R1660-23
Clone Type
PolyclonalHost
RabbitSource
HumanIsotype
IgGGrade
Affinity PurifiedApplications
WBCrossreactivity
HuShipping Temp
Blue IceStorage Temp
-20°CRabbit Anti-Retinoblastoma, phosphorylated (Thr356) (Rb)
Target Group: Rb is a tumor suppressor gene which functions as a negative regulator of the cell cycle by interacting with transcription factors including E2F-1, PU.1, ATF-2, UBF, Elf-1 and c-abl. This ability to alter transcription is regulated by phosphorylation catalyzed by the cyclin-dependent protein kinases (cdks). Rb contains at least 16 consensus sequences for cdk phosphorylation, but the significance of all of these sites is unclear. Phosphorylation of threonine 356 is catalyzed by the cdk4 complex Cyclin D-cdk4 and plays a role in mediating growth suppression activity of Rb.
Applications
Suitable for use in Western Blot. Other applications not tested.
Recommended Dilution
Western Blot: 0.25-0.75ug/ml Optimal dilutions to be determined by the researcher.
Positive Control
Jurkat cells in high growth phase.
Storage and Stability
May be stored at 4°C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20°C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
Immunogen
Synthetic phosphopeptide derived from a region of human Rb that contains threonine 356 (P06400). Species sequence homology: mouse (80%) rat (87%).
Form
Supplied as a liquid in PBS, pH 7.2, 1mg/ml BSA, 0.05% sodium azide.
Purity
Purified by immunoaffinity chromatography.
Specificity
Recognizes human Rb when phosphorylated at Thr356.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
References
1. Brantley, M.A., Jr. and J.W. Harbour (2001) The molecular biology of retinoblastoma. Ocul. Immunol. Inflamm. 9(1):1-8. 2. Tamrakar, S., et al. (2000) Role of pRB dephosphorylation in cell cycle regulation. Front. Biosci. 5:D121-D137. 3. Brown, V.D., et al. (1999) Cumulative effect of phosphorylation of pRB on regulation of E2F activity. Mol. Cell. Biol. 19:3246-3256. 4. Harbour, J.W., et al. (1999) Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. Cell 98:859-869. 5. Driscoll, B., et al. (1999) Discovery of a regulatory motif that controls the exposure of specific upstream cyclin-dependent kinase sites that determine both conformation and growth suppressing activity of pRb. J. Biol. Chem. 274(14):9463-9471. 6. Zarkowska, T. and S. Mittnacht (1997) Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases. J. Biol. Chem. 272:12738-12746. 7. Knudsen, E.S. and J.Y. Wang (1997) Dual mechanisms for the inhibition of E2F binding to RB by cyclin-dependent kinase-mediated RB phosphorylation. Mol. Cell. Biol. 17:5771-5783. 8. Knudsen, E.S. and J.Y. Wang (1996) Differential regulation of retinoblastoma protein function by specific cdk phosphorylation sites. J. Biol. Chem. 271:8313-8320.USBio References
No references available