Matrix metallopeptidase 9 (MMP-9) is also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B (GELB), CLG4B, is secreted from neutrophils, macrophages, and a number of transformed cells, and is the most complex family member in terms of domain structure and regulation of its activity.
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Structurally, MMP9 maybe 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.
This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin.
MMP9 is involved in a variety of autoimmune diseases such as systemic lupus erythematosus, rheumatoid arthritis, and multiple sclerosis, and be regarded as a potential therapeutic target.
特徴
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 50.8 kDa.
The protein migrates as 65 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
仕様
容量：50ug
Source：Human MMP-9, His Tag (MM9-H5229) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 469 (Accession # AAH06093.1). It needs to be activated by agents such as APMA in vitro to have hydrolytic activity.
Species Reactivity：Human
Host：HEK293
Tag：C-6×His
Exp Region：Ala 20 - Pro 469
Format：Liquid
Conjugate：Unconjugated
Protein ID：AAH06093.1
Endotoxin：1.0 EU per μg
Purity：95%
Buffer：25 mM Tris, 150 mM NaCl, 20% glycerol, pH7.5
