MMP-9 Protein, Mouse, Recombinant (His)

Catalog No. TMPJ-00957

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.

MMP-9 Protein, Mouse, Recombinant (His)

Catalog No. TMPJ-00957

Pack Size	Price	Availability
10 μg	$184	7-10 days
50 μg	$545	7-10 days
500 μg	$1,900	7-10 days
1 mg	$2,970	7-10 days

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Product Information

Biological Activity	Activity has not been tested. It is theoretically active, but we cannot guarantee it. If you require protein activity, we recommend choosing the eukaryotic expression version first.
Description	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.
Species	Mouse
Expression System	HEK293 Cells
Tag	C-10xHis
Accession Number	P41245
Synonyms	MMP-9,Matrix metalloproteinase-9,GELB,Gelatinase B,92 kDa type IV collagenase,92 kDa gelatinase
Amino Acid	Ala20-Pro730
Construction	Ala20-Pro730. The proenzyme needs to be activated by APMA for an activated form.
Protein Purity	Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight	100 KDa (reducing condition)
Endotoxin	< 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation	Supplied as a 0.2 μm filtered solution of 20 mM Tris-HCl, 150 mM NaCl, 20% Glycerol, pH7.5.
Stability & Storage	Lyophilized powders can be stably stored for over 12 months, while liquid products can be stored for 6-12 months at -80°C. For reconstituted protein solutions, the solution can be stored at -20°C to -80°C for at least 3 months. Please avoid multiple freeze-thaw cycles and store products in aliquots.
Shipping	Shipping with blue ice.
Research 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.