Product Pathways - Protein Translation
BRF1/2 Antibody #2119
|2119S||100 µl (10 western blots)||---||In Stock||---|
|2119||carrier free and custom formulation / quantity||email request|
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|W||1:1000||Human, Mouse, Rat, Monkey||Endogenous||40 to 50, 62||Rabbit|
Species cross-reactivity is determined by western blot.
Applications Key: W=Western Blotting, IF-IC=Immunofluorescence (Immunocytochemistry), F=Flow Cytometry
Species predicted to react based on 100% sequence homology: Chicken, Bovine.
Specificity / Sensitivity
This antibody detects endogenous levels of total BRF1 and BRF2 proteins.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human BRF1 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Western blot analysis of cell lysates from HT1080, HT1080 BRF1-/-, HCT15, C6, COS and NIH/3T3 cells, using BRF1/2 Antibody.
Flow cytometric analysis of A549 cells, using BRF1/2 Antibody (blue) compared to a nonspecific negative control antibody (red).
Butyrate response factor 1 (BRF1; also known as EGF response factor 1 [ERF1], TIS11B, ZFP36L1) and butyrate response factor 2 (BRF2; also known as EGF response factor 2 [ERF2], TIS11D, ZFP36L2) both belong to the TIS11 family of CCCH zinc-finger proteins (1). This family of proteins, which also includes tristetraprolin (TTP), bind to AU-rich elements (ARE) found in the 3'-untranslated regions of mRNAs and promote de-adenylation and rapid degradation by the exosome (2,3). These proteins play a critical role in cell growth control by regulating the mRNA turnover of multiple cytokines, growth factors and cell cycle regulators, including GM-CSF, TNFα, IL-2, IL-3 and IL-6 (4,5). Deregulated ARE-mRNA stability can contribute to both inflammation and oncogenic transformation (6-8). Insulin-induced stabilization of ARE-containing transcripts is mediated by Akt/PKB phosphorylation of BRF1 at Ser92, which results in binding by 14-3-3 protein and inactivation of BRF1 (9).
- Varnum, B.C. et al. (1991) Mol. Cell. Biol. 11, 1754-1758.
- Stoecklin, G. et al. (2002) EMBO J. 21, 4709-4718.
- Lykke-Andersen, J. and Wagner, E. (2005) Genes Dev. 19, 351-361.
- Stoecklin, G. et al. (2000) Mol. Cell. Biol. 20, 3753-3763.
- Stoecklin, G. et al. (2001) RNA 7, 1578-1588.
- Schuler, G.D. and Cole, M.D. (1988) Cell 55, 1115-1122.
- Nair, A.P. et al. (1994) Nature 369, 239-242.
- Carballo, E. et al. (1998) Science 281, 1001-1005.
- Schmidlin, M. et al. (2004) EMBO J. 23, 4760-4769.
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