Phospho-Rb (Ser807) Antibody #99274
- WB
Supporting Data
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 110 |
SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Phospho-Rb (Ser807) Antibody recognizes endogenous levels of Rb protein only when phosphorylated at Ser807.
Species Reactivity:
Human
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser807 of human Rb protein. Antibodies are purified by peptide affinity chromatography.
Background
The retinoblastoma tumor suppressor protein Rb regulates cell proliferation by controlling progression through the restriction point within the G1-phase of the cell cycle (1). Rb has three functionally distinct binding domains and interacts with critical regulatory proteins including the E2F family of transcription factors, c-Abl tyrosine kinase, and proteins with a conserved LXCXE motif (2-4). Cell cycle-dependent phosphorylation by a CDK inhibits Rb target binding and allows cell cycle progression (5). Rb inactivation and subsequent cell cycle progression likely requires an initial phosphorylation by cyclin D-CDK4/6 followed by cyclin E-CDK2 phosphorylation (6). Specificity of different CDK/cyclin complexes has been observed in vitro (6-8) and cyclin D1 is required for Ser780 phosphorylation in vivo (9).
- Sherr, C.J. (1996) Science 274, 1672-7.
- Nevins, J.R. (1992) Science 258, 424-9.
- Welch, P.J. and Wang, J.Y. (1993) Cell 75, 779-90.
- Hu, Q.J. et al. (1990) EMBO J 9, 1147-55.
- Knudsen, E.S. and Wang, J.Y. (1997) Mol Cell Biol 17, 5771-83.
- Lundberg, A.S. and Weinberg, R.A. (1998) Mol Cell Biol 18, 753-61.
- Connell-Crowley, L. et al. (1997) Mol Biol Cell 8, 287-301.
- Kitagawa, M. et al. (1996) EMBO J 15, 7060-9.
- Geng, Y. et al. (2001) Proc Natl Acad Sci USA 98, 194-9.
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