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MMP-9 Protein, Mouse, Recombinant (His)

カタログ番号 TMPJ-00957
別名: Matrix metalloproteinase-9, 92 kDa gelatinase, GELB, Gelatinase B, MMP-9, 92 kDa type IV collagenase

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
MMP-9 Protein, Mouse, Recombinant (His)
パッケージサイズ 在庫状況 単価(税別)
10 μg 約5 days ¥ 42,500
50 μg 約5 days ¥ 125,000
500 μg 約5 days ¥ 436,000
1 mg 約5 days ¥ 682,000
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生物学的特性に関する説明
Technical Params
Product Properties
説明 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 Host HEK293 Cells
Tag C-10xHis
Accession Number P41245
別名 Matrix metalloproteinase-9, 92 kDa gelatinase, GELB, Gelatinase B, MMP-9, 92 kDa type IV collagenase
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)
分子量 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℃. For reconstituted proteinsolutions, 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

In general, Lyophilized powders are shipping with blue ice. Solutions are shipping with dry 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.

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Keywords

MMP-9 Protein, Mouse, Recombinant (His) Matrix metalloproteinase-9 92 kDa gelatinase GELB Gelatinase B MMP-9 MMP9 MMP 9 92 kDa type IV collagenase recombinant recombinant-proteins proteins protein