Recombinant Human Alpha 1 antichymotrypsin protein (rFc Tag)
Species
Human
Purity
>90 %, SDS-PAGE
Tag
rFc Tag
Activity
not tested
Cat no : Eg12047
Validation Data Gallery
Product Information
| Purity | >90 %, SDS-PAGE |
| Endotoxin | <0.1 EU/μg protein, LAL method |
| Activity |
Not tested |
| Expression | HEK293-derived Human Alpha 1 antichymotrypsin protein Asn26-Ala423 (Accession# P01011-1) with a rabbit IgG Fc tag at the C-terminus. |
| GeneID | 12 |
| Accession | P01011-1 |
| PredictedSize | 71.1 kDa |
| SDS-PAGE | 75-100 kDa, reducing (R) conditions |
| Formulation | Lyophilized from 0.22 μm filtered solution in PBS, pH 7.4. Normally 5% trehalose and 5% mannitol are added as protectants before lyophilization. |
| Reconstitution | Briefly centrifuge the tube before opening. Reconstitute at 0.1-0.5 mg/mL in sterile water. |
| Storage Conditions |
It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
|
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the recommended temperature. |
Background
Human SerpinA3, also known as Alpha 1-antichymotrypsin (AACT), is a member of the serine protease inhibitor class, and is a plasma alpha globulin glycoprotein which increases in the blood during the inflammatory process. SerpinA3, is also an inhibitor of neutrophil cathepsin G, mast cell chymases and pancreatic chymotrypsin. SerpinA3 is produced primarily in the liver, and is identified as an acute-phase inflammatory protein. SerpinA3 deficiency has been associated with liver disease. SerpinA3 has also been implicated in the pathology of a number of devastating human diseases including chronic obstructive pulmonary disease (COPD), Parkinson's disease (PD), Alzheimer's disease (AD), Stroke, Cystic Fibrosis, Cerebral Haemorrhage and Multiple System Atrophy.
References:
1.Rabin, M et al. Somatic cell and molecular genetics vol. 12,2 (1986): 209-14. 2.Liu, Tao et al. Journal of proteome research vol. 4,6 (2005): 2070-80. 3.Hwang, S R et al. The Journal of biological chemistry vol. 274,3 (1999): 1821-7. 4.Travis, J et al. Biochemistry vol. 17,26 (1978): 5651-6.