|Other Names||DNA mismatch repair protein Msh2, hMSH2, MutS protein homolog 2, MSH2|
|Format||Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI 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||Component of the post-replicative DNA mismatch repair system (MMR). Forms two different heterodimers: MutS alpha (MSH2- MSH6 heterodimer) and MutS beta (MSH2-MSH3 heterodimer) which binds to DNA mismatches thereby initiating DNA repair. When bound, heterodimers bend the DNA helix and shields approximately 20 base pairs. MutS alpha recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. MutS beta recognizes larger insertion-deletion loops up to 13 nucleotides long. After mismatch binding, MutS alpha or beta forms a ternary complex with the MutL alpha heterodimer, which is thought to be responsible for directing the downstream MMR events, including strand discrimination, excision, and resynthesis. ATP binding and hydrolysis play a pivotal role in mismatch repair functions. The ATPase activity associated with MutS alpha regulates binding similar to a molecular switch: mismatched DNA provokes ADP-->ATP exchange, resulting in a discernible conformational transition that converts MutS alpha into a sliding clamp capable of hydrolysis-independent diffusion along the DNA backbone. This transition is crucial for mismatch repair. MutS alpha may also play a role in DNA homologous recombination repair. In melanocytes may modulate both UV-B-induced cell cycle regulation and apoptosis.|
|Tissue Location||Ubiquitously expressed.|
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MSH2 was identified as a locus frequently mutated inhereditary nonpolyposis colon cancer (HNPCC). When cloned, it wasdiscovered to be a human homolog of the E. coli mismatch repairgene mutS, consistent with the characteristic alterations inmicrosatellite sequences (RER+ phenotype) found in HNPCC. [providedby RefSeq].
Kim, M., et al. Cancer Sci. 101(11):2436-2442(2010)Mangoni, M., et al. Int. J. Radiat. Oncol. Biol. Phys. (2010) In press :Srivastava, K., et al. Cancer 116(13):3160-3169(2010)van der Post, R.S., et al. J. Med. Genet. 47(7):464-470(2010)Langner, E., et al. J. Genet. 89(1):101-104(2010)
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