epitope mapping near the C-terminus of RINT-1 of human origin
recommended for detection of RINT-1 of human origin by WB, IF and ELISA; also reactive with additional species, including equine, canine, bovine, porcine and avian
RINT-1 Background Information Rad50, a structural maintenance of chromosomes (SMC) protein family member, participates in a variety of cellular processes, including DNA double-strand break repair, cell cycle checkpoint activation, telomere maintenance, and meiosis (1-5). In addition
to its ability to form a complex with the DNA double-strand
break repair proteins Mre11 and NBS1, Rad50 may interact with other cellular proteins to execute its full range of biological
activities (1,2). A novel protein named RINT-1 was identified using the C-terminal region of human Rad50 as the bait in a yeast two-hybrid screen (1). Human RINT-1 shares sequence homology with a novel protein identified in Drosophila melanogaster (1). The conserved central and C-terminal regions of RINT-1 are required for its interaction with Rad50 (1). While Rad50 and RINT-1 are both expressed throughout the cell cycle, RINT-1 specifically binds to Rad50 only during late S and G(2)/M phases, suggesting that RINT-1 may be involved in cell cycle regulation (1). RINT-1 may also play a role in the regulation of cell cycle control after DNA damage (1).
