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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Phospho-RB1 Ser608 Antibody / RB1 Phospho Ser608 Polyclonal Antibody recognizes retinoblastoma protein phosphorylated at serine 608, a regulatory residue involved in controlling the growth-suppressive activity of RB1. Retinoblastoma protein is a nuclear tumor suppressor that coordinates cell cycle progression by regulating E2F transcription factors and their associated gene expression programs. Encoded by the RB1 gene, this protein contains a conserved pocket domain that mediates interactions with transcriptional regulators. Phosphorylation at specific residues changes these interactions and contributes to the transition between growth arrest and cellular proliferation.
Ser608 is located within a flexible loop associated with the RB1 pocket domain. Phosphorylation at this residue promotes an intramolecular interaction in which the phosphorylated loop associates with the pocket structure, altering the surface involved in E2F binding. Structural and biochemical studies have demonstrated that this mechanism contributes to reduced affinity for E2F transcription factors. Ser608 therefore represents a particularly informative phosphorylation site because its regulatory effects have been linked to a defined conformational change rather than simply serving as a general indicator of RB1 phosphorylation.
RB1 phosphorylation is coordinated by cyclin-dependent kinases responding to extracellular growth signals and intracellular cell cycle regulators. Cyclin D-associated CDK4/6 and cyclin E-associated CDK2 participate in modifying RB1 at multiple residues during cell cycle progression. These phosphorylation events are not necessarily functionally equivalent, and different combinations can influence distinct protein interactions. Phosphorylation at Ser608 contributes to this regulatory network by modifying the ability of RB1 to restrain E2F-dependent transcription. Consequently, analysis of this residue can provide information about a specific molecular mechanism involved in RB1 regulation.
Disruption of the RB1 pathway is common in cancer, occurring through RB1 gene alterations or changes in upstream regulators of cyclin-dependent kinase activity. Increased CDK signaling can modify RB1 phosphorylation patterns and contribute to inappropriate cell cycle entry. Conversely, inhibition of CDK4/6 can alter RB1 phosphorylation and help restore growth control in susceptible tumor cells. Distinguishing phosphorylation at Ser608 from total RB1 abundance is important because protein expression alone does not establish its functional regulatory state. This Phospho-RB1 Ser608 Antibody supports investigation of site-specific phosphorylation, RB1 conformational regulation, and the molecular mechanisms connecting kinase signaling with E2F-dependent cell cycle progression.
Explore our Retinoblastoma Antibody FCD-18, a rabbit monoclonal antibody targeting RB1, for an additional option with Western blot, immunohistochemistry, and immunofluorescence validation.
Titration of the Phospho-RB1 Ser608 Antibody / RB1 Phospho Ser608 Polyclonal Antibody may be required due to differences in protocols and secondary/substrate sensitivity.
This Phospho-RB1 Ser608 Antibody was produced from rabbits immunized with a KLH conjugated synthetic phosphopeptide corresponding to amino acid residues surrounding phosphorylated S608 of human Rb.
Aliquot the Phospho-RB1 Ser608 Antibody and store frozen at -20oC or colder. Avoid repeated freeze-thaw cycles.
Phospho-Rb Ser608 antibody, Phospho-Retinoblastoma Ser608 antibody, Phospho-pRb Ser608 antibody, Phosphorylated RB1 Ser608 antibody, Retinoblastoma Protein Phospho Ser608 antibody
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