background:
Cysteine-rich secretory proteins (CRISPs) represent a family of evolutionarily conserved proteins which play a role in the innate immune system and are transcriptionally regulated by androgens in several tissues. CRISP-8 (Cysteine-rich secretory protein 8), also known as PI15 (Peptidase inhibitor 15), P25TI or SugarCrisp, is a 258 amino acid secreted protein that belongs to the CRISP family. Expressed at low levels in thyroid, prostate, salivary and mammary tissue, CRISP-8 functions as a serine protease inhibitor that exhibits weak inhibitory action against Trypsin, a serine protease found in the digestive system. In addition to its role as a protease inhibitor, CRISP-8 is secreted in neuroblastoma and glioblastoma cell lines, suggesting a role for CRISP-8 in tumor formation and metastasis within the central nervous system.
Function:
The soybean trypsin inhibitor was first crystallized by Kunitz in 1945 and is Serine protease inhibitor which displays weak inhibitory activity against trypsin.
Subcellular Location:
Secreted.
Tissue Specificity:
Weakly expressed. Expressed at low level in prostate, mammary gland, salivary gland and thyroid gland.
Post-translational modifications:
N-glycosylated (Probable).
Similarity:
Belongs to the CRISP family.
Database links:
UniProtKB/Swiss-Prot: O43692.1
Important Note:
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
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