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> Serpin Superfamily Serpin Superfamily
Sino Biological offers quality reagents for serpin superfamily related studies, including recombinant proteins, antibodies (rabbit mAbs, mouse mAbs, rabbit pAbs), ELISA kits, and ORF cDNA clones. Serpins (serine protease inhibitors) are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. Over 1000 serpins have now been identified, including 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are thus the largest and most diverse family of protease inhibitors.
These high-quality reagents include:
| Product Categories / Species | Human | Mouse |
| Recombinant Proteins | 17 | 12 |
| Antibodies | 25 | 10 |
| ORF cDNA Clones | 19 | 19 |
Serpin (Serine Protease Inhibitor) Products
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Serpin (Serine Protease Inhibitor) Background
Serine protease inhibitors (Serpins) are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The average protein size of a serpin superfamily member is 350-400 amino acids, but gene structure varies in terms of number and size of exons and introns. Over 1000 serpins have now been identified, including 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are thus the largest and most diverse family of protease inhibitors. In humans, extracellular serpin-enzyme complexes are rapidly cleared from circulation. In mammals, one mechanism by which this occurs is via the low-density lipoprotein receptor-related protein (LRP receptor), which binds to inhibitory complexes made by antithrombin, PA1-1, and neuroserpin, causing uptake and subsequent signaling events. Thus, as a consequence of the conformational change during serpin-enzyme complex formation, serpins may act as signaling molecules that alert cells to the presence of protease activity. Serpins play very important roles in the maintenance of various physiologically important systems. As knowledge of the workings of proteins of this family grows, new understanding is gained of the mechanisms by which they inhibit target proteases, using conformational changes for which the structure of serpins is uniquely adapted. This finely balanced system is utilized to healthy benefit in the control of serpin function by modulators, arguably the most striking examples of which occur in the control of proteolytic cascades, such as the coagulation system. Serpins also play very important intracellular roles: one example is the protection of immune cells from their own cytotoxic proteases.
Serpin (Serine Protease Inhibitor) Related Studies
- Travis J, et al. (1990) Serpins: structure and mechanism of action. Biol Chem Hoppe Seyler. 371 Suppl: 3-11.
- Irving JA, et al. (2000). Phylogeny of the Serpin Superfamily: Implications of Patterns of Amino Acid Conservation for Structure and Function. Genome Res. 10(12): 1845–64.
- Irving J, et al. (2002). Serpins in prokaryotes. Mol Biol Evol. 19 (11): 1881–90.
- van Gent D, et al. (2003) Serpins: structure, function and molecular evolution. Int J Biochem Cell Biol. 35(11): 1536-47.
- Cao C, et al. (2006). Endocytic receptor LRP together with tPA and PAI-1 coordinates Mac-1-dependent macrophage migration. Embo J. 25 (9): 1860–70.
- Steenbakkers PJ, et al. (2008). A serpin in the cellulosome of the anaerobic fungus Piromyces sp. strain E2. Mycol. Res. 112 (Pt 8): 999–1006.
