Cell Signaling Technology

Product Pathways - Chromatin Regulation / Epigenetics

TH1L Antibody #3088

Applications Reactivity Sensitivity MW (kDa) Source
W IP H M R Mk (Hm) (C) (X) (B) (Dg) (Pg) (GP) (Hr) Endogenous 66 Rabbit

Applications Key:  W=Western Blotting  IP=Immunoprecipitation
Reactivity Key:  H=Human  M=Mouse  R=Rat  Hm=Hamster  Mk=Monkey  C=Chicken  X=Xenopus  B=Bovine  Dg=Dog  Pg=Pig  GP=Guinea Pig  Hr=Horse
Species cross-reactivity is determined by western blot. Species enclosed in parentheses are predicted to react based on 100% sequence homology.

Protocols

Specificity / Sensitivity

TH1L Antibody recognizes endogenous levels of total TH1L protein.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala132 of human TH1L protein. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using TH1L Antibody.

Background

Negative Elongation Factor (NELF) consists of four subunits: WHSC2 (NELF-A), COBRA-1 (NELF-B), TH1L (NELF-C/D), and NELF-E (1). NELF, together with DRB-sensitivity inducing factor (DSIF), inhibits RNA Polymerase II (RNAPII) elongation resulting in RNAPII promoter proximal pausing, where it awaits additional signaling to resume transcription (2,3). The release of RNAPII from promoter proximal pausing is a critical regulatory point during transcription and is signaled by positive transcription elongation factor (p-TEF-b) phosphorylation of both NELF and the C-terminal domain (CTD) within the largest subunit of RNAPII (4,5). WHSC2 is thought to connect the NELF complex to RNAPII machinery, while NELF-E contains an RNA binding motif that is necessary for NELF function (1,6,7). TH1L, together with COBRA-1, are integral subunits that bring WHSC2 and NELF-E together in the NELF complex (1).

In addition to its role in transcription regulation, TH1L is a negative regulator of MAPK signaling by inhibiting A-Raf and PAK1 kinase activities. Research studies have shown that TH1L expression is negatively correlated with breast cancer proliferation and migration (8-10).

  1. Narita, T. et al. (2003) Mol Cell Biol 23, 1863-73.
  2. Yamaguchi, Y. et al. (1999) Cell 97, 41-51.
  3. Nechaev, S. and Adelman, K. (2011) Biochim Biophys Acta 1809, 34-45.
  4. Buratowski, S. (2009) Mol Cell 36, 541-6.
  5. Yamaguchi, Y. et al. (1999) Cell 97, 41-51.
  6. Yamaguchi, Y. et al. (2001) Science 293, 124-7.
  7. Yamaguchi, Y. et al. (2002) Mol Cell Biol 22, 2918-27.
  8. Cheng, C. et al. (2009) J Biol Chem 284, 8786-96.
  9. Liu, W. et al. (2004) J Biol Chem 279, 10167-75.
  10. Zou, W. et al. (2010) Cancer Sci 101, 2156-62.

Application References

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Companion Products

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

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