Anti-Retinoblastoma / Rb, clone SPM353

1 mg/ml in 1X PBS, BSA free, sodium azide free. Recognizes a 105kDa phosphoprotein, identified as retinoblastoma (Rb) gene product. It shows no cross reaction with p107 or p130. It specifically stains the nuclei of BT-20 cells and primary human foreskin fibroblast (HFF) cells. It does not stain the Rb-negative BT549 cells. It reacts with the hyperphosphorylated as well as the un (under) phosphorylated form of the Rb protein. Retinoblastoma gene product plays a key role in cell cycle control. It has been identified as a tumor suppressor gene whose loss of its function leads to tumor development. It is widely expressed in a variety of human tissues including breast, esophageal, squamous cell and cervical carcinoma. Protein function: Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G0-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, KMT5B and KMT5C, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity. [The UniProt Consortium]