Anti-MCM6 Antibody Picoband® Fluoro488 Conjugated

MCM6 (Minichromosome maintenance, s. pombe, homolog of, 6) is a protein that in humans is encoded by the MCM6 gene. MCM6 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The MCM genes were originally identified in yeast defective in minichromosome maintenance and have since been shown to play roles in the progression of the cell cycle; many are cell division control genes. The MCM6 gene is mapped on 2q21.3. Mcm 6 has recently been shown to interact strongly Cdt1 at defined residues, by mutating these target residues Wei et al. observed lack of Cdt1 recruitment of Mcm2-7 to the pre-RC. An approximately 200-kb region surrounding the C/T (-13910) polymorphism in MCM6 intron 13 functioned as an enhancer of the lactase gene promoter in intestinal cell culture.

A synthetic peptide corresponding to a sequence in the middle region of human MCM6, different from the related rat and mouse sequences by one amino acid.

In fluids, highest levels found in milk of lactating women followed by cerebrospinal fluid, nipple aspirate fluid and breast cyst fluid. Also found in serum, seminal plasma and some amniotic fluids and breast tumor cytosolic extracts. Not detected in urine. At the tissue level, highest concentrations found in glandular tissues such as salivary glands followed by lung, colon, fallopian tube, placenta, breast, pituitary and kidney. Not detected in skin, spleen, bone, thyroid, heart, ureter, liver, muscle, endometrium, testis, pancreas, seminal vesicle, ovary, adrenals and prostate. In brain, detected in gray matter neurons (at protein level) . Colocalizes with pathological inclusions such as Lewy bodies and glial cytoplasmic inclusions. Overexpressed in primary breast tumors but not expressed in metastatic tumors. .

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. .

1. Bersaglieri, T., Sabeti, P. C., Patterson, N., Vanderploeg, T., Schaffner, S. F., Drake, J. A., Rhodes, M., Reich, D. E., Hirschhorn, J. N. Genetic signatures of strong recent positive selection at the lactase gene. Am. J. Hum. Genet. 74: 1111-1120, 2004. 2. Coelho, M., Luiselli, D., Bertorelle, G., Lopes, A. I., Seixas, S., Destro-Bisol, G., Rocha, J. Microsatellite variation and evolution of human lactase persistence. Hum. Genet. 117: 329-339, 2005. 3. Enattah, N. S., Sahi, T., Savilahti, E., Terwilliger, J. D., Peltonen, L., Jarvela, I. Identification of a variant associated with adult-type hypolactasia. Nature Genet. 30: 233-237, 2002.