Appeal No. 2004-1106 July 2004
Application 09/871,388 Page 3
2. SEQ ID NOS: 2, 4, 6 and 8 are said to depict the full length KUZ proteins
encoded by SEQ ID NOS: 1, 3, 5 and 7, which are said to depict "exemplary natural
cDNAs encoding Drosophila, human transmembrane, human soluble (lacking a
transmembrane domain), [and] mouse .... members, respectively, of the disclosed KUZ
family" (id., p. 4, ll. 9-12).
3. Figures 1A-C of appellants' specification are said to illustrate common predicted
functional domains for the described Drosophila KUZ ("DKUZ"), mouse KUZ ("MKUZ")
and Xenopus KUZ ("XKUZ"), i.e., a prodomain, metalloprotease and disintegrin
domains, a cysteine-rich domain and finally a transmembrane domain (also
specification, p. 3, ll. 10-27).
4. These domains, as identified in Figures 1A-C, are said to provide KUZ domain
specific activity or function, including protease activity, in particular cleaving a NOTCH
protein, disintegrin activity and ligand/antibody binding activity (id., p. 2, ll. 26-30; p. 5, ll.
14-17).
5. The mouse protein (MKUZ) is said to be 45% identical in primary amino acid
sequence with Drosophila KUZ (DKUZ, Fig. 1) and 95% identical with a bovine protein
(MADM) isolated by Howard.[5] Sequence similarity between MKUZ and DKUZ is said
to extend over the whole coding region, except that MKUZ, like other vertebrate KUZ
homologs, has a much shorter intracellular domain. The intracellular domain of MKUZ
kuz is a gene, whereas DKUZ is the protein expressed by the kuz gene in Drosophila.
5 Appellants' specification cites to "the bovine protein of Howard, L., et al. (1996). Biochem. J.
317, 45-50." at p. 5, ll. 29-31. A copy of this article, i.e., Howard et al., ("Howard"), "Molecular cloning of
MADM: a catalytically active mammalian disintegrin-metalloprotease expressed in various cell types,"
Biochemical Journal, Vol. 317, part 1, pp. 45-50 (1 July 1996), is enclosed.
Page: Previous 1 2 3 4 5 6 7 8 9 10 11 12 13 Next
Last modified: November 3, 2007