MMP9 polyclonal, anti-human, mouse, rat
€388.00
In stock
SKU
BS6893
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 taphylococcal 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. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Alternative Name:
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB, MMP9, CLG4B
Application Dilution: WB: 1:500~1:2000, IHC: 1:50~1:200
Specificity: MMP9 polyclonal antibody detects endogenous levels of MMP9 protein.
Immunogen:
Recombinant full length Human MMP9.
MW: ~ 92 kDa
Swis Prot.: P14780
Purification & Purity:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Format:
1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Storage:
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
For research use only, not for use in diagnostic procedure.
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 taphylococcal 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. MMP-1 is down-regulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Alternative Name:
Matrix metalloproteinase-9, MMP-9, 92 kDa gelatinase, 92 kDa type IV collagenase, Gelatinase B, GELB, MMP9, CLG4B
Application Dilution: WB: 1:500~1:2000, IHC: 1:50~1:200
Specificity: MMP9 polyclonal antibody detects endogenous levels of MMP9 protein.
Immunogen:
Recombinant full length Human MMP9.
MW: ~ 92 kDa
Swis Prot.: P14780
Purification & Purity:
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Format:
1 mg/ml in Phosphate buffered saline (PBS) with 0.05% sodium azide, approx. pH 7.2.
Storage:
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
For research use only, not for use in diagnostic procedure.
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