Cell Signaling Technology

Product Pathways - Transcription Factors

TCF11/NRF1 (D5B10) Rabbit mAb #8052

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M Mk Endogenous 120-140 Rabbit IgG

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  Mk=Monkey
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

TCF11/NRF1 (D5B10) Rabbit mAb recognizes endogenous levels of total TCF11 protein.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Gly129 of human TCF11 protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from U-2 OS cells, untreated (-) or treated (+) with MG132 (10 µM, 8 hr), using TCF11/NRF1 (D5B10) Rabbit mAb and β-Actin (D6A8) Rabbit mAb #8457.

Background

Transcription factor 11 (TCF11) is a basic leucine zipper transcription factor. It is also referred to as Nuclear factor E2-related factor 1 (NRF1). TCF11 was initially reported to activate erythroid-specific, human globin gene expression (1). It plays an essential role during embryonic development (2). It also associates with other transcription factors, such as Jun proteins, to transcriptionally control antioxidant response element (ARE)-mediated expression in response to antioxidants and xenobiotics (3-5). TCF11 has been shown to regulate proteasomal degradation and mediate the proteasome recovery pathway after proteasome inhibition (6,7). TCF11 is ubiquitously expressed (8) and several isoforms have been reported. The 120 kDa form exists in the endoplasmic reticulum (ER) membrane under normal conditions. Upon proteasome inhibition, TCF11 translocates to the nucleus (9). The 65 kDa N-terminal-truncated form is constitutively localized to the nucleus (10,11). TCF11 protein levels are regulated by ubiquitination and proteasomal-mediated degradation (12); proteasome inhibitors stabilize TCF11.

  1. Caterina, J.J. et al. (1994) Nucleic Acids Res 22, 2383-91.
  2. Murphy, P. and Kolstø, A. (2000) Mech Dev 97, 141-8.
  3. Johnsen, O. et al. (1998) Nucleic Acids Res 26, 512-20.
  4. Venugopal, R. and Jaiswal, A.K. (1998) Oncogene 17, 3145-56.
  5. Kwong, M. et al. (1999) J Biol Chem 274, 37491-8.
  6. Radhakrishnan, S.K. et al. (2010) Mol Cell 38, 17-28.
  7. Steffen, J. et al. (2010) Mol Cell 40, 147-58.
  8. Chan, J.Y. et al. (1993) Proc Natl Acad Sci USA 90, 11371-5.
  9. Steffen, J. et al. (2010) Mol Cell 40, 147-58.
  10. Wang, W. and Chan, J.Y. (2006) J Biol Chem 281, 19676-87.
  11. Wang, W. et al. (2007) J Biol Chem 282, 24670-8.
  12. Chepelev, N.L. et al. (2011) PLoS One 6, e29167.

Application References

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

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