Reactive species
Human;Monkey
Antibody type
Polyclonal Antibody
Protein name
Matrix metalloproteinase-15
Immunogen
The antiserum was produced against synthesized peptide derived from human MMP15. AA range:113-162
Specificity
Cleaved-MMP-15 (Y132) Polyclonal Antibody detects endogenous levels of fragment of activated MMP-15 protein resulting from cleavage adjacent to Y132.
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: 1/10000. 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
MMP15; Matrix metalloproteinase-15; MMP-15; Membrane-type matrix metalloproteinase 2; MT-MMP 2; MTMMP2; Membrane-type-2 matrix metalloproteinase; MT2-MMP; MT2MMP; SMCP-2
Background
This gene encodes a member of the peptidase M10 family and membrane-type subfamily of matrix metalloproteinases (MMPs). Proteins in this 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. Members of this subfamily contain a transmembrane domain suggesting that these proteins are expressed at the cell surface rather than secreted. The encoded preproprotein is proteolytically processed to generate the mature protease. This protein may play a role in cancer progression. [provided by RefSeq, Jan 2016],
Function
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:Endopeptidase that degrades various components of the extracellular matrix. May activate progelatinase A.,PTM:The precursor is cleaved by a furin endopeptidase.,similarity:Belongs to the peptidase M10A family.,similarity:Contains 4 hemopexin-like domains.,tissue specificity:Appeared to be synthesized preferentially in liver, placenta, testis, colon and intestine. Substantial amounts are also detected in pancreas, kidney, lung, heart and skeletal muscle.,