|Other Names||Matrix metalloproteinase-24, MMP-24, 3424-, Membrane-type matrix metalloproteinase 5, MT-MMP 5, MTMMP5, Membrane-type-5 matrix metalloproteinase, MT5-MMP, MT5MMP, Processed matrix metalloproteinase-24, MMP24, MT5MMP|
|Target/Specificity||The synthetic peptide sequence used to generate the antibody AP6205a was selected from the Center region of human MMP24 . A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay.|
|Format||The synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml deionized water for a final concentration of 1 mg/ml.|
|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.|
|Function||Metalloprotease that mediates cleavage of N-cadherin (CDH2) and acts as a regulator of neuro-immune interactions and neural stem cell quiescence. Involved in cell-cell interactions between nociceptive neurites and mast cells, possibly by mediating cleavage of CDH2, thereby acting as a mediator of peripheral thermal nociception and inflammatory hyperalgesia. Key regulator of neural stem cells quiescence by mediating cleavage of CDH2, affecting CDH2-mediated anchorage of neural stem cells to ependymocytes in the adult subependymal zone, leading to modulate their quiescence. May play a role in axonal growth. Able to activate progelatinase A. May also be a proteoglycanase involved in degradation of proteoglycans, such as dermatan sulfate and chondroitin sulfate proteoglycans. Cleaves partially fibronectin, but not collagen type I, nor laminin (By similarity).|
|Cellular Location||Matrix metalloproteinase-24: Cell membrane; Single-pass type I membrane protein Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. Note=Recycled back to the plasma membrane through the trans-Golgi network via interaction with APBA3.|
|Tissue Location||Predominantly expressed in brain, kidney, pancreas and lung. Overexpressed in a series of brain tumors, including astrocytomas and glioblastomas|
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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 MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. However, MMP24 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 by cleavage. The gene has previously been referred to as MMP25 but has been renamed matrix metalloproteinase 24 (MMP24).
Jung, M., et al., Prostate 55(2):89-98 (2003).Kajita, M., et al., FEBS Lett. 457(3):353-356 (1999).Llano, E., et al., Cancer Res. 59(11):2570-2576 (1999).Nagase, H., et al., J. Biol. Chem. 274(31):21491-21494 (1999).Kinoh, H., et al., Cytogenet. Cell Genet. 87 (1-2), 97-98 (1999).
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