|Calculated MW||H=66 KDa|
|Antigen Region||485-519 aa|
|Other Names||Matrix metalloproteinase-14, MMP-14, MMP-X1, Membrane-type matrix metalloproteinase 1, MT-MMP 1, MTMMP1, Membrane-type-1 matrix metalloproteinase, MT1-MMP, MT1MMP, MMP14|
|Target/Specificity||This MMP14 antibody is generated from mice immunized with a KLH conjugated synthetic peptide between 470-519 amino acids from the C-terminal region of human MMP14.|
|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||MMP14 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Seems to specifically activate progelatinase A. May thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. May be involved in actin cytoskeleton reorganization by cleaving PTK7. Acts as a positive regulator of cell growth and migration via activation of MMP15. Involved in the formation of the fibrovascular tissues in association with pro- MMP2.|
|Cellular Location||Membrane; Single-pass type I membrane protein. Melanosome. Cytoplasm Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Forms a complex with BST2 and localizes to the cytoplasm|
|Tissue Location||Expressed in stromal cells of colon, breast, and head and neck. Expressed in lung tumors|
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Provided below are standard protocols that you may find useful for product applications.
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.
Onimaru, M., et al. Arterioscler. Thromb. Vasc. Biol. 30(4):818-826(2010)
Wipff, J., et al. J. Rheumatol. 37(3):599-602(2010)
Liao, M.C., et al. Biochemistry 49(6):1127-1136(2010)
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