|Other Names||Serpin B8, Cytoplasmic antiproteinase 2, CAP-2, CAP2, Peptidase inhibitor 8, PI-8, SERPINB8, PI8|
|Target/Specificity||The synthetic peptide sequence is selected from aa 289-301 of HUMAN SERPINB8|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 1 mg/ml.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||Has an important role in epithelial desmosome-mediated cell-cell adhesion.|
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Provided below are standard protocols that you may find useful for product applications.
The superfamily of high molecular weight serine proteinase inhibitors (serpins) regulate a diverse set of intracellular and extracellular processes such as complement activation, fibrinolysis, coagulation, cellular differentiation, tumor suppression, apoptosis, and cell migration. Serpins are characterized by well-conserved a tertiary structure that consists of 3 beta sheets and 8 or 9 alpha helices (Huber and Carrell, 1989 [PubMed 2690952]). A critical portion of the molecule, the reactive center loop connects beta sheets A and C. Protease inhibitor-8 (PI8; SERPINB8) is a member of the ov-serpin subfamily, which, relative to the archetypal serpin PI1 (MIM 107400), is characterized by a high degree of homology to chicken ovalbumin, lack of N- and C-terminal extensions, absence of a signal peptide, and a serine rather than an asparagine residue at the penultimate position (summary by Bartuski et al., 1997 [PubMed 9268635]).
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
de Koning, P.J., et al. Pancreas 38(4):461-467(2009)
Luke, M.M., et al. Stroke 40(2):363-368(2009)
Shiffman, D., et al. Arterioscler. Thromb. Vasc. Biol. 28(1):173-179(2008)
Denoeud, F., et al. Genome Res. 17(6):746-759(2007)
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