MMP9 Antibody
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Application ![]()
| WB, IF, E, IHC-P |
---|---|
Primary Accession | P14780 |
Other Accession | NP_004985, 74272287 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | IgG |
Calculated MW | 78458 Da |
Concentration (mg/ml) | 1 mg/mL |
Conjugate | Unconjugated |
Application Notes | MMP9 antibody can be used for detection of MMP9 by Western blot at 1 - 2 µg/ml. |
Gene ID | 4318 |
---|---|
Other Names | Matrix metalloproteinase-9, MMP-9, 3.4.24.35, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB, 67 kDa matrix metalloproteinase-9, 82 kDa matrix metalloproteinase-9, MMP9, CLG4B |
Target/Specificity | MMP9; MMP9 antibody is human, mouse and rat reactive. At least three isoforms of MMP9 are known to exist; this antibody only recognizes the two longest isoforms. |
Reconstitution & Storage | MMP9 antibody can be stored at 4℃ for three months and -20℃, stable for up to one year. |
Precautions | MMP9 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:12879005, PubMed:1480034, PubMed:2551898). 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. |
For Research Use Only. Not For Use In Diagnostic Procedures.
Provided below are standard protocols that you may find useful for product applications.
BACKGROUND
The matrix metalloproteinase (MMP) family are a family of proteins that are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases (1). MMP9 degrades type IV and V collagens (2) and studies suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow (3) and plays a role in tumor-associated tissue remodeling (4).
REFERENCES
Iyer RP, Patterson NL, Fields GB, et al. The history of matrix metalloproteinases: milestones, myths, and misperceptions. Am. J. Heart Circ. Physiol 2012; 303:H919-30.
Murphy G, Knauper V, Atkinson S, et al. Matrix metalloproteinases in arthritic disease. Arthritis Res. 2002; 4 Suppl. 3:S39-49.
Sweeney EA, Lortat-Jacob H, Priestley GV, et al. Sulfated polysaccharides increase plasma levels of SDF-1 in monkeys and mice: involvement in mobilization of stem/progenitor cells. Blood 2002; 99:44-51.
Rhee JW, Lee KW, Sohn WJ, et al. Regulation of matrix metalloproteinase-9 gene expression and cell migration by NF-kappa B in response to CpG-oligodeoxynucleotides in RAW 264.7 cells. Mol. Immunol. 2007; 44:1393-400.

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