SerpinA10 Antibody

SerpinA10 Antibody Datasheet

SerpinA10 Antibody Product Information

• 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). Total IgG was purified by Protein A affinity chromatography.

SerpinA10 Antibody Usage Guide

• Specificity: Mouse SerpinA10
• Western blot: This antibody can be used at 1-2 μg/mL with the appropriate secondary reagents to detect Mouse SerpinA10 in WB.
• Direct ELISA: This antibody can be used at 0.5-1.0 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.

SerpinA10 Antibody Background

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

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