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TCEB1 Antibody (C-term)

Affinity Purified Rabbit Polyclonal Antibody (Pab)

     
  • 1 - TCEB1 Antibody (C-term) AP14814b
    All lanes : Anti-TCEB1 Antibody (C-term) at 1:1000 dilution Lane 1: Hela whole cell lysate Lane 2: PC-3 whole cell lysate Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L), Peroxidase conjugated at 1/10000 dilution. Predicted band size : 12 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
  • 14 - TCEB1 Antibody (C-term) AP14814b
    TCEB1 Antibody (C-term) (AP14814b)immunohistochemistry analysis in formalin fixed and paraffin embedded human prostate carcinoma followed by peroxidase conjugation of the secondary antibody and DAB staining.This data demonstrates the use of TCEB1 Antibody (C-term) for immunohistochemistry. Clinical relevance has not been evaluated.
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Product Information
Application
  • Applications Legend:
  • E=ELISA
  • WB=Western Blotting
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin)
  • IP=Immunoprecipitation
  • IF=Immunofluorescence
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • FC=Flow Cytometry
  • DB=Dot Blot
IHC-P, WB, E
Primary Accession Q15369
Other Accession P83941, P83940, Q2KII4, NP_005639.1
Reactivity Human
Predicted Bovine, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Isotype Rabbit IgG
Calculated MW 12473 Da
Antigen Region 69-98 aa
Additional Information
Gene ID 6921
Other Names Transcription elongation factor B polypeptide 1, Elongin 15 kDa subunit, Elongin-C, EloC, RNA polymerase II transcription factor SIII subunit C, SIII p15, TCEB1
Target/Specificity This TCEB1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 69-98 amino acids from the C-terminal region of human TCEB1.
Dilution IHC-P~~1:100~500
WB~~1:1000
E~~Use at an assay dependent concentration.
Format Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.
StorageMaintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles.
PrecautionsTCEB1 Antibody (C-term) is for research use only and not for use in diagnostic or therapeutic procedures.
Protein Information
Name ELOC (HGNC:11617)
Function SIII, also known as elongin, is a general transcription elongation factor that increases the RNA polymerase II transcription elongation past template-encoded arresting sites. Subunit A is transcriptionally active and its transcription activity is strongly enhanced by binding to the dimeric complex of the SIII regulatory subunits B and C (elongin BC complex) (PubMed:7821821). In embryonic stem cells, the elongin BC complex is recruited by EPOP to Polycomb group (PcG) target genes in order generate genomic region that display both active and repressive chromatin properties, an important feature of pluripotent stem cells (By similarity).
Cellular Location Nucleus.
Tissue Location Overexpressed in prostate cancer cell line PC-3 and breast cancer cell line SK-BR-3.
Research Areas

For Research Use Only. Not For Use In Diagnostic Procedures.

BACKGROUND

This gene encodes the protein elongin C, 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.

REFERENCES

Marcsisin, S.R., et al. J. Mol. Biol. 402(5):892-904(2010)
Rose, J.E., et al. Mol. Med. 16 (7-8), 247-253 (2010) :
Lievens, S., et al. J. Proteome Res. 8(2):877-886(2009)
Jalava, S.E., et al. Int. J. Cancer 124(1):95-102(2009)
Piessevaux, J., et al. J. Biol. Chem. 283(31):21334-21346(2008)

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