a working concentration using an antibody stabilizer (‘BSA’) (See Page 3…Enzyme-labeled antibody: HRP-rabbit polyclonal antibody diluted 1:2000-1:20000; sample diluent: 1×PBS with pH=7.4, containing 0.05% Tween-20, containing BSA with PBST volume of 0.5%) , so as to form antibody microspheres (See Page 3…Enzyme-labeled antibody: HRP-rabbit polyclonal antibody diluted 1:2000-1:20000; sample diluent: 1×PBS with pH=7.4, containing 0.05% Tween-20, containing BSA with PBST volume of 0.5%) ; and forming HRP enzyme microspheres with HRP enzyme (See Page 3…the enzyme-labeled antibody is an HRP-rabbit polyclonal antibody ; See Page 7… HRP-labeled enzyme-labeled antibody ). Examiner further submits that the claimed “so as to form antibody microspheres” is viewed as a result, purpose, or intended function of a previously described step “diluting detecting antibodies of a target protein to a working concentration using an antibody stabilizer” and the antibody microspheres is formed as a result of the interaction of the Enzyme-labeled antibody with BSA. See MPEP 2111.04; Step 5, placing the microspheres (See Page 3…Enzyme-labeled antibody: HRP-rabbit polyclonal antibody diluted 1:2000-1:20000…containing BSA with PBST volume of 0.5%) obtained in Step 4 into heat-dried 96-well plate obtained in Step 3, so as to obtain the ELISA plate ( See Page 4…The 96-well microtiter plate was coated with the capture antibody to make a solid-phase antibody. Then the standard and detection samples were added, and then horseradish peroxidation was added. The enzyme-labeled labeled antibody forms a solid phase antibody-Dispase II-labeled antibody sandwich conjugate, washed after the reaction, and then the substrate is added to carry out the color reaction. The substrate is converted into blue under the catalysis of HRP, …) . Niu does not explicitly teach 300 µl of the water solution containing sucrose, trehalose, and gelatin to each well, placing at room temperature for 15 minutes” . In the analogous art of a plate chemiluminescent immunoassay kit of a carbohydrate antigen 242, Peng teaches a water solution containing sucrose, trehalose, and gelatin to each well, placing at room temperature” (See Page 3…Using sucrose, trehalose and fish skin gelatin as stabilizing systems, the coated plates provide enhanced resistance to high temperatures and dryness, ensuring resistance Biotin antibody coated plate performance; See Page 8…0.1 M pH7.4 TBS buffer, 0.3% BSA, 1% sheep serum, 0.1% Proclin 300 (v / v), 1% fish skin gelatin, 2% trehalose and 10% sucrose was formulated as a blocking solution to wash After the coating plate, the closed volume of 150µL per well, the closure temperature of 37 ± 1 ℃ , the closure time of 2 to 5 hours). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have the method of Niu to incorporate a water solution containing sucrose, trehalose, and gelatin to each well, placing at room temperature”, as taught by Peng for the benefit of preparing a blocking solution for a chemiluminescence plate detection kit (Peng, Page 12-13), allowing for the provision of the plate chemiluminescent immunoassay kit has the advantages that the plate chemiluminescent immunoassay kit is designed mainly based on chemiluminescent immunoassay, and through introduction of an anti-biotin antibody-biotin system, kit detection specificity is stabilized, detection sensitivity is enhanced and detection time is prolonged; a high-temperature oscillatory type anti-biotin antibody coating technology is improved, and accordingly antibody/antigen consumption is reduced, reagent production is simplified and a production period is shortened (Peng, Abstract). Regarding the volume of 300 µl of the water solution and a room temperature for 15 minutes”. MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including temperature and reagent volumes are critical for maximizing binding kinetics, ensuring high signal-to-noise ratios, and achieving reproducible, accurate results. Thus, the volume of 300 µl of the water solution and a room temperature for 15 minutes” are a result effective variables. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method having a volume of 300 µl of the water solution and a room temperature for 15 minutes, as taught by Peng for the benefit of preparing a blocking solution for a chemiluminescence plate detection kit (Peng, Page 12-13), allowing for the provision of the plate chemiluminescent immunoassay kit has the advantages that the plate chemiluminescent immunoassay kit is designed mainly based on chemiluminescent immunoassay, and through introduction of an anti-biotin antibody-biotin system, kit detection specificity is stabilized, detection sensitivity is enhanced and detection time is prolonged; a high-temperature oscillatory type anti-biotin antibody coating technology is improved, and accordingly antibody/antigen consumption is reduced, reagent production is simplified and a production period is shortened (Peng, Abstract). Regarding Claim 7 , the method of claim 6 is obvious over Niu in view of Peng . Niu teaches that wherein in Step 1, the working concentration is 1 or 2 µ g/ml (See Page 7… Dilute the purified coated antibody with coating solution to 2 concentrations, namely 1ug/ml, 2ug/ml, 100µl per well, 4 ℃ after being washed with PBST overnight) . The combination of Niu and Peng does not explicitly teach that the working concentration is 1 or 2 µg/ml. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including the concentration of the capture antibodies directly impacts sensitivity, background noise, and the linear range of detection. Thus, the concentration of the capture antibodies is a result effective variable. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method where the working concentration is 10-20 µg/ml for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page 5). Regarding Claim 8 , the method of claim 6 is obvious over Niu in view of Peng . The combination of Niu and Peng does not teach that wherein in Step 3, the mass concentration of sucrose in the water solution is 30%, the mass concentration of trehalose is 10%, and the mass concentration of gelatin is 5%. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including reagent concentrations are critical for maximizing binding kinetics, ensuring high signal-to-noise ratios, and achieving reproducible, accurate results. Thus, “ the mass concentration of sucrose in the water solution is 30%, the mass concentration of trehalose is 10%, and the mass concentration of gelatin is 5% ” are a result effective variables. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method incorporating that the mass concentration of sucrose in the water solution is 30%, the mass concentration of trehalose is 10%, and the mass concentration of gelatin is 5% , for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page 5). Regarding Claim 9 , the method of claim 6 is obvious over Niu in view of Peng . The combination of Niu and Peng does not teach that wherein in Step 3, the drying is under the temperature of 20 °C, for 2 hours. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including temperature and process time are critical for maximizing binding kinetics, ensuring high signal-to-noise ratios, and achieving reproducible, accurate results. Thus, “ wherein in Step 3, the drying is under the temperature of 20 °C, for 2 hours ” are a result effective variables. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method incorporating that wherein in Step 3, the drying is under the temperature of 20 °C, for 2 hours , for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page 5). Claim 10 is rejected under 35 U.S.C. 103 as being unpatentable over by Niu et al. (CN114740205A) in view of Peng et al. (CN107167590A) as applied to claim 6 above, and further in view of Abolnik et al. ( US 20210349092A1 ) Regarding Claim 10 , the method of claim 6 is obvious over Niu in view of Peng . The combination of Niu and Peng does not teach that wherein in Step 4, the antibody stabilizer is BioStab antibody stabilizer. In the analogous art of a method of detecting the presence of an antibody to an avian influenza hemagglutinin antigen in a sample from a subject and to a device for assaying the presence of an antibody to avian influenza hemagglutinin antigen in a sample from a subject, Abolnik teaches the use of BioStab Antibody Stabilizer (See Para 0160-0161… Protein Coupling to HRP (Secondary Antibody Conjugate and DAS Labelled Antigen)… After the incubation step with LL-quencher, and equal volume of BioStab Antibody Stabilizer (Sigma Life Science, Germany) was added, and the conjugates were stored at 4° C.). It would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to have modified a method of Niu and Peng to use wherein in Step 4, the antibody stabilizer is BioStab antibody stabilizer, as taught by Abolnik for the benefit of facilitating protein coupling to HRP (secondary antibody conjugate and DAS labelled antigen) (Abolnik, Para 0160-0161), allowing for the provision of a device for assaying the presence of an antibody to avian influenza hemagglutinin antigen in a sample from a subject (Abolnik, Abstract). The combination of Niu, Peng and Abolnik does not explicitly teach “wherein in Step 4, the antibody stabilizer is BioStab antibody stabilizer, with a working concentration of 1 - 100 ng/ml; the particle size of the antibody microspheres is 1 - 5 mm, and the particle size of the HRP enzyme microspheres is 1 - 5 mm ”. However, MPEP § 2144.05, Part II, Subpart B holds that a particular parameter that is recognized as a result effective variable (“a variable that achieves a recognized result”) would be one, but not the only motivation for a person of ordinary skill in the art to experiment to reach another workable product or process. In the development of ELISA methods, the selection of optimal experimental conditions including the antibody stabilizer which is BioStab antibody stabilizer, with a working concentration of 1 - 100 ng/ml directly impacts sensitivity, background noise, and the linear range of detection. Also, optimal experimental conditions including the particle size of the antibody microspheres is 1 - 5 mm, and the particle size of the HRP enzyme microspheres is 1 - 5 mm” impacts reaction kinetics, sensitivity, and efficiency. Smaller particles generally increase enzyme reaction rates and efficiency, while larger particles can hinder diffusion. Proper size management ensures higher surface area, enhancing detection and reducing steric hindrance, crucial for optimizing antibody-enzyme conjugates. Thus, the antibody stabilizer is BioStab antibody stabilizer, with a working concentration of 1 - 100 ng/ml; the particle size of the antibody microspheres is 1 - 5 mm, and the particle size of the HRP enzyme microspheres is 1 - 5 mm” are a result effective variables. Therefore, it would have been obvious to one of ordinary skill in the art before the effective filing date of the claimed invention to develop an ELISA method incorporating that “wherein in Step 4, the antibody stabilizer is BioStab antibody stabilizer, with a working concentration of 1 - 100 ng/ml; the particle size of the antibody microspheres is 1 - 5 mm, and the particle size of the HRP enzyme microspheres is 1 - 5 mm”, for the benefit of providing a special kit having characteristics of good specificity, sensitivity and stability (Niu, Page 2) which is used for quantitative detection of Dispase II in cell culture or biomedicine production (Niu, Page 5). Conclusion Any inquiry concerning this communication or earlier communications from the examiner should be directed to FILLIN "Enter examiner's name" \* MERGEFORMAT OYELEYE ALEXANDER ALABI whose telephone number is FILLIN "Phone number" \* MERGEFORMAT (571)272-1678 . The examiner can normally be reached on FILLIN "Work schedule?" \* MERGEFORMAT M-F 7:30am-5:30pm . 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, FILLIN "SPE Name?" \* MERGEFORMAT Lyle Alexander can be reached on FILLIN "SPE Phone?" \* MERGEFORMAT (571) 272-1254 . 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 https://ppair-my.uspto.gov/pair/PrivatePair. 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. /OYELEYE ALEXANDER ALABI/ Examiner, Art Unit 1797