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
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office Action.
Status of Claims
Claims 1-3, 6-10, 13, 14 and 16-25 are currently pending. Claims 1-3, 6-10, 13, 14 and 16-20 have been amended by Applicants’ amendment filed 04-02-2026. Claims 4, 5, 11, 12, and 15 have been canceled by Applicant’s amendment filed 04-02-2026. Claims 21-25 have been added by Applicants’ amendment filed 04-02-2026.
Applicant's election with traverse of Group I, claims 1-8, directed to a data system, in the reply filed on November 25, 2025 is acknowledged; and Applicant’s election of Species as follows:
Species (A): wherein the system of claim 1 further comprises a reader configured to identify the different combinations of the plurality of different plant-based molecules (claim 2); and
Species (B): wherein the method of claim 17 further comprises (claim 18), during the telephone interview held on December 10, 2025 was previously acknowledged.
Claims 9-20 were previously withdrawn, and claims 24 and 25 are newly withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected invention, there being no allowable generic or linking claim. Applicant timely traversed the restriction (election) requirement in the reply filed on October 22, 2025.
Claims 4-8 were previously withdrawn, and claims 21 and 22 are newly withdrawn from further consideration pursuant to 37 CFR 1.142(b) as being drawn to a non-elected species, there being no allowable generic or linking claim.
Please Note: Claims 21 and 22 depend from instant claim 1. In the response to the Election/ Restriction requirement, Applicant elected claim 2 (further comprising a reader). Claim 21 is directed to grid elements further comprising labels; and claim 22 is directed to the system further comprising an adhesive. Thus, claims 21 and 22 are withdrawn as being directed to a non-elected species.
A complete reply to the final rejection must include cancellation of nonelected claims or other appropriate action (37 CFR 1.144) See MPEP § 821.01.
Therefore, claims 1-3 and 23 are under consideration to which the following grounds of rejection are applicable.
Priority
The present application filed June 20, 2022, claims the benefit of US Provisional Patent Application 63/213946, filed June 23, 2021.
Interview Summary
Applicant contacted the Examiner to set up an interview, where such telephonic interview was conducted between the Examiner and Applicant’s representatives Alina Kalb on March 25, 2026, where the species election and potential amendments to claim 1 were discussed.
Withdrawn Objections/Rejections
Applicants’ amendment and arguments filed April 2, 2026 are acknowledged and have been fully considered. The Examiner has re-weighed all the evidence of record. Any rejection and/or
objection not specifically addressed below are herein withdrawn.
Drawing Objection
The objections to the drawings are withdrawn due to Applicant’s amendment of the Specification at paragraph [0031], in the reply filed 04-02-2026.
Claim Rejections - 35 USC § 112(d)
The rejection of claim 2 is withdrawn under 35 U.S.C. 112(d) 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 due to Applicant’s amendment of claim 1, in the reply filed 04-02-2026.
Due to the withdrawn rejection, Applicant’s arguments are rendered moot.
Claim Rejections - 35 USC § 102
The rejection of claims 1-3 is withdrawn under 35 U.S.C. 102(a1)/102(a2) as being anticipated by Gupta et al. (hereinafter “Gupta”) (Journal of Biosciences, 2014, 39(5), 931-944).
Gupta does not specifically exemplify a glass plate.
In view of the withdrawn rejection, Applicant’s arguments are rendered moot.
The rejection of claims 1-3 is withdrawn under 35 U.S.C. 102(a1)/(a2) as being anticipated by Horwath et al. (hereinafter “Horwath”) (US Patent Application Publication 20020273024, published November 21, 2002).
Horwath does not specifically exemplify a molecule generator.
In view of the withdrawn rejection, Applicant’s arguments are rendered moot.
Maintained Objections/Rejections
Claim Rejections - 35 USC § 112(b)
The rejection of claims 1-3 is maintained, and claim 23 is newly rejected under 35 U.S.C. 112(b) as being indefinite for failing to particularly point out and distinctly claim the subject matter which applicant regards as the invention.
Claim 1 is indefinite for the recitation of the term “freeze-tolerant data storage medium” such as recited in claim 1, line 10 because the term “freeze-tolerant” is a relative term that renders the claim indefinite. The term “freeze-tolerant” is not defined by the claim, and the Specification does not provide a standard for ascertaining the requisite amount of ‘tolerance’ as compared to some other value that qualifies as being a “freeze-tolerant” data storage medium, such that one of ordinary skill in the art would not be reasonably appraised of the scope of the invention. Moreover, the meaning of the term “freeze-tolerant” is unclear, such that it is unclear whether the term refers to a data storage medium that has an ability to maintain its shape or do not crack at temperatures below 32oF, the reduction or absence of ice crystals at certain temperatures for a specific period of time, or whether the term refers to something else and, thus, the metes and bounds of the claim cannot be determined.
Claim 23 is indefinite for the recitation of the term “antifreeze protein” such as recited in claim 23, line 1. There is insufficient antecedent basis for the term “antifreeze protein” in the claim because claim 1, line 12 recites the term “a plant-based antifreeze protein.” Moreover, instant claim 23 depends from claim 1, where claim 1 does not recite “antifreeze proteins” including antifreeze proteins derived from plants. The Examiner suggests that Applicant amend the claim to recite, for example, “wherein the plant-base antifreeze protein is derived from Arecaceae.”
Claim 23 is indefinite for the recitation of the term “antifreeze protein is derived from Arecaceae” such as recited in claim 23, lines 1-2 because the instant as-filed Specification and original claims do not teach or recite a single antifreeze protein derived from Arecaceae, and/or the use of an antifreeze protein derived from Arecaceae to coat glass as an antifreeze layer. Instead, the as-filed Specification teaches that: “molecules that are similar to molecules found in Arecaceae are generated and utilized to represent data, and media having antifreeze properties of Arecaceae are developed and utilized to store the generated molecules” paragraph [0015]; “molecules that are formed using amino acids found in Arecaceae” (paragraph [0020]); and “a glass plate, with one or more surfaces of the glass plate coated with an antifreeze layer (e.g., an antifreeze protein (AFP)) similar to chemical properties of Arecaceae” (paragraph [0024]), where it is known that all plant proteins comprise the amino acids found in Arecaceae as evidenced by Kumar (pg. 198, col 1, first full paragraph, lines 1-5), such that it appears that molecules having antifreeze properties are used for coating and/or storage, but that AFPs from Arecaceae are not specifically used in the method and, thus, the metes and bounds of the claim cannot be determined.
Claims 2 and 3 are indefinite insofar as they ultimately depend from instant claim 1.
New Objections/Rejections
Claim Rejections - 35 USC § 112(d)
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 23 is rejected under 35 U.S.C. 112(d) 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. This is a new rejection necessitated by amendment of the claims in the response filed 04-02-2026.
Claim 23 recites (in part): “wherein antifreeze protein is derived from Arecaceae” in lines 1-2 because instant claim 23 depends from claim 1, where claim 1 does not recite “antifreeze proteins” including antifreeze proteins derived from plants. Thus, claim 23 is an improper dependent claim 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.
Applicant may cancel the claim, amend the claim to place the claim in proper dependent form, rewrite the claim in independent form, or present a sufficient showing that the dependent claim complies with the statutory requirements.
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 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 may not be obtained though the invention is not identically disclosed or described as set forth in section 102 of this title, 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 negatived by the manner in which the invention was made.
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 1-3 and 23 are rejected under 35 U.S.C. 103 as being unpatentable over Ba et al. (hereinafter “Ba”) (US Patent Application Publication No. 20200344998, published November 5, 2020) in view of Jacobson et. al. (hereinafter “Jacobson”) (US Patent No. 10982208, issued April 20, 2021; US20200181604, published June 11, 2020). This is a new rejection necessitated by amendment of the claims in the response filed 04-02-2026.
Regarding claims 1 (in part) and 23, Ba teaches modified antifreeze proteins having the formula AFP-PEG, where AFP is an antifreeze protein, PEG is a poly(alkylene glycol) unit, and the PEG is linked to an amino acid residue in the AFP that is not involved in direct ice-surface binding and that has a functional group selected from an amine, a thiol, a hydroxy, a carboxylate, an amide and a guanidine in its side chain; as well as, a formulation including the same, a method of protecting a biological tissue, organ or body using the same, and a method of synthesizing a modified antifreeze proteins (interpreted as freeze-tolerant data storage medium; AFP; encompassing AFP-derived from Arecaceae; and molecules formed from amino acids, claim 1) (Abstract). Ba teaches that antifreeze proteins (AFPs) are found in various organisms including fish, insects and plants to protect living cells from freezing damages in subzero environments (interpreted proteins and peptides as freeze-tolerant storage medium; and plant-based AFP, claim 1) (paragraph [0002]). Ba teaches that plant AFPs include AFPs from winter rye (Secale cereale L.) and ryegrass (Lolium perenne) [Worral et al., Science, 282, (1998), 115-117; Side-bottom et al., Nature, 406, (2000), 256] (interpreted as plant-based AFP; and encompassing Arecaceae, claims 1 and 23) (paragraph [0004]). Ba teaches that synthetic approaches can be applied to any AFP having an amino acid with an amine or thiol functional group, wherein: (1) PEG groups can be attached to amino acid residues with other functional groups; and (2) other AFP types (e.g., Type-I, Type-II, Type-IV, insect, plant, a recombinant version of a naturally-occurring AFP, synthetic [e.g., comprising or consisting essentially of known repeating units of known AFPs, such as [Thr-Ala-Ala ]n where n is 3 or more [e.g., 4, 5, 6, 8, 10 or 12] and optionally 30 or less [e.g., 20, 15 or 12], etc.) having one or more amino acids with an amine, thiol, hydroxy, carboxylate, amide, guanidine or other functional group can be pegylated using any of the pegylation techniques disclosed herein or other pegylation technique known to those skilled in the art (interpreting synthetic approaches as a molecule generator; and as plant-based AFPs, claim 1) (paragraph [0061]). Ba teaches that antifreeze active mutants of AFPs can be used to make the PEGylated AFPs, wherein the mutants can be made by chemical synthesis, such as solid-phase synthesis of peptides and proteins (paragraph [0135], lines 1-4). Ba teaches the determination of antifreeze activities of the Pegylated Type-III AFPs using an Ortago Osmometer, a thermoelectric temperature controlling device, with a temperature-controlled cooling stage, and an Olympus BX 51 microscope (maximum magnification of 800 times with resolution of 1 micron) as well as a RETIGA 2000R Color Video Camera were used to determine the antifreeze activities (interpreting the microscope and video camera as readers configured to identify different combinations of different molecules made from amino acids, claim 2) (paragraph [0066]). Ba teaches a metal disk which has 6 holes with a diameter of 0.6 mm each was used to hold the samples, wherein type B immersion oil was placed in the bottom of each hole, to the surface of the sidewall of the hole; and an AFP sample solution (around 0.1-0.15 microliters) was added to the top of the type B oil in each hole, then type A oil was finally added; and the whole thermal stage was covered with a glass sheet which was sealed with vacuum grease, wherein the thermal stage was placed on top of the microscope stage; and the temperature controller was then set to the flash freezing mode, such that a target temperature of below -20° C for bulk freezing and temperature reduction rate of 0.1 ° C was set (interpreted as storage container comprising grid elements; AFPs comprising an antifreeze layer; a glass plate; and interpreting the controller as a reader, claim 1) (paragraph [0067]). Ba teaches that Figure 7A shows a MALDI TOF mass spectrum of crude pegylated Type-III AFPs with mPEG-SG (2,000 Da) including a 10:1 molar ratio of mPEG-SG to wild-type Type-III AFP and a buffer having a pH=7.4 were used; and the MALDI TOF mass spectrum in Figure 7 shows that both single pegylated Type-III AFPs (interpreted as a ready configured to identify a molecular weight; and a plurality of different molecules formed from amino acids, claims 1 and 3) (paragraph [0071], lines 1-6; and Figure 7). Ba teaches that the cryopreservation of living organs/tissues is challenging because organs are very complicated, containing different types of cells, blood vessels and intercellular structures, wherein the toxicity of cryoprotectants, and the formation of big ice crystals, especially during the thawing process, are the two major lethal factors for living organs/tissues cryopreservation; and the present invention offers a gateway to cryoprotectants that enable full revival of frozen living tissues and organs (paragraph [0147]).
Regarding claim 2, Ba teaches the determination of antifreeze activities of the Pegylated Type-III AFPs using an Ortago Osmometer, a thermoelectric temperature controlling device, with a temperature-controlled cooling stage, and an Olympus BX 51 microscope (maximum magnification of 800 times with resolution of 1 micron) as well as a RETIGA 2000R Color Video Camera were used to determine the antifreeze activities (interpreting the microscope and video camera as readers configured to identify different combinations of different molecules made from amino acids, claim 2) (paragraph [0066]).
Regarding claim 3, Ba teaches that Figure 7A shows a MALDI TOF mass spectrum of crude pegylated Type-III AFPs with mPEG-SG (2,000 Da) including a 10:1 molar ratio of mPEG-SG to wild-type Type-III AFP and a buffer having a pH=7.4 were used; and the MALDI TOF mass spectrum in Figure 7 shows that both single pegylated Type-III AFPs (interpreted as a ready configured to identify a molecular weight; and a plurality of different molecules formed from amino acids, claims 1 and 3) (paragraph [0071], lines 1-6; and Figure 7).
Claim 1 does not specifically exemplify a molecule depositor (claim 1, in part).
Regarding claim 1 (in part), Jacobson teaches methods and devices are provided for preparing a protein array having a plurality of proteins, wherein the method includes providing a plurality of nucleic acids each having a predefined sequence and expressing in vitro a plurality of proteins from the plurality of nucleic acid (Abstract, lines 1-5). Jacobson teaches that Figure 2A illustrates a nucleic acid having a T7 promoter (100), an E. coli ribosome binding site (110) upstream of a gene of interest (120), and a transcriptional terminator (130) downstream of the gene of interest (120); Figure 2B illustrates a library of synthetic nucleic acid constructs integrated into a plasmid (140) or in linear form (150) being transferred to individual wells of a micro-well plate containing the appropriate transcription-translation reaction reagents (160), and expression of the proteins (170) encoded by the gene library; and Figure 2C illustrates a droplet based dispensing apparatus (200) to dispense droplets (210) of transcription/translation reagents directly onto specific locations of the solid surface (180) and covering the deposited nucleic acid constructs (190) forming a self-contained reaction volume (220) (interpreting the array to comprise a molecule generator; dispensing apparatus is interpreted to be a molecule depositor; and a microwell plate is a container comprising grid elements, claims 1 and 3) (col 3, lines 25-42; and Figure 2A-C). Jacobson teaches using one or more of the devices or device components described herein can be combined in a system (e.g., a robotic system) or in a micro-environment (e.g., a micro-fluidic reaction chamber), wherein assembly reaction mixtures (e.g., liquid reaction samples) can be transferred from one component of the system to another using automated devices and procedures (e.g., robotic manipulation and/or transfer of samples and/or sample containers, including automated pipetting devices, micro-systems, etc.), such that the system and any components thereof can be controlled by a control system (interpreted as molecule depositors; generators; controllers, claim 1) (col 43, lines 1-12). Jacobson teaches that sampling can be performed by an automated sampling device including a sample uptake tube (380), a pump (385) and the appropriate separation method, for example a chromatography column (390) capable of separating the enzyme reaction product from the substrate, reactants or contaminating molecules, wherein the presence of the enzyme reaction product can be detected in a variety of manners, including fluorescence emissions, absorbance of light or mass spectrometry (395), while other technologies, such as the RapidFire@ technology from Biocius Life Sciences can also be used to allow high throughput measurement of reaction products, analyzing thousands of reactions per day (see, e.g., U.S. Pat. Nos. 6,932,939, 6,S12,030, 7,100,460, and 7,5SS,725) (interpreted as identifying molecules in different storage containers by UV, or molecular weight, claim 3) (col 49, lines 25-39). Jacobson teaches that the support can be a polymer membrane, glass, controlled pore glass, magnetic controlled pore glass, ceramics, metals, and the like (interpreted as glass, claim 1) (col 11, lines 3-4 and 15-18).
“It is prima facie obvious to combine prior art elements according to known methods to yield predictable results; the court held that, "…a conclusion that a claim would have been obvious is that all the claimed elements were known in the prior art and one skilled in the art could have combined the elements as claimed by known methods with no change in their respective functions, and the combination would have yielded nothing more than predictable results to one of ordinary skill in the art. KSR International Co. v. Teleflex Inc., 550 U.S. ___, ___, 82 USPQ2d 1385, 1395 (2007); Sakraida v. AG Pro, Inc., 425 U.S. 273, 282, 189 USPQ 449, 453 (1976); Anderson’s-Black Rock, Inc. v. Pavement Salvage Co., 396 U.S. 57, 62-63, 163 USPQ 673, 675 (1969); Great Atlantic & P. Tea Co. v. Supermarket Equipment Corp., 340 U.S. 147, 152, 87 USPQ 303, 306 (1950)”. Therefore, in view of the benefits of automating method steps in a laboratory environment as exemplified by Jacobson, it would have been prima facie obvious for one of ordinary skill in the art before the effective filing date of the claimed invention to modify the method of synthesizing and analyzing AFPs and/or AFP derivatives including plant AFPs as disclosed by Ba to include the methods and automated sample handling devices for the high- throughput synthesis of thousands of proteins on an array as disclosed by Jacobson, with a reasonable expectation of success in using automation and robotic techniques for the rapid synthesis, analysis, and/or identification of plant AFPs, plant AFP variants, and/or plant AFP derivatives having new and/or improved antifreeze properties including enhanced bulk freezing point depression, the lowering of the bulk melting point of frozen AFP solutions, and/or melting point lowering of seed ice crystals in the AFP solutions; and/or in selecting AFPs and/or AFP derivatives having desired properties for biomedical applications such as prolonging the shelf lives of blood platelets, mammalian cells, tissues and organs at low storage temperatures; as well as, producing AFP derivatives with enhanced water solubility and/or reduced toxicity.
Thus, in view of the foregoing, the claimed invention, as a whole, would have been obvious to one of ordinary skill in the art at the time the invention was made. Therefore, the claims are properly rejected under 35 USC §103 as obvious over the art.
Conclusion
Claims 1-3 and 23 remain rejected.
Applicant's amendment necessitated the new ground(s) of rejection presented in this Office action. Accordingly, THIS ACTION IS MADE FINAL. See MPEP § 706.07(a). 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 mailing date of this final action.
Any inquiry concerning this communication or earlier communications from the examiner should be directed to AMY M BUNKER whose telephone number is (313) 446-4833. The examiner can normally be reached on Monday-Friday (6am-2:30pm).
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/AMY M BUNKER/Primary Examiner, Art Unit 1684
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