Interference No. 105,099 Paper 25
Hannum v. Immunex Corp. Page 4
[13] Consequently, according to Hannum, the two-way test for an interference-in-fact fails
because Hannum's claimed invention would not bar issuance (i.e., would not have
anticipated or rendered obvious the subject matter of) Immunex's claims.
[14] The examiners who proposed the interference were consulted. They replied:
Both applications describe the isolation of the mouse Flt3 ligand which
binds to Flt3, a receptor found on hematopoietic cells, and stimulates
proliferation of those cells. Although the claims of the two applications
claim the protein differently, Hannum by physical properties and partial
sequence, and [Immunex] by amino acid sequence alone, the proteins are
from the same organism and have the same activity, and the partial
sequences of Hannum et al. are comprised in the complete sequence of
[Immunex]. Immunex [sic, Hannum's] argument that Hannum has three
"isoforms" of the protein is not supported by fact. Rather, it appears that
Hannum had three partial or preliminary clones, which do not necessarily
represent different forms in vivo. Rather, the person of ordinary skill in the
art, given Hannum's three sequences, would derive a consensus
sequence from them, likely to represent the actual protein. Hence, as
Hannum actually had the mouse protein in hand and determined its
physical properties and activity, in the express absence of evidence to the
contrary, it is presumed that the protein of Hannum is identical to that of
Immunex, and that the amino acid sequence, which is an inherent
property of the protein, is also identical. Therefore, the claims of
Immunex would be held to be anticipated by Hannum.
To overcome a 102 rejection as set forth above, the burden would be on
Immunex to show fact or evidence that their protein did, in fact, differ from
that isolated by Hannum et al. The mere presence of three sequences in
Hannum's specification is not sufficient to establish this.
[15] Representative Hannum 882 claim 28 claims the invention as follows [2005]:
A substantially pure naturally occurring mammalian Flt3
ligand protein which binds to a Flt3 receptor, wherein said protein has the
following physical characteristics:
a) said protein migrates as an approximately 30 KD
glycoprotein on SDS-Polyacrylamide gel electrophoresis under reducing
conditions;
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