MMP-9 Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB |
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Primary Accession | P14780 |
Other Accession | AAM97934 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 78458 Da |
Gene ID | 4318 |
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Application & Usage | Western blotting (0.5-4 µg/ml). However, the optimal concentrations should be determined individually. The antibody recognizes the full length (proenzyme, 92 kDa) and cleaved (active enzyme, 84 kDa) MMP-9 in samples from human, mouse, and rat origins. |
Other Names | GELB , EC 3.4.24.35 , CLG4B , Matrix metalloproteinase |
Target/Specificity | MMP-9 |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | 100 µg (0.5 mg/ml) peptide affinity purified rabbit polyclonal antibody in phosphate-buffered saline (PBS) containing 30% glycerol, 0.5% BSA, and 0.01% thimerosal. |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | MMP-9 Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | MMP9 |
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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. |
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Provided below are standard protocols that you may find useful for product applications.
Background
The matrix metalloproteinases (MMP) are a family of peptidase enzymes responsible for the degradation of extracellular matrix components, including collagen, gelatin, fibronectin, laminin and proteoglycan. Transcription of MMP genes is differentially activated by phorbol ester, lipopolysaccharide (LPS) or staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 92-kDa type IV collagenase or gelatinase B) has been shown to degrade bone collagens in concert with MMP-1 (also designated interstitial collagenase, fibroblast collagenase or collagenase-1), and cysteine proteases and may play a role in bone osteoclastic resorption.
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