Mouse MMP-9 (20-471) Protein, His Tag (active enzyme, MALS verified)

DESCRIPTION

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. . 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.

DETAILS

Tag: C-10×His
Host: HEK293
Size: 1mg
Buffer: 25 mM Tris,150 mM NaCl,pH7.5,50% Glycerol
Format: Liquid
Purity: 95%
Source: Mouse MMP-9 (20-471), His Tag (MM9-M52H1) is expressed from human 293 cells (HEK293). It contains AA Ala 20 - Pro 471 (Accession # P41245-1). It needs to be activated by agents such as APMA in vitro to have hydrolytic activity.
Storage: -70℃
Category: Enzymes
Molecule: MMP-9
Conjugate: Unconjugated
Stability: ● -20°C to -70°C for 12 months in lyophilized state; ● -70°C for 3 months under sterile conditions after reconstitution. For long term storage, the product should be stored at lyophilized state at -20°C or lower.
Exp Region: Ala 20 - Pro 471
Swiss-prot: P41245-1
Package Size: 1mg*1
Characteristics: This protein carries a polyhistidine tag at the C-terminus. The protein has a calculated MW of 52.0 kDa. The protein migrates as 60-66 kDa under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin Level: 1.0 EU per μg
Molecular Weight: 52.0 kDa
Shipping Condition: Dry ice
Species Reactivity: Mouse
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