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SERPINB8 Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P50452 |
|---|---|
| Other Accession | NP_002631.3 |
| Gene ID | 5271 |
|---|---|
| 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 | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| 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. |
| Name | SERPINB8 |
|---|---|
| Synonyms | PI8 |
| Function | Has an important role in epithelial desmosome-mediated cell- cell adhesion. |
| Cellular Location | Cytoplasm. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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]).
References
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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