|Calculated MW||106159 Da|
|Other Names||Retinoblastoma-associated protein, p105-Rb, pRb, Rb, pp110, RB1|
|Target/Specificity||A synthetic peptide corresponding to residues in human Rb was used as an immunogen.|
|Format||50 mM Tris-Glycine (pH 7.4), 0.15 M NaCl, 40% Glycerol, 0.01% sodium azide and 0.05% BSA.|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.|
|Precautions||Rb Antibody is for research use only and not for use in diagnostic or therapeutic procedures.|
|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 (By similarity). 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.|
|Tissue Location||Expressed in the retina.|
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Provided below are standard protocols that you may find useful for product applications.
Retinoblastoma tumor suppressor protein (Rb) is associated with DNA binding activity and is thought to play a significant role in controlling cell cycle progression during tumor growth (1, 2). Cell cycle-dependent phosphorylation by cdk's inhibits Rb binding, thus allowing cell cycle progression (3). Rb inactivation and cell cycle progression likely requires first phosphorylation by cyclin D-cdk4/6 followed by cyclin E-cdk2 phosphorylation (4).
1. Lee, W.H., et al. Nature 329: 642-5, 1987. 2. Sherr, C.J., et al. Science 274: 1672-1677, 1996. 3. Knudsen, E.S. et al. Mol. Cell. Biol. 17: 5771-5783, 1997. 4. Lundberg, A.S. et al. Mol. Cell. Biol. 18, 753-761, 1998.
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