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Render Timestamp: 2024-11-01T10:05:12.499Z
Commit: 23cb9f61fe67e1e9093fd644a533c4ff516a6463
XML generation date: 2024-09-30 01:55:40.159
Product last modified at: 2024-10-04T19:15:07.885Z
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PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Phospho-Nur77 (Ser351) (D22G5) Rabbit mAb #5095

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 70-80
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Phospho-Nur77 (Ser351) (D22G5) Rabbit mAb detects endogenous levels of Nur77 protein only when phosphorylated at Ser351.

    Species Reactivity:

    Human

    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:

    Mouse, Rat

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser351 of human Nur77 protein.

    Background

    Nur77, also known as TR3 and NGFI-B, is an immediate-early response gene and an orphan member of the steroid/thyroid/retinoid receptor superfamily (1-3). Nur77 is composed of an amino-terminal transactivation domain, a central DNA-binding domain and a carboxy-terminal ligand-binding domain. Expression of Nur77 is rapidly induced by a variety of stimuli, including apoptotic, mitogenic and stress signals (1-6). It has been proposed to have many functions related to cell proliferation, differentiation and apoptosis. Nur77 has been extensively studied in T cells where it has been implicated in the process of negative selection and TCR-mediated apoptosis (5,6). Nur77 binds to specific DNA elements leading to the regulation of target genes (7). As a possible mechanism for regulating apoptosis, Nur77 can induce the expression of apoptotic genes such as FasL and TRAIL (8,9). Nur77 is heavily phosphorylated by multiple kinases, which may affect its transactivation activity as well as its subcellular localization (4,10,11). Translocation of Nur77 from the nucleus to the mitochondria can regulate its association with Bcl-2 and control the release of cytochrome c, thereby triggering apoptosis (12,13).
    Phosphorylation of Nur77 by Akt or RSK occurs at Ser351 (corresponding to rat Nur77 Ser350 and Ser354 of mouse Nur77), a site within the Nur77 DNA binding domain (14-16). Serine phosphorylation at this site can down regulate transcriptional activity of Nur77 (10,17).
    1. Hazel, T.G. et al. (1988) Proc. Natl. Acad. Sci. USA 85, 8444-8448.
    2. Chang, C. and Kokontis, J. (1988) Biochem. Biophys. Res. Commun. 155, 971-977.
    3. Milbrandt, J. (1988) Neuron 1, 183-188.
    4. Fahrner, T.J. et al. (1990) Mol. Cell. Biol. 10, 6454-6459.
    5. Liu, Z.G. et al. (1994) Nature 367, 281-284.
    6. Woronicz, J.D. et al. (1994) Nature 367, 277-281.
    7. Wilson, T.E. et al. (1991) Science 252, 1296-1300.
    8. Weih, F. et al. (1996) Proc. Natl. Acad. Sci. USA 93, 5533-5538.
    9. Rajpal, A. et al. (2003) EMBO J. 22, 6526-6536.
    10. Hirata, Y. et al. (1993) J. Biol. Chem. 268, 24808-24812.
    11. Hazel, T.G. et al. (1991) Mol. Cell. Biol. 11, 3239-3246.
    12. Li, H. et al. (2000) Science 289, 1159-1164.
    13. Lin, B. et al. (2004) Cell 116, 527-540.
    14. Pekarsky, Y. et al. (2001) Proc. Natl. Acad. Sci. U S A 98, 3690-3694.
    15. Han, Y.H. et al. (2006) Oncogene 25, 2974-2986.
    16. Wingate, A.D. et al. (2006) Biochem. J. 393, 715-724.
    17. Katagiri, Y. et al. (1997) J. Biol. Chem. 272, 31278-31284.
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