Datasheet
| Product Name | MMP9 Rabbit mAb |
| Background | This enzyme, MMP9, is a matrix metalloproteinase that degrades components of the extracellular matrix. It specifically cleaves gelatin types I and V and collagen types IV and V. Its activity depends on the binding of essential cofactors—two zinc ions and three calcium ions per subunit. A key regulatory mechanism involves a cysteine-switch motif, in which a conserved cysteine binds the catalytic zinc ion to keep the enzyme inactive until its dissociation during activation. MMP9 is inhibited by histatin-3 (histatin-5) and is activated by agents like 4-aminophenylmercuric acetate and phorbol ester. Functionally, it plays an important role in proteolysis related to leukocyte migration and may contribute to bone resorption. Clinically, defects in MMP9 have been linked to an increased susceptibility to lumbar disk herniation (LDH), a leading cause of low-back pain and unilateral leg pain, and it may also be implicated in joint destruction in arthritis. The enzyme exists in multiple active forms (64, 67, and 82 kDa) and displays diverse structural features, including fibronectin type-II and hemopexin-like domains. It is typically produced by alveolar macrophages and granulocytes, and can exist as a monomer, a disulfide-linked homodimer, or a heterodimer with a 25 kDa protein. |
| Reactivity | Mouse, Rat |
| Source | Rabbit IgG, Kappa |
| Applications | WB; IHC; IF; IP; ELISA |
| Dilutions | IHC 1:200-1:1000, WB 1:500-1:5000, IF 1:200-1:1000, ELISA 1:5000-1:20000, IP 1:50-1:200 |
| Purification | Protein A |
| Formulation | PBS, 50% glycerol, 0.05% Proclin 300, 0.05%BSA |
| Storage and Stability | -20°C/1 year |
| UniProt Accession # | P14780 |
| Protein Name | MMP9 |
| Gene Name | MMP9 CLG4B |
| Gene ID | 4318 |
| Other Names | Matrix metalloproteinase-9 (MMP-9;EC 3.4.24.35;92 kDa gelatinase;92 kDa type IV collagenase;Gelatinase B;GELB) [Cleaved into: 67 kDa matrix metalloproteinase-9;82 kDa matrix metalloproteinase-9] |