Description
Recombinant Mouse MMP-9 Protein (His Tag) | PKSM041109 | Gentaur US, UK & Europe Disrtribition
Synonyms: Matrix metalloproteinase-9; MMP-9; 92 kDa gelatinase; 92 kDa type IV collagenase; Gelatinase B; GELB
Active Protein: N/A
Activity: Recombinant Mouse Matrix Metalloproteinase-9 is produced by our Mammalian expression system and the target gene encoding Ala20-Pro730 is expressed with a 10His tag at the C-terminus.
Protein Construction: Recombinant Mouse Matrix Metalloproteinase-9 is produced by our Mammalian expression system and the target gene encoding Ala20-Pro730 is expressed with a 10His tag at the C-terminus.
Fusion Tag: C-10His
Species: Mouse
Expressed Host: Human Cells
Shipping: This product is provided as liquid. It is shipped at frozen temperature with blue ice/gel packs. Upon receipt, store it immediately at<-20°C.
Purity: > 95 % as determined by reducing SDS-PAGE.
Endotoxin: < 1.0 EU per μg as determined by the LAL method.
Stability and Storage: Store at < -20°C, stable for 6 months. Please minimize freeze-thaw cycles.
Molecular Mass: 80.2 kDa
Formulation: Supplied as a 0.2 μm filtered solution of 20mM Tris, 150mM NaCl, pH7.5 .
Reconstitution: Not Applicable
Background: Matrix metalloproteinases are a family of zinc and calcium dependent endopeptidases with the combined ability to degrade all the components of the extracellular matrix. MMP-9 (gelatinase B) can degrade a broad range of substrates including gelatin, collagen types IV and V, elastin and proteoglycan core protein. It is believed to act synergistically with interstitial collagenase (MMP1) in the degradation of fibrillar collagens as it degrades their denatured gelatin forms. MMP-9 is produced by keratinocytes, monocytes, macrophages and PMN leukocytes. MMP-9 is present in most cases of inflammatory responses. Structurally, MMP-9 may be divided into five distinct domains: a prodomain which is cleaved upon activation, a gelatinbinding domain consisting of three contiguous fibronectin type II units, a catalytic domain containing the zinc binding site, a prolinerich linker region, and a carboxyl terminal hemopexinlike domain.
Research Area: N/A
