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MMP-9, Active, human recombinant

>95% Pure, Active, Human Recombinant, MMP-9/Matrix Metallopeptidase 9. A Protein involved in breakdown of extracellular matrix
Catalog #: 7867
SKU-Size Size Price Qty
7867-500 500 Units
7867-1000 1000 Units
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Product Details

Alternate Name Matrix Metalloproteinase-9, Gelatinase B, 92 kDa Type IV Collagenase, MMP9, CLG4B, GELB, MANDP2
Gene Symbol MMP-9
Gene ID 4319
Accession # P14780
Source E. coli
Appearance Lyophilized
Physical Form Description Lyophilized from a proprietary buffer
Molecular Weight 39 kDa (aa 107-457 + NT His Tag)
Purity by SDS-PAGE ≥95%
Biological Activity The activity was determined using fluorogenic substrate McaPLGL-Dpa-AR-NH2. The specific activity is > 70 U/µg.
Reconstitution Instructions Reconstitute with pre-chilled 30% Glycerol solution (in dH2O) to 10 U/µl and incubate on ice until it completely dissolves. Aliquot and store the reconstituted MMP-9 at -20°C. Stable for 2 months after reconstitution.
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans


Matrix metallopeptidase 9 (MMP-9), also known as 92 kDa type IV collagenase, 92 kDa gelatinase or gelatinase B, is the mostly studied MMP, due to its fundamental role in cancer biology, autoimmune disease, and other conditions. This enzyme degrades various substrates including gelatin, collagen types IV and V, and elastin. MMP-9 is structurally a multi-domain metalloenzyme, composed of a prodomain, a catalytic domain, a gelatin binding domain, a metal-binding domain, and a carboxyl terminal hemopexin like domain. This active human MMP-9 is composed of the catalytic domain, a gelatin binding domain, and a metal binding domain (AA 107-457). The protein was expressed in E.coli and purified and refolded using proprietary techniques.

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Elyse S. Fischer , Bismaleimide cross‐linked anthrax toxin forms functional octamers with high specificity in tumor targeting . Protein Sci ,Apr 19; 30942916
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