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MMP-9 Antibody
Purified Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC, IP |
|---|---|
| Primary Accession | P14780 |
| Reactivity | Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 78458 Da |
| Gene ID | 4318 |
|---|---|
| Other Names | MMP9, MMP-9, MMP 9, Matrix metalloproteinase-9, Matrix metalloproteinase 9, Gelatinase B, 92kDa type IV collagenase |
| Target/Specificity | MMP-9 |
| Formulation | 100 µg (0.5 mg/ml) affinity purified rabbit anti-rat MMP-9 polyclonal antibody in phosphate buffered saline (PBS), pH 7.2, containing 50% glycerol, 1% BSA, 0.02% thimerosal. |
| Handling | The antibody solution should be gently mixed before use. |
| Background Descriptions | |
| Precautions | MMP-9 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | MMP9 |
|---|---|
| Synonyms | CLG4B |
| Function | Matrix metalloproteinase that plays an essential role in local proteolysis of the extracellular matrix and in leukocyte migration (PubMed:2551898, PubMed:1480034, PubMed:12879005). Could play a role in bone osteoclastic resorption (By similarity). Cleaves KiSS1 at a Gly-|-Leu bond (PubMed:12879005). Cleaves NINJ1 to generate the Secreted ninjurin-1 form (PubMed:32883094). Cleaves type IV and type V collagen into large C-terminal three quarter fragments and shorter N- terminal one quarter fragments (PubMed:1480034). Degrades fibronectin but not laminin or Pz-peptide. |
| Cellular Location | Secreted, extracellular space, extracellular matrix |
| Tissue Location | Detected in neutrophils (at protein level) (PubMed:7683678). Produced by normal alveolar macrophages and granulocytes. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
The mammalian Matrix metalloproteinases (MMPs) degrade extracellular matrix in physiological and pathological processes. After cleavage of a single peptide domain of about 20 amino acids, the MMPs are secreted in latent forms. Upon activation, the N-terminal propeptide domain is cleaved to generate the active forms of MMP. MMP-9 (92 kDa type IV collagenase, Gelatinase-B) contains the basic structure of propeptide, catalytic, and hemopexin domains. It is an important proteinase in tissue remodeling.
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