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TCEB2 encodes the protein elongin B, which is a subunit of the transcription factor B (SIII) complex.
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EPOP (E130012A19Rik) functionally links elongin B, elongin C, and polycomb in pluripotent stem cells.
EPOP (E130012A19Rik) interacts with elongin B, elongin C, and USP7 to modulate the chromatin landscape.
Crystal structure shows interaction between SOCS2 (zeige SOCS2 ELISA Kits)-elongin BC and Cullin-5 (zeige CUL5 ELISA Kits).
both P-TEFb (zeige CCNT1 ELISA Kits) activity and H1 phosphorylation are necessary for the full differentiation of C2C12 myoblasts into myotubes.
Elongin B/C recruitment regulates substrate binding by CIS
SOCS box acts as an independent binding domain capable of recruiting elonginBC and cullin5 to promote E3 ligase formation.
Study shows that TCEB2 is involved in the development of acquired resistance to bevacizumab in ovarian cancer cells via the mechanisms of suppression of VEGF-A (zeige VEGFA ELISA Kits) expression by promoting HIF-1alpha (zeige HIF1A ELISA Kits) degradation and induction of interleukin-8 (IL-8 (zeige IL8 ELISA Kits)) expression.
crystals of SOCS2 (zeige SOCS2 ELISA Kits) in complex with its adaptor proteins, Elongin C and Elongin B, underwent a change in crystallographic parameters when treated with dimethyl sulfoxide during soaking experiments.
The crystal structure of VHL bound to a Cul2 N-terminal domain, Elongin B, and Elongin C.
Vif interaction with EloB-EloC may contribute to recruitment of CBF-beta to Vif, demonstrating that the EloB C-teminus may play a role in improving Vif function and that the over-expression of EloB results in Vif stabilization.
ASB9 (zeige ASB9 ELISA Kits) is unstable alone but forms a stable ternary complex with EloBC that binds with high affinity to the Cullin 5 (zeige CUL5 ELISA Kits) N-terminal domain.
Elongin B also enhances gene expression from the double-stranded DNA genome of human cytomegalovirus.
Recombinant full-length Vif interacted with the Elongin BC complex in vitro with a K(d) of 1.9 muM and resulted in observable changes in deuterium uptake in both Elongin C and B.
findings report that HIV-1 Vif interacts with cellular proteins Cul5 (zeige CUL5 ELISA Kits), elongins B and C, and Rbx1 to form an Skp1 (zeige SKP1 ELISA Kits)-cullin-F-box (SCF (zeige KITLG ELISA Kits))-like complex
show that ASB2, by interacting with the Elongin BC complex, can assemble with Cullin5.Rbx1 to form an E3 ubiquitin ligase complex that stimulates polyubiquitination by the E2 ubiquitin-conjugating enzyme Ubc5
the E3 ubiquitin ligase activity of the Vif-BC-Cul5 (zeige CUL5 ELISA Kits) complex is essential for Vif function against APOBEC3G (zeige APOBEC3G ELISA Kits)
This gene encodes the protein elongin B, which is a subunit of the transcription factor B (SIII) complex. The SIII complex is composed of elongins A/A2, B and C. It activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin A functions as the transcriptionally active component of the SIII complex, whereas elongins B and C are regulatory subunits. Elongin A2 is specifically expressed in the testis, and capable of forming a stable complex with elongins B and C. The von Hippel-Lindau tumor suppressor protein binds to elongins B and C, and thereby inhibits transcription elongation. Two alternatively spliced transcript variants encoding different isoforms have been described for this gene. Pseudogenes have been identified on chromosomes 11 and 13.
18 kDa, elongin B
, RNA polymerase II transcription factor SIII subunit B
, SIII p18
, elongin 18 kDa subunit
, elongin B
, transcription elongation factor B (SIII), polypeptide 2 (18 kDa, elongin B)
, transcription elongation factor B polypeptide 2
, transcription elongation factor B (SIII) polypeptide 2 (18kD, elongin B)
, transcription elongation factor B, polypeptide 2
, RNA polymerase II transcription factor SIII p18 subunit
, elongin, 18-kD subunit