G/T mismatch-binding protein; GTBP; GTMBP; MutS-alpha 160 kDa subunit; p160

For Research Use Only. Not for use in diagnostic procedures.

E Coli or Yeast or Baculovirus or Mammalian Cell

Greater than 90% as determined by SDS-PAGE. (lot specific)

Liquid containing glycerol

This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.

Sterile filter available upon request.

Low endotoxin available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Manufactured in an ISO 13485:2003 and EN ISO 13485:2012 Certified Laboratory.

Small volumes of MSH6 recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, 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. Recruited on chromatin in G1 and early S phase via its PWWP domain that specifically binds trimethylated 'Lys-36' of histone H3 (H3K36me3): early recruitment to chromatin to be replicated allowing a quick identification of mismatch repair to initiate the DNA mismatch repair reaction

Epigenetics and Nuclear Signaling

(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)

60.03kD

mutS homolog 6

DNA mismatch repair protein Msh6

DNA mismatch repair protein Msh6

GTBP; hMSH6; GTBP; GTMBP; p160??[Similar Products]

MSH6_HUMAN

This gene encodes a member of the DNA mismatch repair MutS family. In E. coli, the MutS protein helps in the recognition of mismatched nucleotides prior to their repair. A highly conserved region of approximately 150 aa, called the Walker-A adenine nucleotide binding motif, exists in MutS homologs. The encoded protein heterodimerizes with MSH2 to form a mismatch recognition complex that functions as a bidirectional molecular switch that exchanges ADP and ATP as DNA mismatches are bound and dissociated. Mutations in this gene may be associated with hereditary nonpolyposis colon cancer, colorectal cancer, and endometrial cancer. Transcripts variants encoding different isoforms have been described. [provided by RefSeq, Jul 2013]

MSH6: Component of the post-replicative DNA mismatch repair system (MMR). Heterodimerizes with MSH2 to form MutS alpha, which binds to DNA mismatches thereby initiating DNA repair. When bound, MutS alpha bends the DNA helix and shields approximately 20 base pairs, and recognizes single base mismatches and dinucleotide insertion-deletion loops (IDL) in the DNA. After mismatch binding, 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. Heterodimer consisting of MSH2-MSH6 (MutS alpha). Forms a ternary complex with MutL alpha (MLH1-PMS1). Interacts with EXO1. Part of the BRCA1-associated genome surveillance complex (BASC), which contains BRCA1, MSH2, MSH6, MLH1, ATM, BLM, PMS2 and the RAD50-MRE11-NBS1 protein complex. This association could be a dynamic process changing throughout the cell cycle and within subnuclear domains. Interacts with ATR. Belongs to the DNA mismatch repair MutS family. 2 isoforms of the human protein are produced by alternative splicing.

Protein type: DNA-binding

Chromosomal Location of Human Ortholog: 2p16

Cellular Component: cytoplasm; Golgi apparatus; intracellular membrane-bound organelle; MutSalpha complex; nuclear chromatin; nucleoplasm; plasma membrane

Molecular Function: ADP binding; ATP binding; ATPase activity; chromatin binding; double-stranded DNA binding; four-way junction DNA binding; guanine/thymine mispair binding; magnesium ion binding; methylated histone residue binding; mismatched DNA binding; MutLalpha complex binding; oxidized purine DNA binding; protein binding; protein homodimerization activity; single guanine insertion binding; single thymine insertion binding

Biological Process: determination of ***** life span; DNA damage response, signal transduction resulting in induction of apoptosis; DNA repair; isotype switching; maintenance of DNA repeat elements; meiotic mismatch repair; mismatch repair; negative regulation of DNA recombination; positive regulation of helicase activity; positive regulation of isotype switching; response to UV; somatic hypermutation of immunoglobulin genes; somatic recombination of immunoglobulin gene segments; viral reproduction

Disease: Colorectal Cancer, Hereditary Nonpolyposis, Type 5; Endometrial Cancer; Mismatch Repair Cancer Syndrome

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Biol. Chem. 273:32055-32062(1998) DNA-dependent activation of the hMutSalpha ATPase.Blackwell L.J., Bjornson K.P., Modrich P.J. Biol. Chem. 273:32049-32054(1998) hMSH2 and hMSH6 play distinct roles in mismatch binding and contribute differently to the ATPase activity of hMutSalpha.Iaccarino I., Marra G., Palombo F., Jiricny J.EMBO J. 17:2677-2686(1998) Functional analysis of human MutSalpha and MutSbeta complexes in yeast.Clark A.B., Cook M.E., Tran H.T., Gordenin D.A., Resnick M.A., Kunkel T.A.Nucleic Acids Res. 27:736-742(1999) hMSH2-hMSH6 forms a hydrolysis-independent sliding clamp on mismatched DNA.Gradia S., Subramanian D., Wilson T., Acharya S., Makhov A., Griffith J., Fishel R.Mol. Cell 3:255-261(1999) The role of mismatched nucleotides in activating the hMSH2-hMSH6 molecular switch.Gradia S., Acharya S., Fishel R.J. Biol. 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U.S.A. 105:10762-10767(2008) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) DNA mismatch repair proteins are required for efficient herpes simplex virus 1 replication.Mohni K.N., Mastrocola A.S., Bai P., Weller S.K., Heinen C.D.J. Virol. 85:12241-12253(2011) System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.Sci. Signal. 4:RS3-RS3(2011) The histone mark H3K36me3 regulates human DNA mismatch repair through its interaction with MutSalpha.Li F., Mao G., Tong D., Huang J., Gu L., Yang W., Li G.M.Cell 153:590-600(2013) Structure of the human MutSalpha DNA lesion recognition complex.Warren J.J., Pohlhaus T.J., Changela A., Iyer R.R., Modrich P.L., Beese L.S.Mol. 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Mutat. 29:367-374(2008) A rapid and cell-free assay to test the activity of lynch syndrome-associated MSH2 and MSH6 missense variants.Drost M., Zonneveld J.B., van Hees S., Rasmussen L.J., Hofstra R.M., de Wind N.Hum. Mutat. 33:488-494(2012) Mismatch repair analysis of inherited MSH2 and/or MSH6 variation pairs found in cancer patients.Kantelinen J., Kansikas M., Candelin S., Hampel H., Smith B., Holm L., Kariola R., Nystrom M.Hum. Mutat. 33:1294-1301(2012) +Additional computationally mapped references.

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