DETAILED ACTION
Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
Status of Claims
Receipt of Arguments/Remarks filed on 7/1/2026 is acknowledged. Claims 1 and 8 were amended. Claims 1-8, 10-14, and 18-20 are pending. Claims 6-7, 10-14 and 18-20 are withdrawn as being directed to a non-elected invention.
Information Disclosure Statement
The information disclosure statement (IDS) filed on 7/27/2026 is in compliance with the provisions of 37 CFR 1.97. Accordingly, the information disclosure statement is being considered by the examiner.
Modified rejections necessitated by amendment
Claim Rejections - 35 USC § 112
The following is a quotation of the first paragraph of 35 U.S.C. 112(a):
(a) IN GENERAL.—The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor or joint inventor of carrying out the invention.
The following is a quotation of the first paragraph of pre-AIA 35 U.S.C. 112:
The specification shall contain a written description of the invention, and of the manner and process of making and using it, in such full, clear, concise, and exact terms as to enable any person skilled in the art to which it pertains, or with which it is most nearly connected, to make and use the same, and shall set forth the best mode contemplated by the inventor of carrying out his invention.
Claim 8 is rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the written description requirement. The claim(s) contains 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 or a joint inventor, or for applications subject to pre-AIA 35 U.S.C. 112, the inventor(s), at the time the application was filed, had possession of the claimed invention.
In the instant case, claim 8 is directed to an ADAMTS13 variant comprising an amino acid sequence having at least 90% identity to elected SEQ ID NO: 61. There is not sufficient written description support for an amino acid sequence having 90% identity to SEQ ID NO: 61 and having increased proteolytic activity. As set forth in the instant specification, p. 61, a “variant” refers to a protein having an amino acid sequence comprising one or more substitutions, insertions, deletions, or other modifications relative to the reference protein. However, there is no disclosure of which regions or structural elements of SEQ ID NO: 61 are required or essential for activity, and which regions can be modified, other than the specifically claimed region corresponding to SEQ ID NO: 48, to produce a variant having the recited sequence identity and increased proteolytic activity.
SEQ ID NO: 61 has 1353 amino acid residues. This means that anywhere from 1-135 residues may be substituted or modified, with 19 potential amino acids at any given position, within the scope of 90% identity, in addition to potential insertions or deletions. Thus, 90% identity encompasses a vast number of sequences, and it would not be clear to a skilled artisan which of these variants would have increased proteolytic activity as claimed. There are no examples in the specification directed to variants of SEQ ID NO: 61, other than the specifically claimed substitutions (i.e., recited in claims 2-5), which retain the claimed activity, or any indication of which residues can or cannot be modified.
For this reason, it is not clear that applicant was in possession of the full scope of the invention, an ADAMTS13 enzyme having a sequence with 90% identity to SEQ ID NO: 61 and increased proteolytic activity. Thus, claim 8 fails to comply with the written description requirement.
The following is a quotation of 35 U.S.C. 112(b):
(b) CONCLUSION.—The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the inventor or a joint inventor regards as the invention.
The following is a quotation of 35 U.S.C. 112 (pre-AIA ), second paragraph:
The specification shall conclude with one or more claims particularly pointing out and distinctly claiming the subject matter which the applicant regards as his invention.
Claim 3 is rejected under 35 U.S.C. 112(b) or 35 U.S.C. 112 (pre-AIA ), second paragraph, as being indefinite for failing to particularly point out and distinctly claim the subject matter which the inventor or a joint inventor (or for applications subject to pre-AIA 35 U.S.C. 112, the applicant), regards as the invention.
SEQ ID NOs: 50 and 156 comprise the L3 subregion of ADAMTS13, with a sequence X1X2X3X4GRTTATX5AGASLEWSQARGLLFSX6AX7QX8RRLLX9GX10 (see specification Sequence Table pp. 12-13, 58).
X1-X10 correspond to positions A1144, A1145, A1146, P1147, P1154, P1171, P1173, P1175, P1180, and P1182 in the WT ADAMTS13 sequence, respectively. In both SEQ ID NOs: 50 and 156, X1- X3 may be A and X4- X10 may be P (see specification Sequence Table pp. 12-13, 58; instant SEQ ID NO: 1). If X1- X3 in SEQ ID NOs: 50 and 156 are A and X4- X10 are P, these are the same residues as the WT SEQ ID NO: 48. Thus, this embodiment of SEQ ID NOs: 50 and 156 do not have a substitution compared to WT. The ADAMTS13 variant of claim 1 requires at least one substitution in the region corresponding to SEQ ID NO: 48, which can be at any residue of SEQ ID NO: 48 (see Sequence Table p. 12). It is unclear if claim 3 is directed to a variant with a sequence comprising SEQ ID NOs: 50 or 156, wherein the substitution can be at any position in the region of SEQ ID NO: 48 (as recited in claim 1); or specifically directed to a variant wherein the substitution must be at the variable positions of SEQ ID NOs: 50 and 156.
Under broadest reasonable interpretation, claim 3 reads on a variant with ANY substitution in the region corresponding to SEQ ID NO: 48, as claim 1 is directed to a variant with any substitution, and SEQ ID NOs: 50 and 56 do not specify that any of the residues must be substituted. SEQ ID NOs: 50 and 156 are shorter than SEQ ID NO: 48 (position 1 of SEQ ID NOs: 50 and 156 corresponds to position 14 of SEQ ID NO: 48). If the variant can have any substitution in the region of SEQ ID NO: 48, this means that the variant may comprise SEQ ID NOs: 50/156 wherein all the residues are the same as wildtype, except for a substitution of one or more residues, including any residue of SEQ ID NO: 48 that is outside of SEQ ID NOs: 50/156 (i.e. positions 1-13 of SEQ ID NO: 48), or any other position.
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 3 is rejected under 35 U.S.C. 112(d) or pre-AIA 35 U.S.C. 112, 4th paragraph, as being of improper dependent form for failing to further limit the subject matter of the claim upon which it depends, or for failing to include all the limitations of the claim upon which it depends.
Claim 3 recites SEQ ID NOs: 50 and 156. As discussed in the rejection under 35 U.S.C. § 112(b) above, SEQ ID NOs: 50 and 156 have variable amino acids at the positions recited in claim 2. However, variable positions X1- X3 may be A and X4- X10 may be P, making SEQ ID NOs: 50 and 156 identical to the wildtype sequence (see specification Sequence Table pp. 12-13, 58). As claim 1, upon which claim 3 depends, requires a substitution in the region corresponding to SEQ ID NO: 48, claim 3 does not further limit claim 1 as it includes sequences that are identical to the WT, and does not specify where the substitution must be made. Therefore, under broadest reasonable interpretation, claim 3 reads on a variant with ANY substitution in the region corresponding to SEQ ID NO: 48, including any residue of SEQ ID NO: 48 that is outside of SEQ ID NOs: 50/156 (i.e. positions 1-13 of SEQ ID NO: 48), or any other position.
Applicant may cancel the claim(s), amend the claim(s) to place the claim(s) in proper dependent form, rewrite the claim(s) in independent form, or present a sufficient showing that the dependent claim(s) complies with the statutory requirements.
It appears that applicant is intending for the one or more substitutions in the region of SEQ ID NO: 48 to correlate with the variable positions of SEQ ID NOs: 50 or 156. However, as written, this is not clear, as SEQ ID NOs: 50 and 156 do not require that any variable positions differ from wildtype.
It is suggested that the claim be amended to instead state:
“The ADAMTS13 variant according to claim 1, wherein the ADAMTS13 variant comprises an amino acid sequence according to SEQ ID NO:50 or 156, and wherein one or more of the variable residues of SEQ ID NO: 50 or 156 differs from the wildtype residue at that position.”
Claim Rejections - 35 USC § 102
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 1, 3, and 8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Roose et al., TH Open; 2(01):e8-15.
Regarding claim 1, Roose teaches human ADAMTS13 with a substitution at residue 1177 (R1177Q) relative to the wildtype sequence (Roose “Abstract”; p. e10 “Expression of Wild Type (WT), p.A900V, p.R1177Q, and p.A900V/R1177Q ADAMTS13”). Residue 1177 is located in the third linker region of the ADAMTS13 sequence (Roose p. e11 “ADAMTS13-Related Parameters in Acute and Remission Samples” para. 2). The limitation “displays increased proteolytic activity as compared to wildtype human ADAMTS13” is a functional limitation of the ADAMTS13 variant of claim 1. Roose teaches an ADAMTS13 variant according to claim 1 as discussed above. Claim 1 encompasses ADAMTS13 variants with substitutions at any position in the linker 3 (SEQ ID NO: 48) region. Absent any missing essential unclaimed features, any ADAMTS13 variant having the structure of claim 1 must have the function of increased proteolytic activity as compared to wildtype human ADAMTS13.
Instant SEQ ID NO: 48 corresponds to the linker 3 region of the WT ADAMTS13 sequence, residues 1131 to 1190 (see instant specification p. 66 lines 13-16). The substitution at position 1177 as taught by Roose is therefore in the region corresponding to SEQ ID NO: 48 relative to the wild-type sequence, in the linker 3 region between residues 1131-1190.
Regarding claim 3, SEQ ID NOs: 50 and 156 have variable amino acids at the positions recited in claim 2. Variable positions X1- X3 may be A, and positions X4- X10 may be P, making SEQ ID NOs: 50 and 156 identical to the wildtype sequence (see specification Sequence Table pp. 12-13, 58; instant SEQ ID NO: 1). Therefore, SEQ ID NOs: 50 and 156 include the wildtype ADAMTS13 sequence. Roose teaches wildtype human ADAMTS13 (Roose p. e10 “Expression of Wild Type (WT), p.A900V, p.R1177Q, and p.A900V/R1177Q ADAMTS13”). Thus, the variant sequence taught by Roose comprises a sequence according to SEQ ID NO: 50 or 156 that has a substitution at a position in the region corresponding to SEQ ID NO: 48.
Regarding claim 8, instant SEQ ID NO: 61 is 99.9% identical to the WT ADAMTS13 sequence (see WT ADAMTS13 sequence, instant SEQ ID NO: 1). The variant sequence taught by Roose differs from the WT by 1 amino acid, R1177Q. Thus, the variant taught by Roose has a sequence that is over 90% identical to SEQ ID NO: 61.
Claims 1, 2, and 8 are rejected under 35 U.S.C. 102(a)(1) as being anticipated by Scheiflinger et al., US 7,763,430 B2.
Regarding claim 1, Scheiflinger teaches von Willebrand Factor-cleaving protease (“vWF-cp”, or ADAMTS13) proteins (Scheiflinger col. 1 lines 19-34). SEQ ID NO: 6 according to Scheflinger is 98.3% identical to instant SEQ ID NO: 48, with one amino acid substitution (see sequence alignment below). The limitation “displays increased proteolytic activity as compared to wildtype human ADAMTS13” is a functional limitation of the ADAMTS13 variant of claim 1. Scheiflinger teaches an ADAMTS13 variant according to claim 1 as discussed above. Absent any missing essential unclaimed features, any ADAMTS13 variant having the structure of claim 1 must have the function of increased proteolytic activity as compared to wildtype human ADAMTS13.
Regarding claim 2, SEQ ID NO: 6 of Scheiflinger comprises a substitution at position 43 of SEQ ID NO: 48 (see sequence alignment below). As set forth on p. 62 of the instant specification, SEQ ID NO:48 corresponds to positions 1131 to 1190 of SEQ ID NO:1 (wildtype ADAMTS13), with the alanine residue at position 14 of SEQ ID NO:48 corresponding to position 1144 of the WT sequence. Therefore, position 43 of SEQ ID NO: 48 corresponds to position 1173 of the WT sequence, and SEQ ID NO: 6 of Scheiflinger comprises a substitution at position P1173.
PNG
media_image1.png
273
669
media_image1.png
Greyscale
PNG
media_image2.png
426
667
media_image2.png
Greyscale
Regarding claim 8, SEQ ID NO: 6 of Scheiflinger has 98% identity to instant SEQ ID NO: 61 and comprises a substitution in the region corresponding to SEQ ID NO: 48, position 1173 (see alignment below).
As set forth on p. 61 of the instant specification, "sequence identity" refers to the percentage of nucleotides/amino acid residues in a subject sequence that are identical to nucleotides/amino acid residues in a reference sequence. As shown in the sequence alignment above, 98.3% of the residues of SEQ ID NO: 6 of Scheiflinger are identical to SEQ ID NO: 61 when the two sequences are aligned. Thus, SEQ ID NO: 6 of Scheiflinger is at least 90% identical to instant SEQ ID NO: 61 with a substitution in the region corresponding to SEQ ID NO: 48.
Claim Rejections - 35 USC § 103
The text of those sections of Title 35, U.S. Code not included in this action can be found in a prior Office action.
Claims 4 and 5 are rejected under 35 U.S.C. 103 as being unpatentable over Scheiflinger et al. as applied to claims 1, 2, and 8 above, in view of Zhang et al., Journal of molecular evolution; 50(1):56-68.
Scheiflinger teaches an ADAMTS13 protein sequence with a substitution of proline for arginine at position 1173. Scheiflinger does not teach a substitution of proline to valine, isoleucine, or lysine.
Regarding claim 4, Zhang teaches that amino acids are classified into groups based on physicochemical properties, and substitutions of amino acids within groups are considered conservative, whereas substitutions between groups are radical (Zhang p. 56 para. 1). A conservative substitution would be expected to maintain the physiochemical properties of the amino acid and therefore result in minimal change to the protein. Zhang teaches that proline, valine, and isoleucine are all neutral, nonpolar amino acids (Zhang p. 57 Fig. 1). Therefore, a substitution of proline to valine or isoleucine would be considered conservative and would not result in a change in physiochemical properties.
It would have been obvious for a skilled artisan, with a reasonable expectation of success, to substitute the proline at position 1173 in the WT ADAMTS13 protein with a valine or isoleucine. Scheiflinger teaches substitution of the proline at this position of ADAMTS13, and a skilled artisan would therefore recognize that this position may be substituted. Substitution of proline to valine or isoleucine would be a conservative substitution, as taught by Zhang. Thus, introducing a substitution of valine or isoleucine at this position would be considered a simple substitution of one known element for another having similar properties, with a reasonable expectation that such a substitution would result in a protein having similar properties to the wildtype.
Regarding claim 5, instant SEQ ID NO: 57 is an ADAMTS13 variant L3 region with a substitution of P1173V, and SEQ ID NO: 152 is an ADAMTS13 variant L3 region with a substitution of P1173I. As discussed above, it would have been obvious to make these mutations in view of the teachings of Scheiflinger and Zhang. Therefore, an ADAMTS13 variant comprising the amino acid sequence of SEQ ID NO: 57 or 152 is obvious in view of the prior art.
Allowable Subject Matter
It appears that the elected species, an ADAMTS13 variant comprising the amino acid sequence of SEQ ID NO: 51 (i.e., A1144 substitution) is free of the prior art. The closest prior art is Roose et al. and Scheiflinger et al. Roose teaches an ADAMTS13 variant with a substitution in the region according to SEQ ID NO: 48, but does not teach a substitution at position A1144. Scheiflinger teaches a substitution at position 1173, but not A1144. The prior art does not appear to teach a sequence corresponding to SEQ ID NO: 51, or an ADAMTS13 variant with a substitution at the position corresponding to A1144.
Response to Arguments
Applicant's arguments filed 7/1/2026 have been fully considered but they are not persuasive.
Rejection under 35 U.S.C. § 112(a)
Applicant argues that as amended, claim 8 requires one or more substitutions in the
region corresponding to SEQ ID NO:48 (the L3 linker region). This sequence is clearly identified in the application (and in claim 1), and it is only 60 amino acid residues in length. Applicant argues that the skilled person would be able to identify the L3 region of an ADAMTS13 protein and introduce amino acid substitutions within this region by, e.g., site-directed mutagenesis methods, and the skilled person would understand the type of amino acid substitutions that will generate ADAMTS13 variants that have increased proteolytic activity in view of the guidance in the application to introduce mutations that disturb the conformation of the relatively short L3 region.
In response to this argument, it is noted that while the variant of claim 8 does require at least one substitution in the region corresponding to SEQ ID NO: 48, a variant having 90% identity to SEQ ID NO: 61 also includes substitutions outside this region. For example, if a variant has one substitution in the region corresponding to SEQ ID NO: 48, the variant could also have ~133 other substitutions, as well as various insertions or deletions, in different regions of the protein, within the scope of 90% identity. It is not clear which of these many possible additional modifications would result in an enzyme with increased proteolytic activity. The examples in the specification are directed to variants having at least one substitution in the region of SEQ ID NO: 48, but these examples are not representative of the entire claimed genus of variants having a sequence that is 90% identical to instant SEQ ID NO: 61. Thus, there is sufficient written description support for sequences with the specifically identified substitutions in the region corresponding to SEQ ID NO: 48, but there is not support for all variants having at least one substitution in the region of SEQ ID NO: 48 and 90% identity to SEQ ID NO: 61.
Rejections under 35 U.S.C. § 112(b) and (d)
Applicant argues that claim 3 is dependent on claim 1 and therefore includes all of the features of claim 1. Claim 1 recites that the claimed protein sequence must comprise "one or more amino acid substitutions in the region corresponding to SEQ ID NO:48 relative to the amino acid sequence of wildtype human ADAMTS13", and it is entirely and unambiguously clear that SEQ ID NOs: 50 and 156 MUST require a substitution in the region corresponding to SEQ ID NO: 48 because this is a requirement of claim 1. Applicant argues that SEQ ID NO: 48 is 60 amino acids in length, and SEQ ID NO:50 and 156 are 39 amino acids in length, corresponding to the sequence starting at position 14 of SEQ ID NO: 48, and thus claim 3 limits the scope of claim 1 by specifying the region of SEQ ID NO: 48 that must contain an amino acid substitution.
The limitation “wherein the ADAMTS13 variant comprises SEQ ID NO: 50 or 156” in claim 3 indicates that the variant can comprise any of the options for the variable positions in SEQ ID NOs: 50 and 156. One embodiment of SEQ ID NOs: 50 or 156 includes X1- X3 being A and X4- X10 being P. Therefore, based on the limitation of claim 3 “comprising an amino acid sequence according to SEQ ID NO: 50 or 156”, the ADAMTS13 variant can comprise a sequence with X1- X3 being A and X4- X10 being P. This embodiment does not include a substitution compared to the wildtype sequence. Therefore, the limitation in claim 3 is not clear, and does not further limit the subject matter of claim 1, because if X1- X3 are selected to be A and X4- X10 are selected to be P, there is no substitution compared to wildtype. SEQ ID NOs: 50 and 156 do not specify that one of the residues has to be different than the residue that is in the WT sequence (see specification Sequence Table pp. 12-13). It is noted that while it is clear based on claim 1 that a substitution in the region corresponding to SEQ ID NO: 48 is required, SEQ ID NOs: 50 and 156 do not include all the residues of SEQ ID NO: 48. It is therefore unclear if claim 3 is directed to variants with substitutions at the variable regions of SEQ ID NOs: 50 and 156, or with any substitution in the region corresponding to SEQ ID NO: 48.
Regarding the argument that SEQ ID NOs: 50 and 156 are shorter than SEQ ID NO: 48 and therefore limit where the substitutions may occur, this is not the case based on the broadest reasonable interpretation of claim 3. Under broadest reasonable interpretation, claim 3 requires that the ADAMTS13 variant has any substitution in the region corresponding with SEQ ID NO: 48. This includes, for example, residues outside of the residues in SEQ ID NOs: 50 and 156 (i.e. residues 1-13 of SEQ ID NO: 48). SEQ ID NO: 3 states that the variant comprises either SEQ ID NOs: 50 or 156, and the variable positions of these sequences may be the same as wildtype (see specification Sequence Table pp. 12-13). Therefore, for example, a sequence wherein position 1 of the region corresponding to SEQ ID NO: 48 is substituted, and all other positions are the same as wildtype, reads on claim 3. The limitation “comprises SEQ ID NO: 50 or 156” therefore does not further limit claim 1.
Rejection under 35 U.S.C. § 102
Applicant argues that the ADAMTS13 variant of Roose has reduced activity, rather than increased proteolytic activity as claimed. Applicant argues that the statement that “any ADAMTS13 variant having the structure of claim 1 must have the function of increased proteolytic activity as compared to wildtype human ADAMTS13” is a misinterpretation of Roose and incorrect.
In response to this argument, it is noted that the structure of claim 1 is an ADAMTS13 variant with an amino acid substitution in the region corresponding to SEQ ID NO: 48 (the linker 3 region). Roose clearly teaches this structure, i.e. a substitution of R1177Q, which is in the linker 3 region. The limitation “wherein the ADAMTS13 variant displays increased proteolytic activity” is a functional limitation that does not impact the structure of the claimed enzyme. Therefore, absent any unclaimed required structural features, any ADAMTS13 variant with a substitution in the region as claimed must have the claimed function. While Roose does provide results that this enzyme has decreased activity, it is also noted that “proteolytic activity” is broad, and the activity of an enzyme can be measured in different ways under different conditions, leading to different activity levels. Therefore, while in the specific activity assay performed by Roose there is a decrease in enzyme activity, it is not necessarily the case that the modified enzyme always has decreased proteolytic activity in all conditions. The instant specification, p. 75, states that proteolytic activity can be measured using any method known in the art, and claim 1 does not specify the method or conditions under which the enzyme has increased activity. Further, it can be seen from the examples in the instant specification that the proteolytic activity of the ADAMTS13 variants differs based on the presence or absence of activating VWF-D4CK, for example (see instant specification Figs. 1a and 1b, pp. 96-97 Example 2).
Further, if it is the case that not all enzymes having the claimed structure (one or more substitutions in the region corresponding to SEQ ID NO: 48) have increased proteolytic activity as claimed, this could represent an enablement issue, as claim 1 is directed to a structure which includes ALL possible substitutions in the region of SEQ ID NO: 48. It is additionally noted that the examples of enzymes which have increased proteolytic activity are substitutions of valine, lysine, or isoleucine at positions 1144, 1145, 1146, 1147, 1154, 1171, 1173, 1175, 1180, and 1182 (see instant specification Figs. 1a and 1b, pp. 96-97 Example 2).
Applicant argues that there is no disclosure or suggestion in Scheiflinger that the P1173R substitution that is allegedly disclosed has an increased proteolytic activity relative to the wild-type, and the peptides disclosed in Scheiflinger are not ADAMTS13 variants as claimed in the present application, and may not possess any proteolytic activity. Applicant argues that Scheiflinger teaches away from the use of a full-length ADAMTS13 variant protein because it is stated in Scheiflinger that it is advantageous for the peptides to be 6-50 amino acids in length.
In response to this argument, it is again noted that the structure of claim 1 requires one or more substitutions in the region corresponding to SEQ ID NO: 48, which is taught by Scheiflinger. The instant specification, p. 61, states that a "variant" generally refers to a protein having an amino acid sequence comprising one or more amino acid substitutions, insertions, deletions or other modifications relative to the amino acid sequence of the reference protein, but retaining a considerable degree of sequence identity (e.g. at least 40%) to the amino acid sequence of the reference protein. There is not a requirement for any particular sequence length. Further, the fact that Scheiflinger does not expressly teach that the variants have proteolytic activity does not necessarily mean that they are incapable of or do not have activity. Additionally, as discussed above, absent any unclaimed required structural features, any ADAMTS13 variant with a substitution in the region as claimed must have the claimed function.
Conclusion
Claims 1-5 and 8 are 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 EMILY F EIX whose telephone number is (571)270-0808. The examiner can normally be reached M-F 8am-5pm ET.
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, Sharmila Landau can be reached at (571)272-0614. The fax phone number for the organization where this application or proceeding is assigned is 571-273-8300.
Information regarding the status of published or unpublished applications may be obtained from Patent Center. Unpublished application information in Patent Center is available to registered users. To file and manage patent submissions in Patent Center, visit: https://patentcenter.uspto.gov. Visit https://www.uspto.gov/patents/apply/patent-center for more information about Patent Center and https://www.uspto.gov/patents/docx for information about filing in DOCX format. For additional questions, contact the Electronic Business Center (EBC) at 866-217-9197 (toll-free). If you would like assistance from a USPTO Customer Service Representative, call 800-786-9199 (IN USA OR CANADA) or 571-272-1000.
/EMILY F EIX/Examiner, Art Unit 1653
/JENNIFER M.H. TICHY/Primary Examiner, Art Unit 1653
Prosecution Insights