|Calculated MW||H=63 KDa|
|Other Names||Matrix metalloproteinase-25, MMP-25, 3424-, Leukolysin, Membrane-type matrix metalloproteinase 6, MT-MMP 6, MTMMP6, Membrane-type-6 matrix metalloproteinase, MT6-MMP, MT6MMP, MMP25, MMP20, MMPL1, MT6MMP|
|Target/Specificity||This MMP25 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 470-499 amino acids from the C-terminal region of human MMP25.|
|Storage||Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||MMP25 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Synonyms||MMP20, MMPL1, MT6MMP|
|Function||May activate progelatinase A.|
|Cellular Location||Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix|
|Tissue Location||Expressed predominantly in leukocytes, lung and spleen. Expressed also in colon carcinoma, astrocytoma and glioblastomas|
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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MMP25 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. In addition, it is thought that this protein is activated intracellularly by furin-like enzymes. This protein activates MMP2 by cleavage. The gene has previously been referred to as MMP20 but has been renamed matrix metalloproteinase 25 (MMP25).
Matsuda, A., et al., J. Biol. Chem. 278(38):36350-36357 (2003).
Velasco, G., et al., Cancer Res. 60(4):877-882 (2000).
Nagase, H., et al., J. Biol. Chem. 274(31):21491-21494 (1999).
Pei, D., Cell Res. 9(4):291-303 (1999).
Kojima, S., et al., FEBS Lett. 480 (2-3), 142-146 (2000).