Leukocyte Elastase Inhibitor/Serpin B1/SERPINB1 Protein(C-6His) (recombinant human)

Protein Construction: Recombinant Human Serine Protease Inhibitor-clade B1 is produced by our Mammalian expression system and the target gene encoding Met1-Pro379 is expressed with a 6His tag at the C-terminus. Sequence: Met 1-Pro379. Fusion tag: C-6His Endotoxin: < 1.0 EU per µg as determined by the LAL method. Apparent Molecular Mass: 44 kDa. Protein function: SERPINB1 is a member of the serpin family and Ov-serpin subfamily. As protease inhibitors, serpins have an array of functions including regulating blood coagulation, fibrinolysis, the complement pathway, angiogenesis, inflammation, tumor suppression, extracellular matrix remodeling, and cell motility. SERPINB1 regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Reactive bond 1 of SerpinB1 is specific for reaction with chymotrypsin-like protease such as cathepsin G, chymotrypsin or chymase. Reactive bond 2 of SerpinB1 is specific for reaction with elastase-like protease such as neutrophyl elastase, proteinase-3, pancreatic elastase or PSA. In addition, SERPINB1 also functions as a potent intracellular inhibitor of granzyme H. Protein function: Regulates the activity of the neutrophil proteases elastase, cathepsin G, proteinase-3, chymase, chymotrypsin, and kallikrein-3. Also functions as a potent intracellular inhibitor of granzyme H. [The UniProt Consortium]