Matrix metalloproteinases (MMP) are proteolytic enzymes capable of degrading extracellular matrix. Stromelysin, a member of the matrix metalloproteinase family, demonstrates wide substrate specificity with the ability to degrade proteoglycan, fibronectin, laminin, casein, and the nonhelical region of collagen. The two forms of stromelysin (SL), types 1 (MMP-3) and 2 (MMP-10), share 82% sequence homology, but exhibit differences in cellular synthesis and inducibility by cytokines and growth factors in vitro.
Host Species: Mouse
Species Reactivity: Human. Others not known.
Epitope: Not determined
Immunogen: Human recombinant MMP-10 (stromelysin-2 protein)
Molecular Weight: ∽57kDa (proform) and ∽44kDa (active form)
Positive Control: Conditioned, serum-free medium from (TPA-treated) human large cell lymphoma U937 cells; Placenta; Bladder, breast and ovarian CAs
Cellular Localization: Cytoplasmic
- Western Blotting
- Immunoprecipitation (Native verified)
USA: RUO; Int'l: RUO
1. Bord S, et al. Bone 199823(1):7-12.
2. Saarialho-Kere UK: Arch Dermatol Res 1998290 Suppl:S47-S54.