SerpinA3 / AACT Protein (His Tag)

Alpha-1-antichymotrypsin ( SerpinA3 / SERPINA3 ) Protein

SerpinA3 / SERPINA3 / AACT Protein Product Information

• Synonym: SERPINA3, AACT, ACT, GIG24, GIG25, MGC88254
• Protein Construction: A DNA sequence encoding the human SERPINA3 ( NP_001076.2 ) ( Met 1 - Ala 423 ) was expressed, with a C-terminal polyhistidine tag
• Source: Human
• Expression Host: Human Cells

SerpinA3 / SERPINA3 / AACT Protein QC Testing

• Purity: > 97 % as determined by SDS-PAGE
• Bio-activity: Measured by its ability to inhibit trypsin cleavage of a fluorogenic peptide substrate, Mca-RPKPVE-Nval-WRK(Dnp)-NH2 ( Anaspec, Catalog# 27114 )
  The IC₅₀ value is < 20 nM
• 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: Asn 26
• Molecular Mass: The recombinant human SERPINA3 consisting of 409 amino acids and has a calculated molecular mass of 46.5 kDa. As a result of different glycosylation, the apparent molecular mass of the recombinant protein is approximately 45kDa and 55-70 kDa in SDS-PAGE under reducing conditions
• Formulation: Lyophilized from sterile 25 mM HEPES, 0.15M NaCl , pH 7.8
  1. Normally 5 % - 8 % trehalose and mannitol are added as protectants before lyophilization. Specific concentrations are included in the hardcopy of COA.
  2. Please contact us for any concerns or special requirements.
• SDS-PAGE: SerpinA3 protein

SerpinA3 / SERPINA3 / AACT 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.

SerpinA3 / SERPINA3 / AACT Protein Description

Human SerpinA3, also known as Alpha 1-antichymotrypsin (AACT), is a plasma alpha globulin glycoprotein, and is a member of serpin superfamily of the serine protease inhibitors consisting of at least 35 members. SerpinA3 has been demonstrated to inhibit the activity of certain serine proteases, such as cathepsin G found in neutrophils, and chymases present in mast cells, by inducing a major conformational rearrangement, and thus protects some tissues from damage caused by proteolytic enzymes. This enzyme is produced primarily in the liver, and is identified as an acute-phase inflammatory protein. SerpinA3 deficiency has been associated with liver disease, and mutations of this gene have been observed in patients with Parkinson disease and chronic obstructive pulmonary disease. In addition, ACT gene polymorphism has been implicated with Alzheimer’s disease (AD), cerebral amyloid angiopathy (CAA), as well as stroke, since SerpinA3 is a major constituent of the plaques in AD and an inhibitor of amyloid beta peptide degradation.

References

1. Nilsson, L.N. et al., 2001, J. Neurosci. 21: 1444-1451.
2. Ikari, Y. et al., 2001, J. Biol. Chem. 276: 11798-11803.
3. Vila, N. et al., 2000, Stroke. 31: 2103-2105
4. Eriksson, S. et al., 1995, Proc. Natl. Acad. Sci. USA. 92: 2313-2317.
5. Skeel, A. et al., 2001, J. Biol. Chem. 276: 21932-21937.