Serpin A10 Protein, Mouse, Recombinant (His)

カタログ番号 TMPY-01855

別名: serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10, ZPI, serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 10, Serpin A10, PZI

Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.

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Serpin A10 Protein, Mouse, Recombinant (His)

パッケージサイズ	在庫状況	単価(税別)
100 μg	約5 days	￥ 161,000

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Product Properties

参考文献

説明

Species	Mouse
Expression Host	HEK293 Cells
Tag	His
Accession Number	Q8R121-1
別名	serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10, ZPI, serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 10, Serpin A10, PZI
Construction	The mature form of Mouse SERPINA10 isoform 1 (Q8R121-1) (Met 1-Leu 448) was fused with a polyhistidine tag at the C-terminus.
Protein Purity	> 95 % as determined by SDS-PAGE
分子量	51 kDa (predicted)

Endotoxin	< 1.0 EU/μg of the protein as determined by the LAL method.
Formulation	Lyophilized from a solution filtered through a 0.22 μm filter, containing PBS, pH 7.4. Typically, a mixture containing 5% to 8% trehalose, mannitol, and 0.01% Tween 80 is incorporated as a protective agent before lyophilization.
Reconstitution	A Certificate of Analysis (CoA) containing reconstitution instructions is included with the products. Please refer to the CoA for detailed information.
Stability & Storage	It is recommended to store recombinant proteins at -20°C to -80°C for future use. Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at-80℃. For reconstituted proteinsolutions, the solution can be stored at -20°c to -80'c for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	In general, Lyophilized powders are shipping with blue ice.
Research Background	Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA1 and ZPI, is a secreted protein that belongs to the serpin family. It is expressed by the liver and secreted in plasma. SERPINA1 / Serpin-A1 inhibits factor Xa activity in the presence of protein Z, calcium and phospholipid. Serpins are a group of proteins with similar structures that were first identified as a set of proteins able to inhibit proteases. The acronym serpin was originally coined because many serpins inhibit chymotrypsin-like serine proteases (serine protease inhibitors). Over 1 serpins have now been identified, these include 36 human proteins, as well as molecules in plants, fungi, bacteria, archaea and certain viruses. Serpins are the largest and most diverse family of protease inhibitors. Most serpins control proteolytic cascades, certain serpins do not inhibit enzymes, but instead perform diverse functions such as storage (ovalbumin, in egg white), hormone carriage proteins (thyroxine-binding globulin, cortisol-binding globulin) and tumor suppressor genes (maspin). Most inhibitory serpins target chymotrypsin-like serine proteases. These enzymes are defined by the presence of a nucleophilic serine residue in their catalytic site. Some serpins inhibit other classes of protease. A number of such serpins have been shown to target cysteine proteases. These enzymes differ from serine proteases in that they are defined by the presence of a nucleophilic cysteine residue, rather than a serine residue, in their catalytic site.

参考文献

1. Han X, et al., 1998, Proc Natl Acad Sci. USA 95: 9250-5. 2. Han X, et al., 2000, Blood 96: 3049-55. 3. Irving JA, et al.,2000, Genome Res. 10 (12): 1845-64. 4. Irving J, et al.,2002, Mol Biol Evol. 19 (11): 1881-90. 5. Rawlings ND, et al.,2004, Biochem J. 378 (Pt 3): 705-16. 6. Water N, et al., 2004, Br J Haematol. 127:190-4. 7. Wei Z, et al., 2009, Blood 114 (17): 3662-7. 8. Whisstock JC, et al.,2010, J Biol Chem. 285 (32): 24307-12.

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Keywords

Serpin A10 Protein, Mouse, Recombinant (His) serpin peptidase inhibitor, clade A (alpha-1 antiproteinase, antitrypsin), member 10 ZPI serpin peptidase inhibitor, clade A (α-1 antiproteinase, antitrypsin), member 10 Serpin A10 PZI recombinant recombinant-proteins proteins protein