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Rabbit Polyclonal Cleaved-MMP-1 22k (F100) antibody (STJ90098)
Supplier: St John’s Laboratory Ltd.
Recommended applications: WB, ELISA
Recommended dilution: WB 1:500-1:2000; ELISA 1:10000;
Recommended protocols: check protocols
Click or hover above images to see image description for Cleaved-MMP-1 22k (F100) Polyclonal Antibody.
Check alternative names for the antibodyExpand
MMP1 antibody, CLG antibody,|27 kDa interstitial collagenase antibody|CLG antibody|CLGN antibody|collagenase, fibroblast antibody|collagenase, interstitial antibody|Fibroblast collagenase antibody|Interstitial collagenase antibody|Matrix metallopeptidase 1 (interstitial collagenase) antibody|Matrix metalloprotease 1 antibody|Matrix Metalloproteinase 1 antibody|Matrix metalloproteinase-1 antibody|MMP 1 antibody|MMP-1 antibody|MMP1 antibody|MMP1_HUMAN antibody|OTTHUMP00000045866 antibody|Anti-MMP1 antibody [EP1247Y] (ab52631)
SCBT cat No: sc-21731|sc-6837|sc-12348|sc-8834|sc-58377|sc-137044|sc-30069|
Cleaved-MMP-1 22k (F100) Polyclonal Antibody
|Catalogue No.|| |
Cleaved-MMP-1 22k (F100) Polyclonal Antibody detects endogenous levels of fragment of activated MMP-1 22k protein resulting from cleavage adjacent to F100.
Synthesized peptide derived from Cleaved-MMP-1 22k (F100) at AA range 50-130
|Recommended dilution|| |
WB 1:500-1:2000; ELISA 1:10000;
|Molecular weight|| |
Cleaved-MMP-1 22k (F100) Antibody was tube-contained. Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Cleaved-MMP-1 22k (F100) Antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
-20 Celsius degree. Avoid repeated freeze/thaw cycles.
|Alternative antibody names|| |
Interstitial collagenase antibody, Fibroblast collagenase antibody, Matrix metalloproteinase-1 antibody, MMP-1 antibody
|Protein names|| |
Interstitial collagenase , Fibroblast collagenase , Matrix metalloproteinase-1 , MMP-1
|Protein function|| |
Cleaves collagens of types I, II, and III at one site in the helical domain. Also cleaves collagens of types VII and X. In case of HIV infection, interacts and cleaves the secreted viral Tat protein, leading to a decrease in neuronal Tat’s mediated neurotoxicity. / Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at 775-Gly-, -Ile-776 in the alpha-1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1′ is a hydrophobic residue. / Ca2+ / Zn2+ / Can be activated without removal of the activation peptide.
|Protein sequence and domain|| |
There are two distinct domains in this protein; the catalytic N-terminal, and the C-terminal which is involved in substrate specificity and in binding TIMP (tissue inhibitor of metalloproteinases). / The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme. / Belongs to the peptidase M10A family. / Contains 4 hemopexin repeats.
|Protein post-translational modifications|| |
Undergoes autolytic cleavage to two major forms (22 kDa and 27 kDa). A minor form (25 kDa) is the glycosylated form of the 22 kDa form. The 27 kDa form has no activity while the 22/25 kDa form can act as activator for collagenase. / Tyrosine phosphorylated in platelets by PKDCC/VLK.
|Protein cellular localization|| |
Secreted > extracellular space > extracellular matrix
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St John’s Laboratory Ltd.
|Product type|| |
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