Notice of Pre-AIA or AIA Status
The present application, filed on or after March 16, 2013, is being examined under the first inventor to file provisions of the AIA .
DETAILED ACTION
1. Applicant’s amendment and response filed 10/29/25 is acknowledged and has been entered.
2. Applicant is reminded of Applicant's election with traverse of Group I and species of an anti-CD96 antibody or fragment thereof, a method for treating or preventing cancer or cancer metastasis, and an anti-cancer agent in Applicant’s response filed 12/12/23.
Claims 1, 4-7, 9 and 10 read on the elected species and are presently being examined as they read upon the elected species.
3. 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.
4. Claims 1, 4-7, 9 and 10 are 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 pre-AIA the inventor(s), at the time the application was filed, had possession of the claimed invention. This is a written description rejection.
This is a new ground of rejection necessitated by Applicant’s amendment filed 10/29/25.
An applicant shows possession of the claimed invention by describing the claimed invention with all of its limitations using such descriptive means as words, structures, figures, diagrams, and formulas that fully set forth the claimed invention. Lockwood v. Amer. Airlines, Inc., 107 F.3d 1565, 1572, 41 USPQ2d 1961, 1966 (Fed. Cir. 1997). Possession may be shown in a variety of ways including description of an actual reduction to practice, or by showing that the invention was "ready for patenting" such as by the disclosure of drawings or structural chemical formulas that show that the invention was complete, or by describing distinguishing identifying characteristics sufficient to show that the applicant was in possession of the claimed invention. See, e.g., Pfaff v. Wells Elecs., Inc., 525 U.S. 55, 68, 119 S.Ct. 304, 312, 48 USPQ2d 1641, 1647 (1998); Eli Lilly, 119 F.3d at 1568, 43 USPQ2d at 1406; Amgen, Inc. v. Chugai Pharm., 927 F.2d 1200, 1206, 18 USPQ2d 1016, 1021 (Fed. Cir. 1991) (one must define a compound by "whatever characteristics sufficiently distinguish it"). "Compliance with the written description requirement is essentially a fact-based inquiry that will ‘necessarily vary depending on the nature of the invention claimed.’" Enzo Biochem, 323 F.3d at 963, 63 USPQ2d at 1612. An invention described solely in terms of a method of making and/or its function may lack written descriptive support where there is no described or art-recognized correlation between the disclosed function and the structure(s) responsible for the function. See MPEP 2163 I.A.
An applicant may also show that an invention is complete by disclosure of sufficiently detailed, relevant identifying characteristics which provide evidence that applicant was in possession of the claimed invention, i.e., complete or partial structure, other physical and/or chemical properties, functional characteristics when coupled with a known or disclosed correlation between function and structure, or some combination of such characteristics. Enzo Biochem, 323 F.3d at 964, 63 USPQ2d at 1613 (quoting the Written Description Guidelines, 66 Fed. Reg. at 1106, n. 49, stating that "if the art has established a strong correlation between structure and function, one skilled in the art would be able to predict with a reasonable degree of confidence the structure of the claimed invention from a recitation of its function".). "Thus, the written description requirement may be satisfied through disclosure of function and minimal structure when there is a well-established correlation between structure and function." See MPEP 2163 II.3.
Applicant has broadly claimed a method of treating a solid cancer or cancer metastasis in a human, said method including the step of administering an anti-CD96 antibody to a human, wherein:
the anti-CD96 antibody inhibits or reduces CD96 binding activity to CD155 in one or more T cells or NK cells of the human to thereby relieve immune inhibition and/or enhance or restore immune surveillance in the human, wherein the step of inhibiting or reducing CD96 activity in the human does not include killing of CD96-expressing cells in the human, thereby treating the solid cancer or the cancer metastasis in the human (as is recited in instant base claim 1).
Thus, the anti-CD96 antibody or antigen binding fragment thereof must possess the functional properties of: inhibiting CD96 binding activity to CD155 while not having the functional property of killing CD96-expressing cells.
In addition the antibody must possess the functional properties of binding or interacting with one or a plurality of external Ig-like domains of CD96 (as is recited in instant dependent claims 4 and 6), wherein the said external domains are selected from those recited in instant dependent claim 5, or wherein the antibody must possess the functional properties of at least partially blocking or inhibiting intracellular signaling by CD96 (as is recited in instant dependent claim 7), which appears to be a function of not only where the antibody binds to CD96 but also affinity of binding.
Claims 9 and 10 recite administering one or more other therapeutic agents (and depend upon claim 1 which does not recite administering a therapeutic agent).
The genus of anti-CD96 antibody administered in the claimed method must possess the aforementioned functional properties while simultaneously not possessing the functional property of killing CD96-expessing cells; and consideration of the functional properties is in the face of no limiting definition disclosed by the instant specification for the functional property of “at least partly inhibits CD96-binding to CD155”.
The antibody ingredient administered in the claimed method is a functional subgenus of an anti-CD96 antibody.
There is no evidence of record for a representative number of these said anti-human CD96 or non-human-mammal anti-CD96CD96 antibodies that possess these said functional properties, and while not including or depending upon killing of CD96-expressing cells in humans.
The art recognizes that there is no structure-function relationship for the amino acid sequences of the cognate CDRs of an antibody that bind to its antigen. Antibodies that bind to the same antigen have diverse sequences.
The specification does not disclose a representative number of species of such CD69 inhibitory antibodies that are administered in the claimed method, nor sufficient relevant identifying characteristics in the form of structure or functional characteristics coupled with a known or disclosed correlation between structure and function.
This is because there is no evidence of record for a representative number of species of such CD69 antibody that are administered in the claimed method, nor a structure function relationship for said agent or antibodies that possess the recited/aforementioned functional properties (i.e., the structure of the cognate CDRs of antibodies that possess these said functional properties are a very large and structurally diverse genus, as is enunciated below.)
The specification discloses that CD96 is highly expressed by resting NK cells and T cell subsets and competes with DNAM-1 for the binding of CD155 on resting NK cells (page 10 at lines 1-3), but that CD96 has also been reported to associate with CD111 (nectin-1) and plays a role in promoting NK and T cell adhesion (page 3 at lines 1-3). The specification further discloses that CD96 acts as a negative regulator of T cell and NK cell anti-tumor functions (page 3 at lines 6-7).
The specification discloses that human CD96 is a transmembrane form that exists in two isoforms, isoform I, detected on AML cells and that includes additional amino acid residues compared with isoform 2. The specification further discloses that isoform 2 is the more common form. The specification discloses that the predicted domain architecture of isoform 2 has three external Ig-like domains as listed in Table 1, and consists of the amino acid sequence of SEQ ID NO: 2. (See page 11 at lines 14-20.)
With regard to CD96 inhibitory activity, the specification discloses:
“Suitably, the step of inhibiting or reducing CD96 activity in the mammal does not include, or at least depend upon, killing of CD96-expressing cells in the mammal. In some embodiments, the step of inhibiting or reducing CD96 activity in the mammal includes inhibiting or reducing CD96 binding to CD155 and/or intracellular signaling in one or more cells of the mammal that express CD96.
The specification discloses that in an embodiment, the CD96 inhibitory agent is a molecule that possesses or displays an ability to inhibit or reduce CD96 signaling activity, which may be through inhibiting, blocking or antagonizing a binding interaction with CD155 or may be through blocking CD96-initiated signaling that would normally occur in response to CD155 (page 12 at lines 9-13). The specification further discloses that CD96 comprises an ITIM. In one embodiment, the CD96-inhibitory agent possesses or displays an ability to inhibit or reduce CD96 signaling activity mediated by the CD96 ITIM, and preferably enables increased or enhanced cytokine (such as IFNg) expression, production and/or secretion by a cell expressing CD96 (page 12 at lines 13-25.
The specification discloses that in another embodiment, the CD96 inhibitory agent is a molecule that removes cell surface CD96 and/or reduces or down-regulates cell surface expression of CD96 (page 12 at lines 26-27).
“A CD96-inhibitory agent” that is an anti-CD96 antibody or antigen binding fragment thereof “possesses or displays an ability to at least partly inhibit or reduce a biological activity of CD96. Biological activities of CD96 include one or more of binding CD155, cell surface expression, eliciting intracellular signaling and/or stimulating or inducing expression and/or secretion of cytokines or chemokines.” (See page 11 at lines 5-13.)
The specification also discloses that the anti-CD96 antibody may fully or partially inhibit, block or antagonize a binding interaction between CD96 and CD155. (See page 12 at lines 4-9.) (The specification discloses on page 2 at lines 26-28 that engagement of TIGIT by CD155 has been shown to limit IFN-g production and cytotoxicity by NK cells in vitro). The specification discloses that the anti-CD96 antibody may in another embodiment remove cell surface CD96 and/or reduce or down-regulate cell surface expression of CD96. (See page 12 at lines 29-31.) The specification discloses that the CD96 inhibitory agent possesses an ability to at least partly inhibit or reduce a biological activity of CD96 such as binding to CD155, cell surface expression, eliciting intracellular signaling and/or stimulating or inducing expression and/or secretion of cytokines or chemokines (e.g., pro-inflammatory cytokines or chemokines not limited to but including MIP-1, MIP-1, RANTES, TNF- and IFN-) (pages 11 at lines 4-13).
Adequate written description for such a subgenus may require a representative number of species or a structure function correlation using the disclosure of the specification and/or the state of the prior art.
Note that “When a patent claims a genus using functional language to define a desired result, the specification must demonstrate that the applicant has made a generic invention that achieves the claimed result and do so by showing that the applicant has invented species sufficient to support a claim to the functionally-defined genus" (Capon v. Eshhar, 418 F.3d 1349 (Fed. Cir. 2005)) (emphasis added).
“[A] sufficient description of a genus . . . requires the disclosure of either a representative number* of species falling within the scope of the genus or structural features common to the members of the genus so that one of skill in the art can 'visualize or recognize' the members of the genus” (AbbVie, 759 F.3d at 1297, reiterating Eli Lilly, 119 F.3d at 1568-69) (emphasis added).
The specification discloses one antibody that binds to human NK cells “NK92.39” reduces the levels of CD96 present on the NK cell surface. (See page 9 at lines 15-16).
As Applicant is undoubtedly aware, recent court decisions in the biotechnology arena have highlighted the issue with defining binding members strictly using functional terms as can be readily seen in both AbbVie Deutschland GmbH v. Janssen Biotech. Inc. 759 F.3d 1285 (Fed. Cir. 2014) and Amgen v. Sanofi. (Fed Cir, 2017-1480. 10/5/2017). Indeed, in Amgen the court indicates that that it is improper to allow patentees to claim a binding molecule by describing something that is not the invention, i.e., the structure to which it binds, as knowledge of the chemical structure of the thing being bound does not give the required kind of structure-identifying information about the thing being claimed. Notably, in the instant claims the method administers an anti-CD96 inhibitory agent, including an anti-CD96 antibody, that is functionally recited in terms of its ligand CD96 in claims 4-8). As such, artisans would reasonably conclude that Applicant was not in possession of the genus of all such CD96-inhibitory agents, includinganti-CD96 antibodies, and hence not in possession of the claimed method that administers them.
“Possession may not be shown by merely describing how to obtain possession of members of the claimed genus or how to identify their common structural features.” See University of Rochester, 358 F.3d at 927, 69 USPQ2d at 1895.
Although the specification discloses methods for making CD96 inhibitory agents, including anti-CD96 antibodies and screening them for various functional properties, and one of skill in the art could make and test such agents or antibodies for some of the functional properties of binding or interacting with one or more of three domains of human CD96 and/or immediate or downstream functional properties required of this subgenus of agents or antibodies that are administered in the claimed method, one of skill in the art would not be able to readily envision the structure of the said agents or antibodies (i.e., the primary sequence of the antibody including the cognate sets of CDRs) that correlate not only to binding or interacting with CD96, but that also possess the requisite and large breadth of functional properties noted above.
Note that the genus of antibodies encompasses the full repertoire of such anti-CD96 antibodies in any species that they can be produced in.
The skilled artisan was aware that the genus of antibodies that bind to an antigen, antibodies that bind to an epitope of an antigen, and antibodies that bind to overlapping epitopes is a large and extremely structurally diverse genus of (the immune repertoire of) antibodies that bind to an antigen, as is evidenced below.
Edwards et al (JMB, 2003, 334: 103-118, of record) teach that over 1,000 different antibodies to a single protein can be generated, all with different sequences, and representative of almost the entire extensive heavy and light chain germline repertoire (42/49 functional heavy chain germlines and 33 of 70 V-lamda and V-kappa light chain germlines, and with extensive diversity in the HCDR3 region sequences (that are generated by VDJ germline segment recombination) as well. Said reference also teaches a high level of sequence diversity in antibodies that block binding of the antigen with its ligand. Edwards et al teach that antibodies that blocked binding of the antigen to its ligand are highly diverse by sequence and ranged 1,000-fold in terms of IC50 values. Said reference also teaches that factors other than affinity such as epitope recognition and avidity play a significant role in determining how well an antibody inhibits ligand binding (See entire reference.)
Lloyd et al (Protein Engineering, Eng. Design & Selection, 2009, 22(3): 159-168, of record) teach that a large majority of VH/VL germline gene segments are used in the antibody response to an antigen, even when the antibodies were selected by antigen binding. Said reference further teaches that in their studies, of the 841 unselected and 5,044 selected antibodies sequenced, all but one of the 49 functional VH gene segments was observed, and that there are on average about 120 different antibodies generated per antigen. Said reference also teaches that a wide variety of VH and VL pairings further increase diversity. (See entire reference.)
Goel et al (J. Immunol., 2004, 173: 7358-7367, of record) teach that three mAbs that bind to the same short (12-mer) peptide, exhibit diverse V gene usage, indicating their independent germline origin. Said reference further teaches that two of these mAbs recognize the same set of amino acid residues defining the epitope (alternate amino acid residues spread over the entire sequence), however, the relative contribution of each set of residues in the peptide showed significant variation. The said reference notes that all of the mAbs do not show any kind of V gene restriction among themselves, implying variable paratope structure, despite that two of these mAbs bind to the peptide through a common set of residues. (See entire reference).
Khan and Salunke (J. Immunol, 2014, 192: 5398-5405, of record) teach that two structurally diverse germline mAbs recognizing overlapping epitopes of the same short peptide do so in different topologies, the said antibodies possessing entirely different CDR sequences. Said reference teaches that unrelated mAbs structurally adjust to recognize an antigen, indicating that the primary B cell response is composed of BCRs having a high degree of structural adaptability. Said reference also teaches that the common epitope(s) also adopt distinct conformations when bound to different mAbs, with the higher degree of structural plasticity inherent to the mAbs. Said reference further teaches “It has been shown that both the framework region and the CDRs have a considerable amount of inherent conformational plasticity…Therefore, it is not surprising that distinct germline Abs recognize the same epitope by rearranging the CDR conformations. This may well have implications of Ag specificity beyond the naïve BCR repertoire, because Kaji et al….have shown in a recent report that the B cell memory can contain both germline-encoded and somatically mutated BCRs.” (See entire reference).
Poosarla et al (Biotechn. Bioeng., 2017, 114(6): 1331-1342, of record) teach substantial diversity in designed mAbs (sharing less than 75% sequence similarity to all existing natural antibody sequences) that bind to the same 12-mer peptide, binding to different epitopes on the same peptide. Said reference further teaches “most B-cell epitopes…in nature consist of residues from different regions of the sequence and are discontinuous...de novo antibody designs against discontinuous epitopes present additional challenges...". (See entire reference.)
Torres and Casadevall (Trend. Immunol., 2008, 29(2): 91-97, of record) teach that constant heavy domains can affect binding affinity and specificity and V-region structure independent of avidity. (See entire reference.)
The evidentiary references thus underscore a large and structurally diverse genus of (the immune repertoire of) antibodies that bind to an antigen, antibodies that bind to an epitope of an antigen, and antibodies that bind to overlapping epitopes.
There is no evidence of record of a representative number of species of anti-non-human mammal-CD96 or anti-human CD96 antibody, that binds to CD96, including with the other requisite functional properties, nor a structure/function relationship.
In light of this, a skilled artisan would reasonably conclude that Applicant was not in possession of the genus of all the recited CD69 inhibitory agents, including antibodies, at the time the instant application was filed, and hence not in possession of the claimed method that administers said antibody.
Applicant is reminded that the written description provision of 35 U.S.C. 112 is severable from its enablement provision (Ariad Phar., Inc. v. Eli Lilly & Co., 598 F.3d 1336 (Fed. Cir. 2010); see also Centocor Ortho Biotech Inc. v. Abbott Labs., 97 USPQ2d 1870, 1876 (Fed. Cir. 2011).
Applicant’s arguments have been fully considered but are not persuasive.
Applicant’s said arguments are of record in the amendment and response filed 10/29/25 on pages 5 and 6 at section A.
Applicant argues that the specification provides detailed disclosure of CD96 biology, structural features, domain architecture and screening methods for identifying suitable CD96 inhibitory agents (and points to pates 26-28 of the instant specification). Applicant argues that the claims have been amended to remove contested functional language. Applicant argues that the invention is not directed to the development of any particular specific monoclonal antibody.
However, Applicant’s said argument is not persuasive because Applicant was not in possession of an ingredient that is administered in the claimed method and is therefore not in possession of the claimed method. Applicant is reminded that although the instant claims are directed to a method of using the antibody, rather than the antibody itself, the same standard applies with regard to the written description requirement. See University of Rochester v. G.D. Searle & Co., Inc., 69 USPQ2d 1886, 1895 (Fed. Cir. 2004).
Applicant further argues that the specification provides sufficient information on the preparation of an antibody or antigen binding fragment thereof against CD96. However, this said argument pertains to enablement, not to written description. A description of the entity to which an antibody binds does not provide adequate written description, as is enunciated in the instant rejection.
Applicant states that Applicant has amended the claims to remove contested functional language. However, functional properties are still recited in the claims and the rejection is maintained for the reasons set forth in the rejection.
5. Claims 1, 4-7, 9-12 and 14 are rejected under 35 U.S.C. 112(a) or 35 U.S.C. 112 (pre-AIA ), first paragraph, as failing to comply with the enablement requirement. The claim(s) contains subject matter which was not described in the specification in such a way as to enable one skilled in the art to which it pertains, or with which it is most nearly connected, to make and/or use the invention.
This is a new ground of rejection necessitated by Applicant’s amendment filed 10/29/25.
The specification does not disclose how to use the instant invention, the method of claim 1, which treats a solid cancer or cancer metastasis in a human.
The specification has not enabled the breadth of the claimed invention because:
the claim encompasses treating a solid cancer or cancer metastasis in a human by inhibiting or reducing CD96 binding activity to CD155 in one or more T cells or NK cells of the human, wherein the step of inhibiting or reducing CD96 binding activity in the human does not include killing of CD96-expressing cells in the human.
Method claims must be enabled over their full scope without undue experimentation.
The state of the art is such that it is unpredictable in the absence of appropriate evidence whether the claimed method can be used for treatment of the broad genus of solid cancers or cancer metastasis in humans.
The specification discloses a non-limiting laundry list of cancers that may be treated or prevented by administration of an anti-CD96 antibody or antigen binding fragment thereof (see paragraph spanning pages 14-15).
The specification discloses treating a murine model of tumor melanoma cell metastasis (i.e., B16F10 melanoma tumor cells, IV injected into wild type mice, quantification of tumor burden in lungs before and after administration of anti-CD96 antibody) (e.g., Figure 3)).
Evidentiary reference Blake et al (Cancer Discovery, April 2016, 446-459, IDS reference), which shares Inventor Smyth as an author, teaches that blocking CD96 with a monoclonal antibody inhibited experimental metastases in a melanoma lung metastasis murine model (including as a monotherapy). Blake et al report that anti-CD96 antibody administration also inhibited metastasis formation in prostate cancer and lung cancer experimental lung metastasis murine models. Blake et al also teach chemically inducing fibrosarcomas in mice by injection of MCA and treating with anti-CD96 after the tumors were established, with the result that treatment reduced the growth of some tumors. The said reference also teaches that they previously demonstrated that the incidence of MCA-induced (chemically induced) fibrosarcomas was significantly reduced in wild type mice prophylactically treated with an anti-CD96 mAb. However, Blake et al conclude that “Many questions remain to be addressed, including the expression and function of CD96 on human NK cells, other innate lymphoid cells, and T-cell subsets in normal and tumor immune-pathology settings…Whether anti-human CD96 mAbs can promote NK-cell/T-cell function remains to be established. The relative expression and function of CD226, TIGIT, CD96, and their ligands will now be important to characterize in human diseases, notably cancer. Nonetheless, this study has shown CD96 to be an attractive target to enhance NK-cell control of metastasis in mice” (see entire reference, especially last paragraph of reference).
Thus, this said reference evidences that questions remain to be addressed in extrapolating the results of murine studies to human cancer treatment as pertains to CD96. These said teachings also evidence unpredictability in preventing the genus of all cancers in all mammals.
The specification does not disclose any working examples of administering the recited anti-CD96 antibody or antigen binding fragment thereof to a human prevent or treat cancer or cancer metastasis.
“An in vitro or in vivo animal model example in the specification in effect, constitutes a “working example” if that example “correlates” with a disclosed or claimed method invention.” (See MPEP 2164.02).
The moniker (solid) “cancer” encompasses a heterogeneous group of diseases, as was well known to the skilled artisan before the effective filing date of the claimed invention. Importantly, Blake et al evidence that there is unpredictability in the art of using anti-human CD96 mAbs in humans to treat (or prevent) all cancers, i.e., evidences that the working example in mice may not correlate to treatment of cancers in humans. Thus, the working examples in the specification and what is taught by Blake et al in mice is not representative of the full scope of the claimed method.
There is insufficient guidance in the specification as to how to use the instant invention. Undue experimentation would be required of one skilled in the art to practice the instant invention. See In re Wands 8 USPQ2d 1400 (CAFC 1988).
Applicant’s arguments have been fully considered but are not persuasive.
Applicant’s said arguments are of record in the amendment and response filed 10/29/25 on pages 6-7 at section B.
However, the reference cited in the instant rejection evidences unpredictability in extending the results obtained with said murine fibrosarcoma tumor model to humans or other mammals, and including for the genus of all solid cancers.
6. Applicant’s amendment filed 10/29/25 has overcome the prior rejection of record of claims 11 and 12 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.
Applicant has canceled claims 11 and 12.
7. No claim is allowed.
8. 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.
9. Any inquiry concerning this communication or earlier communications from the examiner should be directed to MARIANNE DIBRINO whose telephone number is (571)272-0842. The examiner can normally be reached on M, T, Th, F.
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/Marianne DiBrino/
Marianne DiBrino, Ph.D.
Patent Examiner
Group 1640
/MICHAEL SZPERKA/Primary Examiner, Art Unit 1641