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STF-1 Antibody

STF-1 Antibody #8795

This product is discontinued

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# Product Name Application Reactivity
  • WB
  • IP
  • IF
  • ChIP

Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

STF-1 Antibody recognizes endogenous levels of total STF-1 protein. This antibody does not cross-react with LRH-1/NR5A2.

Species predicted to react based on 100% sequence homology:

Monkey, Bovine, Pig, Horse

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Leu184 of human STF-1 protein. Antibodies are purified by protein A and peptide affinity chromatography.

The orphan nuclear receptor, steroidogenic factor 1 (STF-1, also called Ad4BP), is encoded by the NR5A1 gene and plays an instrumental role in directing the transcriptional control of steroidogenesis (1). Initially identified as a tissue-specific transcriptional regulator of cytochrome P450 steroid hydroxylases, research studies of both global (2) and tissue-specific knockout mice (3-6) have demonstrated that STF-1 is required for the development of adrenal glands, gonads, ventromedial hypothalamus, and for the proper functioning of pituitary gonadotropes. Indeed, humans with mutations that render STF-1 transcriptionally inactive can present with testicular failure, ovarian failure, and adrenal insufficiency (7,8). Furthermore, dysregulation of STF-1 has been linked to diseases such as endometriosis (9) and adrenocortical carcinoma (10).

Like other nuclear hormone receptors, STF-1 has a modular domain structure composed of an amino-terminal zinc finger DNA-binding domain, a ligand-binding domain, a carboxy-terminal AF-2 activation domain, and a hinge region with AF-1-like activation activity. STF-1 also contains a fushi tarazu factor 1 box, which functions as an accessory DNA binding domain (11). STF-1 is primarily phosphorylated at Ser203, which is thought to enhance its transcriptional activity by promoting complex formation with transcriptional cofactors (12). In addition to phosphorylation at Ser203, STF-1 is subject to SUMO conjugation and acetylation at ε-amino groups of target lysine residues. Whereas SUMOylation represses STF-1 function (13,14), acetylation enhances its transcriptional activity (15).

  1. Parker, K.L. and Schimmer, B.P. (1997) Endocr Rev 18, 361-77.
  2. Luo, X. et al. (1994) Cell 77, 481-90.
  3. Zhao, L. et al. (2001) Development 128, 147-54.
  4. Jeyasuria, P. et al. (2004) Mol Endocrinol 18, 1610-9.
  5. Pelusi, C. et al. (2008) Biol Reprod 79, 1074-83.
  6. Zhao, L. et al. (2008) Mol Endocrinol 22, 1403-15.
  7. Achermann, J.C. et al. (1999) Nat Genet 22, 125-6.
  8. Lourenço, D. et al. (2009) N Engl J Med 360, 1200-10.
  9. Bulun, S.E. et al. (2009) Mol Cell Endocrinol 300, 104-8.
  10. Figueiredo, B.C. et al. (2005) J Clin Endocrinol Metab 90, 615-9.
  11. Little, T.H. et al. (2006) Mol Endocrinol 20, 831-43.
  12. Hammer, G.D. et al. (1999) Mol Cell 3, 521-6.
  13. Chen, W.Y. et al. (2004) J Biol Chem 279, 38730-5.
  14. Lee, F.Y. et al. (2011) Dev Cell 21, 315-27.
  15. Chen, W.Y. et al. (2005) Mol Cell Biol 25, 10442-53.
Entrez-Gene Id
Swiss-Prot Acc.
For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
Anti-FLAG is a registered trademark of Sigma-Aldrich Biotechnology.

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