Description

Background:

Transcriptional activator or repressor which probably serves as a general switch factor for erythroid development. It binds to DNA sites with the consensus sequence 5′-[AT]GATA[AG]-3′ within regulatory regions of globin genes and of other genes expressed in erythroid cells.

Product datasheet:

Overview

Product Description  
Species ReactivitiesHuman,Mouse,Rat
ImmunogenSynthesized peptide derived from human GATA-1 around the phosphorylation site of S142.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. Structure and evolution of a human erythroid transcription factor.
    Trainor C.D., Evans T., Felsenfeld G., Boguski M.S.
    Nature 343:92-96(1990) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). Tissue: Bone marrow.
  2. The major human erythroid DNA-binding protein (GF-1): primary sequence and localization of the gene to the X chromosome.
    Zon L.I., Tsai S.-F., Burgess S., Matsudaira P., Bruns G.A.P., Orkin S.H.
    Proc. Natl. Acad. Sci. U.S.A. 87:668-672(1990) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE. Tissue: Erythrocyte.
  3. The DNA sequence of the human X chromosome.
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O’dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d’Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

  4. 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] (ISOFORM 2). Tissue: Bone marrow.
  5. Alternative translation initiation site usage results in two functionally distinct forms of the GATA-1 transcription factor.
    Calligaris R., Bottardi S., Cogoi S., Apezteguia I., Santoro C.
    Proc. Natl. Acad. Sci. U.S.A. 92:11598-11602(1995) [PubMed] [Europe PMC] Cited for: ALTERNATIVE INITIATION (ISOFORM 3), SUBUNIT, TISSUE SPECIFICITY.
  6. Regulation of activity of the transcription factor GATA-1 by acetylation.
    Boyes J., Byfield P., Nakatani Y., Ogryzko V.
    Nature 396:594-598(1998) [PubMed] [Europe PMC] Cited for: INTERACTION WITH EP300, ACETYLATION AT LYS-233; LYS-245 AND LYS-246.
  7. An inherited mutation leading to production of only the short isoform of GATA-1 is associated with impaired erythropoiesis.
    Hollanda L.M., Lima C.S., Cunha A.F., Albuquerque D.M., Vassallo J., Ozelo M.C., Joazeiro P.P., Saad S.T., Costa F.F.
    Nat. Genet. 38:807-812(2006) [PubMed] [Europe PMC] Cited for: INVOLVEMENT IN XLAWT.
  8. PDSM, a motif for phosphorylation-dependent SUMO modification.
    Hietakangas V., Anckar J., Blomster H.A., Fujimoto M., Palvimo J.J., Nakai A., Sistonen L.
    Proc. Natl. Acad. Sci. U.S.A. 103:45-50(2006) [PubMed] [Europe PMC] Cited for: SUMOYLATION AT LYS-137, PHOSPHORYLATION AT SER-142, MUTAGENESIS OF LYS-137 AND SER-142.
  9. GATA-1 and Gfi-1B interplay to regulate Bcl-xL transcription.
    Kuo Y.-Y., Chang Z.-F.
    Mol. Cell. Biol. 27:4261-4272(2007) [PubMed] [Europe PMC] Cited for: INTERACTION WITH GFI1B.
  10. Knockdown of ZNF268, which is transcriptionally downregulated by GATA-1, promotes proliferation of K562 cells.
    Zeng Y., Wang W., Ma J., Wang X., Guo M., Li W.
    PLoS ONE 7:E29518-E29518(2012) [PubMed] [Europe PMC] Cited for: FUNCTION, DNA-BINDING.
external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

Reviews

There are no reviews yet.


Be the first to review “Phospho-GATA-1 (S142) Polyclonal Antibody, 100 µg, (ATB-P0952)”