SerpinA10 Antikörper (Antigen Affinität reinigt)

20.02.2012

Produkt & Information von SerpinA10 Antikörper

Immunogen	Recombinant Mouse SerpinA10 protein (Catalog#50315-M08H)
Antibody Type	Rabbit Polyclonal Antibody ( Antibody Purification Platform )
Ig Type	Rabbit IgG
Formulation	0.2 μm filtered solution in PBS with 5% trehalose
Preparation	Produced in rabbits immunized with purified, recombinant Mouse SerpinA10 (rM SerpinA10;Catalog#50315-M08H; Q8R121-1; Met 1-Leu 448). SerpinA10 specific IgG was purified by Mouse SerpinA10 affinity chromatography.

SerpinA10 Antikörper Usage Guide

Specificity	Mouse SerpinA10
Western blot	This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect Mouse SerpinA10 in WB. Using a DAB detection system, the detection limit for Mouse SerpinA10 is approximately 0.5 ng/lane under non-reducing conditions and 1 ng/lane under reducing conditions.
Direct ELISA	This antibody can be used at 0.1-0.2 μg/mL with the appropriate secondary reagents to detect Mouse SerpinA10. The detection limit for Mouse SerpinA10 is approximately 0.00245 ng/well.
Storage	This antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -70℃. Preservative-Free. Sodium azide is recommended to avoid contamination (final concentration 0.05%-0.1%). It is toxic to cells and should be disposed of properly. Avoid repeated freeze-thaw cycles.

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Hintergrund von SerpinA10 Antikörper

Protein Z-dependent protease inhibitor, also known as PZ-dependent protease inhibitor, SERPINA10 and ZPI, is a secreted protein which belongs to theserpin family. It is expressed by the liver and secreted in plasma. SERPINA10 / Serpin-A10 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 1000 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.

References

Han X, et al., 1998, Proc Natl Acad Sci. USA 95: 9250-5.
Han X, et al., 2000, Blood 96: 3049-55.
Irving JA, et al.,2000, Genome Res.10 (12): 1845-64.
Irving J, et al.,2002, Mol Biol Evol. 19 (11): 1881-90.
Rawlings ND, et al.,2004, Biochem J.378 (Pt 3): 705-16.
Water N, et al., 2004, Br J Haematol. 127:190-4.
Wei Z, et al., 2009, Blood114 (17): 3662-7.
Whisstock JC, et al.,2010, J Biol Chem. 285 (32): 24307-12.

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