Reactive species
Human;Mouse;Rat
Antibody type
Polyclonal Antibody
Protein name
Matrix metalloproteinase-14
Immunogen
The antiserum was produced against synthesized peptide derived from human MMP14. AA range:93-142
Specificity
Cleaved-MMP-14 (Y112) Polyclonal Antibody detects endogenous levels of fragment of activated MMP-14 protein resulting from cleavage adjacent to Y112.
Constitute
Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Source
Polyclonal, Rabbit,IgG
Dilution rate
Western Blot: 1/500 - 1/2000. ELISA: 1/20000. Not yet tested in other applications.
Purification process
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
Other name
MMP14; Matrix metalloproteinase-14; MMP-14; MMP-X1; Membrane-type matrix metalloproteinase 1; MT-MMP 1; MTMMP1; Membrane-type-1 matrix metalloproteinase; MT1-MMP; MT1MMP
Background
Proteins of the matrix metalloproteinase (MMP) family 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. However, the protein encoded by this gene is a member of the membrane-type MMP (MT-MMP) subfamily; each member of this subfamily contains a potential transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. This protein activates MMP2 protein, and this activity may be involved in tumor invasion. [provided by RefSeq, Jul 2008],
Function
catalytic activity:Endopeptidase activity. Activates progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38. Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and 354-Gln-|-Thr-355 in the aggrecan interglobular domain.,cofactor:Binds 1 zinc ion per subunit.,cofactor:Calcium.,domain: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.,function:Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,s
