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YY1 Antibody

Background: The multi-functional transcription factor and nuclear matrix protein YY1 (Ying Yang 1) was first discovered in 1991 for its ability to dually trans-activate or trans-repress gene promoters. YY1 has been studied extensively across multiple disciplines. At least 30 cellular or viral protein factors have been found to physically interact with YY1 protein, and over 70 gene promoters have been found to be regulated by YY1. cDNAs encoding YY1 or YY1 homologs have been cloned from humans, rodents, zebrafish, frogs, fruitfly, and maize. Human and mouse YY1 protein sequences are highly homologous; regions of near 100% sequence homology include the acidic domain, glycine-rich domain, histidine-rich domain, and the zinc finger domain. YY1 is usually expressed at higher levels in proliferating cells. Expression of YY1 is typically low in post-mitotic tissues, and can be down-regulated during cell differentiation. Although the protein has a calculated molecular weight of ~45 kDa, it exhibits a prominently retarded gel mobility corresponding to ~70 kDa in SDS-PAGE.

Antibody Description: Polyclonal antibodies were produced by immunizing rabbits with bacterially expressed full-length human YY1 protein (414 amino acids; 411 amino acids for mouse YY1). The product is for research use only.