Anti-Phospho-Rb (Ser612) mAb (Monoclonal Antibody)
Monoclonal Antibody targeting pRB for ELISA, IP, WB.
| Target | pRB |
|---|---|
| Product Type | Antibody |
| Application | ELISA, IP, WB |
| Clonality | Monoclonal |
| Conjugate | Unlabeled |
| Isotype | IgG2a |
| Immunogen | a synthetic phosphopeptide corresponding to residues surrounding Ser612 of Human Rb (KLH-conjugated ) |
| Host Species | Mouse |
| Species Reactivity | Human |
| Formulation | Supplied in 20 mM phosphate buffer (pH 7.5), 300 mM NaCl, 50 % glycerol. |
| Research Area | Cell Biology |
| Description/Background | The retinoblastoma protein (Rb) is a nuclear phosphoprotein that regulates growth in the G1 phase of the cell cycle. Rb exerts its growth-inhibitory effects in part by binding to and inhibiting critical regulatory proteins, including members of the E2F family of transcription factors; E2F activation is necessary for the G1-S transition. E2F selectively associates with hypophosphorylated Rb, and phosphorylation of Rb appears to release E2F from an inhibitory complex, enabling it to promote the transcription necessary for progression<br /> into late G1 and S.</p> <p>Rb is phosphorylated on a still imprecisely defined number of threonine and serine residues during G1 (1, 2). A temporal sequence of modifications has been defined through use of both Rb variants in which certain of these residues have been replaced and monoclonal antibodies (MAbs) specific for certain phosphorylated domains of Rb. Both serine 608 (S608) and S780 have been identified as among the sites that are initially<br /> phosphorylated. These phosphorylations have distinct effects on the ability of Rb to interact with its various partner proteins. Thus, Rb phosphorylated on S780 appears to lose its ability to bind to E2F. Phosphorylation of S807 and/or S811 is required to abolish Rb binding to c-Abl, while modification of threonine 821 (T821) and/or T826 is required to abolish Rb binding to LXCXE-containing proteins such as simian virus 40 large T antigen. However, these four sites do not appear to be involved in regulating Rb binding to the E2F transcription factors.</p> <p>Phosphorylation of Rb also has effects on cell physiology, ostensibly by changing its association with these and other interacting partner proteins. For example, phosphorylation of S795 is required to inactivate Rb-imposed growth suppression in a microinjection assay. However, the relationship between growth inhibition and E2F binding is complex: phosphorylation of Rb in vitro by cyclin D-, cyclin E-, or cyclin A-associated kinase has been reported to release E2F, yet only action by cyclin D1–cyclin-dependent kinase 4 (cdk4) complexes, but not by cyclin E-cdk2 complexes, abrogates the growth-inhibitory property of Rb when microinjected into SaOS-2 cells. |
| Storage Temperature | -20°C |
| Protocols | ELISA, IP, WB |
| Clone Number | 3C11 |
| Concentration | 1.0 mg/mL |
| Regulatory Statement | For Research Use Only. Not for use in diagnostic procedures. |
