ELL Antibody

This antibody is also available with the following conjugates:
AF350, AF405L, AF405M, AF405S, AF488, AF514, AF532, AF546, AF555, AF568, AF594, AF610, AF635, AF647, AF680, AF700, AF750, AF790, APC, AP, Biotin, Cy3, Cy5.5, Cy5, Cy7, FITC, HRP, PE, Magnetic beads (1 um, 2.8 um, 3 um, 4.5 um, 5 um, 10 um, 15 um, 20 um, 30 um, or different size option)
Please contact sales@hoelzel.de for pricing and availability.

68kDa

Affinity purification

Actin is a key regulator of RNA polymerase (Pol) II-dependent transcription. Positive transcription elongation factor b (P-TEFb), a Cdk9/cyclin T1 heterodimer, has been reported to play a critical role in transcription elongation. However, the relationship between actin and P-TEFb is still not clear. In this study, actin was found to interact with Cdk9, a catalytic subunit of P-TEFb, in elongation complexes. Using immunofluorescence and immunoprecipitation assays, Cdk9 was found to bind to G-actin through the conserved Thr-186 in the T-loop. Overexpression and in vitro kinase assays showed that G-actin promotes P-TEFb-dependent phosphorylation of the Pol II C-terminal domain. An in vitro transcription experiment revealed that the interaction between G-actin and Cdk9 stimulated Pol II transcription elongation. ChIP and immobilized template assays indicated that actin recruited Cdk9 to a transcriptional template in vivo and in vitro. Using cytokine IL-6-inducible p21 gene expression system, we revealed that actin recruited Cdk9 to endogenous gene. Moreover, overexpression of actin and Cdk9 increased histone H3 acetylation and acetylized histone H3 binding to a transcriptional template through the interaction with histone acetyltransferase, p300. Taken together, our results suggested that actin participates in transcription elongation by recruiting Cdk9 for phosphorylation of the Pol II C-terminal domain, and the actin-Cdk9 interaction promotes chromatin remodeling.