Appeal No. 2004-1106 July 2004
Application 09/871,388 Page 5
mouse homolog of kuz which lacked the metalloprotease domain, acted as a dominant
negative in fruit flies and in Xenopus embryo, suggesting that the function of kuz is
evolutionarily conserved (see e.g., Example 3, pp. 20-28).
B. Abbreviated procedural history of the involved application
11. In a preliminary amendment (Paper 1½, filed 31 May 2001), appellants cancelled
all pending claims and presented new claims 14-33 for examination. According to
appellants, the new claims were "directed to the antibody counterparts of the claims
issued and allowed in 09/285,502 and 09/709,126, respectively" (id., p. 6).
12. Claim 14, as presented in the preliminary amendment, read "A composition
comprising an antibody or antibody fragment which specifically binds a KUZ polypeptide
consisting of an amino acid sequence selected from the group consisting of SEQ ID
NO:2, SEQ ID NO:4, SEQ ID NO:6, and SEQ ID NO:8" (id., p. 4).
13. The examiner rejected claims 14, 17, 20, 21, 23, 25, 26 and 33, as presented in
the preliminary amendment, under 35 U.S.C. § 102(b) as anticipated by Howard, the
same Howard reference cited by appellants in their specification (Paper 7, mailed 2
October 2002).
14. According to the examiner,
Howard et al., teaches monoclonal and polyclonal antibody
compositions against MADM. Specifically using a peptide sequence
FDANQPEGKKC that shares 100% homology with residues 486-496 of
SEQ ID NO.8 and shares 9 of 10 amino acid residues with SEQ ID NOS 4
and 6 to make the antibody (page 47, 2nd column in particular). This
antibody would inherently specifically bind with SEQ ID NOS 4, 6 and 8
due to the high amino acid sequence homology between the immunizing
peptide and the claimed sequences. Furthermore the immunizing peptide
is located within the extracellular domain of SEQ ID NO. 4. [Id., p. 2.]
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