MMP-9, Active, human recombinant | 7867

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.

7867 | MMP-9 Active human recombinant DataSheet

Biomolecule/Target: MMP-9

Synonyms: Matrix Metalloproteinase-9, Gelatinase B, 92 kDa Type IV Collagenase, MMP9, CLG4B, GelB, MANDP2

Alternates names: Protein A/G

Taglines: >95% Pure, Active, Human Recombinant, MMP-9/Matrix Metallopeptidase 9. A Protein involved in breakdown of extracellular matrix

NCBI Gene ID #: N/A

NCBI Gene Symbol: N/A

Gene Source: N/A

Accession #: N/A

Recombinant: Yes

Source: E. coli

Purity by SDS-PAGEs: 98%

Assay: SDS-PAGE

Purity: N/A

Assay #2: N/A

Endotoxin Level: <0.1 ng/g

Activity (Specifications/test method): N/A

Biological activity: N/A

Results: N/A

Binding Capacity: N/A

Unit Definition: One unit (U) of the activity is defined as the amount of enzyme that releases 1 pmole of Mca from Mca-PLGL-Dpa-AR-NH2 per min. at 37°C.

Molecular Weight: 59.7 kDa

Concentration: N/A

Appearance: Lyophilized

Physical form description: Lyophilized from a proprietary buffer

Reconstitution Instructions: Reconstitution in HO to a concentration of 5 mg/ml gives a clear solution.

Amino acid sequence: N/A