Anti-MSH6 Antibody Picoband® Fluoro550 Conjugated

MSH6 or mutS homolog 6 is a gene that codes for DNA mismatch repair protein Msh6 in the budding yeast Saccharomyces cerevisiae. 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 biional 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.

A synthetic peptide corresponding to a sequence at the C-terminus of human MSH6, which shares 100% and 85.7% amino acid (aa) sequence identity with mouse and rat MSH6, respectively.

Colocalizes with SMARCA4/BRG1 in E-cadherin-negative cells from established lines, and stroma of normal colon as well as in de-differentiated epithelial cells at the invasion front of colorectal carcinomas (at protein level) . Expressed in heart and skeletal muscle, but not in liver, spleen, or pancreas.

Cancer, Cancer Metabolism, Carbohydrate Metabolism, Energy Metabolism, Energy Transfer Pathways, Metabolic Signaling Pathway, Metabolic Signaling Pathways, Metabolism, Metabolism Of Carbohydrates, Pathways and Processes, Signal Transduction

Catalyzes two distinct but analogous reactions: the reversible epimerization of UDP-glucose to UDP-galactose and the reversible epimerization of UDP-N-acetylglucosamine to UDP-N- acetylgalactosamine. The reaction with UDP-Gal plays a critical role in the Leloir pathway of galactose catabolism in which galactose is converted to the glycolytic intermediate glucose 6- phosphate. It contributes to the catabolism of dietary galactose and enables the endogenous biosynthesis of both UDP-Gal and UDP- GalNAc when exogenous sources are limited. Both UDP-sugar interconversions are important in the synthesis of glycoproteins and glycolipids.

1. Kariola, R., Raevaara, T. E., Lonnqvist, K. E., Nystrom-Lahti, M. Functional analysis of MSH6 mutations linked to kindreds with putative hereditary non-polyposis colorectal cancer syndrome. Hum. Molec. Genet. 11: 1303-1310, 2002. 2. Verma, L., Kane, M. F., Brassett, C., Schmeits, J., Evans, D. G. R., Kolodner, R. D., Maher, E. R. Mononucleotide microsatellite instability and germline MSH6 mutation analysis in early onset colorectal cancer. J. Med. Genet. 36: 678-682, 1999.