MMP17 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Primary Accession | Q9ULZ9 |
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Clone Names | 100427266 |
Gene ID | 4326 |
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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 | The synthetic peptide sequence used to generate the antibody AP13995b was selected from the C-term region of MMP17. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
Name | MMP17 |
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Synonyms | MT4MMP |
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. Cleaves pro-TNF-alpha at the '74-Ala-|-Gln-75' site. 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.
Background
Proteins of the matrix metalloproteinase (MMP) family areinvolved in the breakdown of extracellular matrix in normalphysiological processes, such as embryonic development,reproduction, and tissue remodeling, as well as in diseaseprocesses, such as arthritis and metastasis. Most MMP's aresecreted as inactive proproteins which are activated when cleavedby extracellular proteinases. The protein encoded by this gene isconsidered a member of the membrane-type MMP (MT-MMP) subfamily.However, this protein is unique among the MT-MMP's in that it is aGPI-anchored protein rather than a transmembrane protein. Theprotein activates MMP-2 by cleavage.
References
Romero, R., et al. Am. J. Obstet. Gynecol. 203 (4), 361 (2010) :Nalpas, B., et al. Gut 59(8):1120-1126(2010)Romero, R., et al. Am. J. Obstet. Gynecol. 202 (5), 431 (2010) :Huang, C.H., et al. Neoplasia 11(12):1371-1382(2009)Atkinson, S.J., et al. Biochem. J. 398(1):15-22(2006)
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