Human Matrix Metalloproteinase 9 (MMP9) Protein
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Description
Matrix Metalloproteinase-9 is a recombinant enzyme.
Documents del producto
Product specifications
| Category | Proteins and Peptides |
| Immunogen Target | Matrix Metalloproteinase 9 (MMP9) |
| Host | E. coli |
| Recommended Dilution | Optimal dilutions/concentrations should be determined by the end user. |
| Origin | Human |
| Expression | Recombinant |
| Purity | > 95% (SDS-PAGE) |
| Size 1 | 2 µg |
| Size 2 | 10 µg |
| Size 3 | 1 mg |
| Form | Liquid |
| Tested Applications | SDS-PAGE |
| Availability | Shipped within 5-10 working days. |
| Storage | Store at 4 °C if the entire vial will be used within 2-4 weeks. Store at -20 °C for long term storage. Avoid repeated freeze/thaw cycles. |
| Dry Ice | No |
| UniProt ID | P14780 |
| Alias | GELB,CLG4B,MMP-9,MANDP2,92 kDa type IV collagenase, Gelatinase B |
| Background | Protein MMP9 |
| Status | RUO |
| Note | This product is for research use only. Not for human consumption, cosmetic, therapeutic or diagnostic use. |
Descripción
Matrix metalloproteinase 9 (MMP9), also known as gelatinase B, is an enzyme belonging to the matrix metalloproteinase family. MMP-9 is a zinc-dependent endopeptidase. It is synthesized as a proenzyme, and requires activation by other proteases to become active. The active form of MMP-9 can degrade various components of the extracellular matrix, including collagen type IV, which is a major component of the basement membrane. MMP-9 is implicated in several physiological and pathological processes, including tissue remodeling, angiogenesis, wound healing, inflammation, and cancer metastasis. It is involved in the breakdown of the extracellular matrix, which is essential for processes like tissue repair and remodeling. However, dysregulation of MMP-9 activity can contribute to pathological conditions such as excessive tissue degradation, tumor invasion, and metastasis.MMP-9 activity is tightly regulated at multiple levels, including transcriptional regulation, post-translational modification, and inhibition by tissue inhibitors of metalloproteinases (TIMPs)
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