Phospho-LAT (Y200) Polyclonal Antibody, 100µg, (ATB-P0327)

Description

Background:

The protein encoded by this gene is phosphorylated by ZAP-70/Syk protein tyrosine kinases following activation of the T-cell antigen receptor (TCR) signal transduction pathway. This transmembrane protein localizes to lipid rafts and acts as a docking site for SH2 domain-containing proteins. Upon phosphorylation, this protein recruits multiple adaptor proteins and downstream signaling molecules into multimolecular signaling complexes located near the site of TCR engagement. Alternative splicing results in multiple transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008]

Required for TCR (T-cell antigen receptor)- and pre-TCR-mediated signaling, both in mature T-cells and during their development. Involved in FCGR3 (low affinity immunoglobulin gamma Fc region receptor III)-mediated signaling in natural killer cells and FCER1 (high affinity immunoglobulin epsilon receptor)-mediated signaling in mast cells. Couples activation of these receptors and their associated kinases with distal intracellular events such as mobilization of intracellular calcium stores, PKC activation, MAPK activation or cytoskeletal reorganization through the recruitment of PLCG1, GRB2, GRAP2, and other signaling molecules.

Product datasheet:

Overview
Product Description	Phospho-LAT (Y200) Polyclonal Antibody, 100µg, (ATB-P0327)
Image
Species Reactivities	Human,Mouse,Rat
Immunogen	Synthesized peptide derived from human LAT around the phosphorylation site of Y200.
Properties
Form	Liquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions	-20°C/1 year
Clonality	Polyclonal

References:

1. LAT1 is a critical transporter of essential amino acids for immune reactions in activated human T cells. Hayashi K, et al. J Immunol, 2013 Oct 15. PMID 24038088
2. Cutting edge: cell surface linker for activation of T cells is recruited to microclusters and is active in signaling. Balagopalan L, et al. J Immunol, 2013 Apr 15. PMID 23487428 Free PMC Article
3. Enhanced function of redirected human T cells expressing linker for activation of T cells that is resistant to ubiquitylation. Kunii N, et al. Hum Gene Ther, 2013 Jan. PMID 22998346 Free PMC Article
4. Pre-existing clusters of the adaptor Lat do not participate in early T cell signaling events. Williamson DJ, et al. Nat Immunol, 2011 Jun 5. PMID 21642986
5. LAT–an important raft-associated transmembrane adaptor protein. Delivered on 6 July 2009 at the 34th FEBS Congress in Prague, Czech Republic. Horejsí V, et al. FEBS J, 2010 Nov. PMID 20875087
6. LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation.
   Zhang W., Sloan-Lancaster J., Kitchen J., Trible R.P., Samelson L.E.
   Cell 92:83-92(1998) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), PROTEIN SEQUENCE OF 32-47 AND 219-233, PHOSPHORYLATION AT TYR-200, IDENTIFICATION BY MASS SPECTROMETRY, MUTAGENESIS OF TYR-200 AND TYR-220, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PIK3R1; GRB2; GRAP AND PLCG1. Tissue: Leukemia.
7. Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells.
   Weber J.R., Orstavik S., Torgersen K.M., Danbolt N.C., Berg S.F., Ryan J.C., Tasken K., Imboden J.B., Vaage J.T.
   J. Exp. Med. 187:1157-1161(1998) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). Tissue: Thymus.
8. Inactivation of pre-B cell receptor-mediated tumor suppression by aberrant splicing in Ph+ acute lymphoblastic leukemia.
   Muschen M.
   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databasesCited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 5). Tissue: Bone marrow.
9. The sequence and analysis of duplication-rich human chromosome 16.
   Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
   , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
   Nature 432:988-994(2004) [PubMed] [Europe PMC]

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

10. Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R.
    , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
    Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases

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