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Rb AntibodyRabbit Monoclonal
| Country | United States
Ordering Information
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| Catalog # | Size | Availability | Price | |
| AJ1682a | 100ul 400 ul | 2-3 days | $ 275.00 | DISCONTINED INQUIRE CLICK INQUIRE Add to cart |
- Specification
- Citiations : 0
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- Backgrounds
Rb Antibody - Product info | |
| Application | WB
|
| Primary Accession | P06400 |
| Reactivity | Human |
| Clone Names | EP44(2) |
| Calculated MW | 106159 Da |
| Gene ID 5925 | |
| Other Names RB1, Retinoblastoma-associated protein, pp110;p105-Rb | |
| Target/Specificity A synthetic peptide corresponding to residues in human Rb was used as an immunogen. | |
| Dilution WB~~1:1000~2000 | |
| 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. | |
Rb Antibody - Protein Information | |
| Name RB1 | |
| 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, SUV420H1 and SUV420H2, 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 | |
| Cellular Location Nucleus. | |
| Tissue Location Expressed in the retina. | |
Rb Antibody - Related products
AP3233a: Phospho-Rb-S249 Antibody
AP3235a: Phospho-RB-S608 Antibody
AP3236a: Phospho-RB-S612 Antibody
AP3237a: Phospho-Rb-S780 Antibody
AP3238a: Phospho-Rb-S788 Antibody
AP3239a: Phospho-RB-S795 Antibody
AP3241a: Phospho-Rb-S811 Antibody
AP8575b: RB1 Antibody (C-term)
BP3233a: Phospho-Rb-S249 Antibody Blocking Peptide
BP3235a: Phospho-RB-S608 Antibody Blocking Peptide
BP3236a: Phospho-RB-S612 Antibody Blocking Peptide
BP3237a: Phospho-Rb-S780 Antibody Blocking Peptide
BP3238a: Phospho-Rb-S788 Antibody Blocking Peptide
BP3239a: Phospho-RB-S795 Antibody Blocking Peptide
BP3241a: PhosphoRb-S811 Antibody Blocking Peptide
BP3244a: Phospho-Rb-T826 Antibody Blocking Peptide
BP6265e: RB1 Antibody (S608) Blocking Peptide
BP8575b: RB1 Antibody (C-term) Blocking Peptide
AJ1682b: Rb Antibody Phospho (pS780)
AJ1682c: Rb Antibody Phospho (pT356)
Rb Antibody - Application data
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A.Western blot analysis on (A) Jurkat and (B) K562 cell lysates using anti-Rb RabMAb (Cat. #AJ1682a).
Rb Antibody - Research Areas
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BACKGROUND
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).
REFERENCES
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.
