- CITATIONS: 2
|Application ||WB, IHC-P, FC, E|
|Other Accession||Q10739, Q9XT90, P53690, Q9GLE4, NP_004986|
|Predicted||Mouse, Rat, Pig, Bovine|
|Calculated MW||65894 Da|
|Antigen Region||145-174 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 rabbits immunized with a KLH conjugated synthetic peptide between 145-174 amino acids from the N-terminal region of human MMP14.|
|Format||Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.|
|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 (N-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|
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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. MMP14 seems to specifically activate progelatinase A, and may thus trigger invasion by tumor cells by activating progelatinase A on the tumor cell surface. Expression is significant in stromal cells of colon, breast, and head and neck.
Will, H., et al., Eur. J. Biochem. 231(3):602-608 (1995).
Takino, T., et al., Gene 155(2):293-298 (1995).
Okada, A., et al., Proc. Natl. Acad. Sci. U.S.A. 92(7):2730-2734 (1995).
Sato, H., et al., Nature 370(6484):61-65 (1994).
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