Phospho-Jun B (S259) Polyclonal Antibody, 100 µg, (ATB-P0158)

Description

Background:

Transcription factor involved in regulating gene activity following the primary growth factor response. Binds to the DNA sequence 5′-TGA[CG]TCA-3′.

Product datasheet:

References:

1. jun-B inhibits and c-fos stimulates the transforming and trans-activating activities of c-jun.
   Schuette J., Viallet J., Nau M., Segal S., Fedorko J., Minna J.
   Cell 59:987-997(1989) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
2. Isolation of human cDNA clones of jun-related genes, jun-B and jun-D.
   Nomura N., Ide M., Sasamoto S., Matsui M., Date T., Ishizaki R.
   Nucleic Acids Res. 18:3047-3048(1990) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
3. Complex genetic organization of junB: multiple blocks of flanking evolutionarily conserved sequence at the murine and human junB loci.
   Phinney D.G., Tseng S.W., Ryder K.
   Genomics 28:228-234(1995) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Placenta.
4. NIEHS SNPs program
   Submitted (SEP-2004) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT VAL-230.
5. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
   The MGC Project Team
   Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Pancreas.
6. Negative regulation of the E3 ubiquitin ligase itch via Fyn-mediated tyrosine phosphorylation.
   Yang C., Zhou W., Jeon M.S., Demydenko D., Harada Y., Zhou H., Liu Y.C.
   Mol. Cell 21:135-141(2006) [PubMed] [Europe PMC] Cited for: INTERACTION WITH ITCH, UBIQUITINATION.
7. A quantitative atlas of mitotic phosphorylation.
   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-102; THR-104 AND SER-117, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
8. Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.
   Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
   Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-251; THR-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Leukemic T-cell.
9. Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.
   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
   Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-104; SER-117; SER-251 AND THR-255, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
10. System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-255 AND SER-259, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].