Cell Signaling Technology

Product Pathways - Nuclear Receptor Signaling

STF-1 Antibody #8795

Applications Reactivity Sensitivity MW (kDa) Source
W H M (Mk) (B) (Pg) (Hr) Endogenous 50 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  Mk=Monkey  B=Bovine  Pg=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

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

Source / Purification

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from NCI-H295R and MLTC-1 cells using STF-1 Antibody.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, either mock transfected (-), transfected with a DDK-tagged cDNA expression construct encoding full-length human STF-1 (hSTF-1, +), or transfected with a Myc/DDK-tagged cDNA expression construct encoding full-length human LRH-1, isoform 2 (hLRH-1, +), using STF-1 Antibody (upper) and DYKDDDDK Tag Antibody (Binds to same epitope as Sigma's Anti-FLAG® M2 Antibody) #2368 (lower).

Background

The orphan nuclear receptor, steroidogenic factor 1 (STF-1, also called Ad4BP), encoded by the NR5A1 gene, displays a high degree of homology to the Drosophila nuclear receptor fushi tarazu factor 1 and plays a fundamental role in the development and function of steroidogenic tissues. STF-1 is also similar in sequence to an orphan receptor cloned from mouse liver, designated LRH-1, and its human homolog, PHR-1. Although LRH-1 is derived from a separate gene and has a distinct expression profile, LRH-1 and STF-1 sequences are sufficiently similar to place them within the same subfamily of nuclear receptors, designated NR5A (1).Initially identified as a tissue-specific transcriptional regulator of cytochrome P450 steroid hydroxylases, studies of both global (2) and tissue-specific knockout mice (3-6) have demonstrated that STF-1 is required for the devlopment of adrenal glands, gonads, ventromedial hypothalamus, and for the proper functioning of pituitary gonadotropes. Indeed, humans with heterozygous 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 N-terminal zinc finger DNA-binding domain, a ligand-binding domain, a C-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 or A-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.

Application References

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

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