Function
Snake venom zinc metalloproteinase, which causes strong hemorrhagy and dermonecrosis by degrading the extracellular matrix. Its strong hemorrhagic activity is independent of binding to extracellular matrix (ECM) proteins and is instead due to its high catalytic activity, in contrast to P-III metalloproteinases, which bind to the ECM but have lower catalytic activity. Its unique dermonecrotic action may be explained by its efficacy in laminin hydrolysis (Probable).
Biological Context
Subcellular Location: Secreted
Tissue Specificity: Expressed by the venom gland
Product Specifications
Recombinant Bothrops atrox Zinc metalloproteinase atroxlysin-1 is a recombinant protein from Bothrops atrox (Barba amarilla) (Fer-de-lance), expressed in E.coli, covering amino acids 1-202aa, with N-terminal 10xHis-tagged and C-terminal Myc-tagged tag, molecular weight 30.4kDa, purity Greater than 85% as determined by SDS-PAGE.. Suitable for ELISA and Western Blot applications.
