2μg (R: reducing condition, N: non-reducing condition).
Product Details
Product Details
Product Specification
Species | Human |
Synonyms | A1A, A1AT, AAT, alpha-1-antitrypsin, alpha1AT, nNIF, PI, PI1, SERPINA1 |
Accession | NP_000286.3 |
Amino Acid Sequence | Glu25-Lys418 with His Tag at C-Terminus |
Expression System | HEK293 |
Molecular Weight | 53-68kDa (Reducing) |
Purity | >95% by SDS-PAGE |
Conjugation | Unconjugated |
Tag | His Tag |
Physical Appearance | Lyophilized Powder |
Storage Buffer | PBS, PH7.4, 5% trehalose |
Reconstitution | Reconstitute at 0.1-1 mg/ml according to the size in ultrapure water after rapid centrifugation. |
Stability & Storage | · 12 months from date of receipt, lyophilized powder stored at -20 to -80℃. |
Reference | Hunt JM, Tuder R. Alpha 1 anti-trypsin: one protein, many functions. Curr Mol Med. 2012 Aug;12(7):827-35. |
Background
SerpinA1, also known as Alpha-1 Antitrypsin (AAT), is a prototype member of the Serpin superfamily, which are serine protease inhibitors. This inhibitor specifically targets the protease neutrophil elastase. Primarily produced in the liver, Alpha-1 Antitrypsin functions as an antiprotease, with its main role being the inactivation of neutrophil elastase to prevent tissue damage. SerpinA1 (Alpha-1 Antitrypsin), an acute phase protein and a classical inhibitor of neutrophil elastase, is localized within lipid rafts in primary human monocytes in vitro. Its association with monocytes is modulated by cholesterol levels; it is inhibited by cholesterol-depleting agents such as nystatin, filipin, methyl-beta-cyclodextrin (MbetaCD), and oxidized low-density lipoprotein (oxLDL), and conversely, enhanced by the presence of free cholesterol.
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