Alpha-1-antitrypsin

• Product Name: Alpha-1-antitrypsin
  
• Catalog No.: P2020-112
  
• RefSeq Links: UniProt: P01009; NP_000286.3; NM_000295.4; PIR: A21853; GeneID: 5265
  
• Synonyms: Alpha-1 protease inhibitor; Alpha-1-antiproteinase; Serpin A1; A1AT Protein; Alfa1 antitrypsin; Alpha 1-antitrypsin; Alpha 1-Proteinase Inhibitor; Alpha 1-proteinase inhibitor (human); Alpha 1-proteinase inhibitor, human; Alpha-1 protease inhibitor; Alpha-1 proteinase inhibitor (human); Alpha-1-antiproteinase; Alpha-1-antitrypsin; Alpha-1-proteinase Inhibitor (human); Alpha-1-proteinase inhibitor human; Alpha-1-proteinase Inhibitor, Human; Alpha-1-proteinase inhibitor, human; Alpha1-proteinase Inhibitor; Alpha1-proteinase inhibitor (human); alpha1-proteinase inhibitor human; API
  

• Species: Homo sapiens
• Tags: His-tag, N-terminal
• Sequence without tags (AA 25-418):
  EDPQGDAAQKTDTSHHDQDHPTFNKITPNLAEFAFSLYRQLAHQSNSTNIFFSPVSIATA
  FAMLSLGTKADTHDEILEGLNFNLTEIPEAQIHEGFQELLRTLNQPDSQLQLTTGNGLFL
  SEGLKLVDKFLEDVKKLYHSEAFTVNFGDTEEAKKQINDYVEKGTQGKIVDLVKELDRDT
  VFALVNYIFFKGKWERPFEVKDTEEEDFHVDQVTTVKVPMMKRLGMFNIQHCKKLSSWVL
  LMKYLGNATAIFFLPDEGKLQHLENELTHDIITKFLENEDRRSASLHLPKLSITGTYDLK
  SVLGQLGITKVFSNGADLSGVTEEAPLKLSKAVHKAVLTIDEKGTEAAGAMFLEAIPMSI
  PPEVKFNKPFVFLMIEQNTKSPLFMGKVVNPTQK
  
  

• Expression Host: human, HEK293
  
• Formulation: 10 mM Tris, 200 mM NaCl, 1 mM EDTA, 1 mM ß-Mercaptoethanol; pH 8.0
  
• Format: Liquid, stored and shipped at -80°C
• Purity: 95% as determined by SDS-PAGE
  

Alpha-1-antitrypsin also known as Alpha-1 proteinase inhibitor is a serine protease inhibitor (Serpin). Its primary mechanism is inhibiting the action of the serine protease called elastase (also plasmin and thrombin) preventing the proteolysis of elastin tissues in alveolar lung structures. The reactive center loop (RCL) of alpha-1 proteinase inhibitor extends out from the body of the protein and directs binding to the target protease. The protease cleaves the serpin at the reactive site, establishing a covalent linkage between the carboxyl group of the serpin reactive site and the serine hydroxyl of the protease. The resulting inactive serpin-protease complex is highly stable.

SDS-PAGE/Coll. Coomassie	Histogram of marked lane in gel picture

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