|Application ||WB, IHC, IF|
|Reactivity||Human, Mouse, Rat|
|Calculated MW||66653 Da|
|Other Names||Matrix metalloproteinase-17, MMP-17, 3424-, Membrane-type matrix metalloproteinase 4, MT-MMP 4, MTMMP4, Membrane-type-4 matrix metalloproteinase, MT4-MMP, MT4MMP, MMP17, MT4MMP|
|Target/Specificity||A synthetic peptide corresponding to residues on human MMP-17 was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Precautions||MMP-17 Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|Function||Endopeptidase that degrades various components of the extracellular matrix, such as fibrin. May be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators, such as tumor necrosis factor-alpha. May also be involved in tumoral process. Not obvious if able to proteolytically activate progelatinase A. Does not hydrolyze collagen types I, II, III, IV and V, gelatin, fibronectin, laminin, decorin nor alpha1-antitrypsin.|
|Cellular Location||Isoform Long: Cell membrane; Lipid-anchor, GPI-anchor; Extracellular side. Secreted, extracellular space, extracellular matrix|
|Tissue Location||Expressed in brain, leukocytes, colon, ovary testis and breast cancer. Expressed also in many transformed and non-transformed cell types|
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Provided below are standard protocols that you may find useful for product applications.
Membrane type (MT) matrix metalloproteinases (MMPs) are recently recognized members of the family of Zn(2+)- and Ca(2+)-dependent MMPs. MMP-17 is, therefore, a competent Zn(2+)-dependent MMP with unique specificity among synthetic substrates and the capability to both degrade gelatin and activate progelatinase A (1). (MMP-17) is expressed mainly in the brain, leukocytes, the colon, the ovary, and the testis. The expression of MMP-17 in leukocytes together with its putative membrane localization suggest that this enzyme could be involved in the activation of membrane-bound precursors of growth factors or inflammatory mediators such as tumor necrosis factor-alpha (2). glycosylphospha-tidylinositol (GPI) anchoring of MT4-MMP on the cell surface indicates a unique biological function and character for this proteinase (3).
1. Puente XS, et al. Cancer Res. 56(5):944-9, 1996.
2. Wang Y, et al. J Biol Chem. 274(46):33043-9, 1999.
3. Itoh Y, et al. J Biol Chem 274(48):34260-6, 1999.
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