Human PRSS11-Like S2 serine protease and uses thereof

Details Human PRSS11-Like S2 serine protease and uses thereof Human PRSS11-Like S2 serine protease and uses thereof

2006-11-07

2006-11-07

Swope, Sheridan (Department: 1656)

Organic compounds -- part of the class 532-570 series

Organic compounds

Carbohydrates or derivatives

C435S226000, C435S252300, C435S252330, C435S254200, C435S325000, C435S348000, C435S320100

Reexamination Certificate

active

07132523

ABSTRACT:
A novel human nucleic acid and polypeptide, termed PRSS11-L, are disclosed. PRSS11-L, which is observed in tissues throughout the body, can be used in methods of detection, gene therapy, and screening.

REFERENCES:
Witkowski et al, Conversion of a beta-ketoacyl synthase to a malonyl decarboxylase by replacement of the active-site cysteine with glutamine. Biochemistry. Sep. 7, 1999;38(36):11643-11650.
Wishart et al, A single mutation converts a novel phosphotyrosine binding domain into a dual-specificity phosphatase. J Biol Chem. Nov. 10, 1995;270(45):26782-26785.
N—Geneseq—16Dec04 Database Accession No. AAV41533 from WO9824921 Jun. 11, 1998 Jalkanen et al. Alignment with residues 1-9 of SEQ ID No. 2.
EST Database Accession No. BG548488 Apr. 4, 2001 Strausberg et al. Alignment with residues 1-1038 of SEQ ID No. 1.
McDonagh et al., Production of caseinophosphopeptides (CPPs) from sodium caseinate using a range of commercial protease preparations. International Dairy Journal (1998), 8(1), 39-45.

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