Mouse SERPINA3C / Serpina3c Protein (His Tag)

Serine Protease Inhibitor A3C ( SERPINA3C / Serpina3c ) Protein

SERPINA3C / Serpina3c Protein Product Information

• Synonym: Serpina3c, 1A1, Kalbp, Klkbp, MGC144822, spi2
• Protein Construction: A DNA sequence encoding the extracellular domain of mouse SERPINA3C ( NP_032484.1 ) precursor ( Met 1 - Ala 417 ) was expressed, with a C-terminal polyhistidine tag
• Source: Mouse
• Expression Host: Human Cells

SERPINA3C / Serpina3c Protein QC Testing

• Purity: > 95 % as determined by SDS-PAGE
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Stability: Samples are stable for up to twelve months from date of receipt at -70℃
• Predicted N terminal: Asp 23
• Molecular Mass: The secreted recombinant mouse SERPINA3C comprises 406 amino acids with a predicted molecular mass of 46 kDa. As a result of diiferent glycosylation, the apparent molecular mass of rm SERPINA3C is approximately 50-60 kDa and 110 kDa in SDS-PAGE under reducing conditions
• Formulation: Lyophilized from sterile PBS , pH 7.4
• SDS-PAGE: Serpina3c protein

SERPINA3C / Serpina3c Protein Usage Guide

• Storage: Store it under sterile conditions at -70℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
• Reconstitution: A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.

SERPINA3C / Serpina3c Protein Description

Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. 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 been identified.

Serine protease inhibitor A3C, also known as Kallikrein-binding protein, KBP, and Serpina3c, is a secreted protein which belongs to the serpin family. The reactive center loop (RCL) extends out from the body of the Serpina3c protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site within the RCL, establishing a covalent linkage between the serpin reactive site and the protease. The resulting inactive serpin-protease complex is highly stable. Variability within the reactive center loop (RCL) sequences of Serpina3 paralogs may determine target protease specificity.

References

1. Irving JA. et al., 2000, Genome Res. 10: 1845-64. 
2. Irving J. et al., 2002, Mol Biol Evol 19 (11): 1881-90.
3. Forsyth, S. et al., 2003, Genomics 81: 336-345. 
4. Horvath, AJ. et al., 2004, J. Mol. Evol. 59: 488-497.
5. Steenbakkers PJ. et al., 2008, Mycol. Res. 112 (Pt 8): 999-1006.