Appeal No. 2005-0258 Page 12
Application No. 09/768,877
the function and structure of the calpain 10 polypeptide is sufficient to describe
the entire genus of calpain 10 polypeptides encompassed by the method of claim
51. In this regard, appellants direct our attention to various portions of their
specification and figures. We take each in turn.
Appellants direct our attention to Table 1, at page 30 which according to
appellants (Brief, page 14), “describes the calpain 10 isoforms with indication as
to the encoded exons, the polypeptide length and the sequences corresponding
to the SEQ ID Nos.” In addition, appellants direct our attention to figure 1, which
appellants assert (id.), diagrams “the alternative spliced forms of calpain 10
indicating the various domains.” At page 30 of appellants’ specification, we note
that appellants disclose
[t]here are a number of calpain 10 isoforms that result from
alternative splicing of the CAPN10 gene. Alternative splicing
generates eight related but structurally distinct proteins. The
structures of the mRNAs encoding each isoforms are defined by
unique combinations of exons and splice donor and acceptor sites
(see Table 1, FIG. 1).
As we understand it, the disclosure in Table 1 and Fig. 1 relate to human calpain
10 isoforms, which according to appellants are “structurally distinct proteins.”
Appellants provide no disclosure that all species encompassed by the method of
claim 51 would be expected to contain similar splice variants of these structurally
distinct proteins. Further, appellants stop short of stating that each isoform is
expected to have the same or similar function. In this regard, we note that the
examiner finds (Answer, page 8),
[a]s it can be seen at least in Figure 1, not all the splice variants
disclosed will have the same activity as that of the polypeptide of
SEQ ID NO:2 (Figure 1A, calpain 10[a]) which is the complete gene
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