MMP25

GWB-93D062

Synthetic peptide corresponding to the hinge region of human matrix metalloproteinase-25.

The antibody specifically binds to MMP25 and does not cross react with the other MMP family members (MMP1 MMP2 MMP3 MMP9 etc. ).

Secreted

Affinity isolated antigen specific antibody is obtained from rabbit anti-MMP25 antiserum by immuno-specific purification which removes essentially all rabbit serum proteins including immunoglobulins which do not specifically bind to the peptide. Storage

WB: Use at an assay dependent dilution. A minimum working dilution of 1/1000 is recommended using a cell lysate an alkaline phosphatase conjugated secondary antibody and BCIP/NBT as the substrate. A starting dilution of 1/5000 of the antibody is recommended for chemiluminescent substrates. By blotting against the reduced protein the antibody identifies bands at 65 kDa as well as activation/breakdown products. Treatment of cells with concanavolin A or the phorbol ester TPA stimulates production of MMP25 in some cell types and the enzyme can be recovered in cell lysates.

Secreted Matrix Metalloproteinase 25 also known as membrane type matrix metalloproteinase 6 and leukolysin was initially cloned from human leukocytes and found to be specifically expressed by peripheral blood leukocytes. The expression of MMP25 (leukolysin) at the mRNA level appears to be localized to neutrophils. MMP25 was also found in lung spleen brain tumors and several tumor cell lines. Like the other membrane-type metalloproteinases MMP25 is associated with the cell membrane but is anchored to the cell surface via a GPI (glycosyl-phosphatidyl inositol) attachment rather than through a transmembrane domain. MMP25 is proteolytically active and truncated forms digest gelatin in zymograms. Like the other MT MMPs MMP25 has a furin cleavage site where prohormone convertases can activate the zymogen. MMP25 can be shed from the from the cell surface into the culture media under stimulatory conditions. MMP25 is expressed in brain tumors and may facilitate tumor progression through its ability to activate progelatinase A at the cell membrane in colon carcinomas or brain tumors. MMP25 may also play a role in the cellular migration and invasion of the extracellular matrix and basement membranes. The MMP25 gene maps to human chromosome 16p13. 3.

Cell membrane; Lipid-anchor GPI-anchor; Extracellular side. Secreted extracellular space extracellular matrix.

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 [view classification].