MMP-1 polyclonal, anti-human, mouse
€388.00
In stock
SKU
BS6232
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 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 downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Alternative Name:
Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, 22 kDa interstitial collagenase, 27 kDa interstitial collagenase, MMP1, CLG
Application Dilution: WB: 1:500~1:2000, IHC: 1:50~1:200
Specificity: MMP1 polyclonal antibody detects endogenous levels of MMP1 protein.
Immunogen:
Recombinant full length Human MMP-1.
MW: ~ 54 kDa
Swis Prot.: P03956
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:
1mg/ml in PBS with 0.1% Sodium Azide, 50% Glycerol.
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 staphylococcal enterotoxin B (SEB). MMP catalysis requires both calcium and zinc. MMP-9 (also designated 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 downregulated by p53, and abnormality of p53 expression may contribute to joint degradation in rheumatoid arthritis by regulating MMP-1 expression.
Alternative Name:
Interstitial collagenase, Fibroblast collagenase, Matrix metalloproteinase-1, MMP-1, 22 kDa interstitial collagenase, 27 kDa interstitial collagenase, MMP1, CLG
Application Dilution: WB: 1:500~1:2000, IHC: 1:50~1:200
Specificity: MMP1 polyclonal antibody detects endogenous levels of MMP1 protein.
Immunogen:
Recombinant full length Human MMP-1.
MW: ~ 54 kDa
Swis Prot.: P03956
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:
1mg/ml in PBS with 0.1% Sodium Azide, 50% Glycerol.
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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