STF-1 (D1Z2A) XP® Rabbit mAb #12800
- WB
- IP
- IF
- ChIP
Supporting Data
| REACTIVITY | H M |
| SENSITIVITY | Endogenous |
| MW (kDa) | 50 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
- ChIP-Chromatin Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
Product Information
Product Usage Information
For optimal ChIP and ChIP-seq results, use 10 μl of antibody and 10 μg of chromatin (approximately 4 x 106 cells) per IP. This antibody has been validated using SimpleChIP® Enzymatic Chromatin IP Kits.
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:100 |
| Immunofluorescence (Immunocytochemistry) | 1:100 |
| Chromatin IP | 1:50 |
| Chromatin IP-seq | 1:50 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Source / Purification
Background
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).
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- Jeyasuria, P. et al. (2004) Mol Endocrinol 18, 1610-9.
- Pelusi, C. et al. (2008) Biol Reprod 79, 1074-83.
- Zhao, L. et al. (2008) Mol Endocrinol 22, 1403-15.
- Achermann, J.C. et al. (1999) Nat Genet 22, 125-6.
- Lourenço, D. et al. (2009) N Engl J Med 360, 1200-10.
- Bulun, S.E. et al. (2009) Mol Cell Endocrinol 300, 104-8.
- Figueiredo, B.C. et al. (2005) J Clin Endocrinol Metab 90, 615-9.
- Little, T.H. et al. (2006) Mol Endocrinol 20, 831-43.
- Hammer, G.D. et al. (1999) Mol Cell 3, 521-6.
- Chen, W.Y. et al. (2004) J Biol Chem 279, 38730-5.
- Lee, F.Y. et al. (2011) Dev Cell 21, 315-27.
- Chen, W.Y. et al. (2005) Mol Cell Biol 25, 10442-53.
Limited Uses
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