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MMP-9, Active, human recombinant protein
Matrix Metalloproteinase-9, Gelatinase B, 92 kDa Type IV Collagenase, MMP9, CLG4B, GELB, MANDP2
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P14780 |
|---|---|
| Calculated MW | 39 kDa (aa 107-457 + NT His Tag) |
| Gene ID | 4319 |
|---|---|
| Gene Symbol | MMP-9 |
| Other Names | Matrix Metalloproteinase-9, Gelatinase B, 92 kDa Type IV Collagenase, MMP9, CLG4B, GELB, MANDP2 |
| Gene Source | Human |
| Source | E. coli |
| Assay&Purity | SDS-PAGE ; ≥95% |
| Assay2&Purity2 | N/A; |
| Recombinant | Yes |
| Results | > 70 U/ µg |
| Target/Specificity | MMP-9 |
| Application Notes | 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. |
| Format | Lyophilized |
| Storage | -20°C; Lyophilized from a proprietary buffer |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Wilhelm S.M.,et al.J. Biol. Chem. 264:17213-17221(1989).
Huhtala P.,et al.J. Biol. Chem. 266:16485-16490(1991).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Deloukas P.,et al.Nature 414:865-871(2001).
Sato H.,et al.Oncogene 8:395-405(1993).
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