Appeal No. 2007-0083
Application No. 10/174,574
therapeutic purposes.” (Br. 9.) Appellants also cite Sen,3 as teaching that
thioredoxin has “specific effects on gene expression, for example, by
regulating the transcription factor NF-κB,” and Gallegos4 for its teaching
that transfection of human breast cancer cells with a dominant-negative
mutant of thioredoxin reverses the transformed phenotype. (Id.)
The utilities relied on by Appellants are based on thioredoxin’s
activity in electron transfer and regulation of the oxidation-reduction (redox)
state. Those activities, in turn, rely on the reversible oxidation of the two
cysteine residues in thioredoxin’s active site. Since PRO270 lacks those
cysteine residues, it is unlikely to share thioredoxin’s electron transfer and
redox regulating activities. Therefore, those activities cannot be relied on as
a basis for PRO270’s patentable utility.
Appellants have asserted no utility for the claimed antibodies or for
PRO270 that is not based on electron transfer and redox regulation. Since
the evidence shows that PRO270 is unlikely to have those activities, we
agree with the Examiner that the specification does not disclose a patentable
utility for the claimed polypeptides. The rejections of claims 25-29 under
35 U.S.C. §§ 101 and 112, first paragraph, for lack of utility are affirmed.
3 Sen et al., “Antioxidant and redox regulation of gene transcription,”
FASEB J., Vol. 10, pp. 709-720 (1996).
4 Gallegos et al., “Transfection with human thioredoxin increases cell
proliferation and a dominant-negative mutant thioredoxin reverses the
transformed phenotype of human breast cancer cells,” Cancer Research,
Vol. 56, pp. 5765-5770 (1996).
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