Cat. No. 519 005 |
50 µg specific antibody, lyophilized. Affinity purified with the immunogen. Albumin and azide were added for stabilization. For reconstitution add 50 µl H2O to get a 1mg/ml solution in PBS. Then aliquot and store at -20°C to -80°C until use. Antibodies should be stored at +4°C when still lyophilized. Do not freeze! |
Applications | |
Immunogen | Recombinant protein corresponding to residues near the amino terminus of rat LAT1 (UniProt Id: Q63016) |
Reactivity |
Reacts with: human (Q01650), rat (Q63016), mouse (Q9Z127). Other species not tested yet. |
Remarks |
IHC-G: 9% glyoxal, 8% acetic acid, in ddH2O, pH 4.2-4.4, according to Konno et al. 2023 is recommended |
Data sheet | 519_005.pdf |
LAT1 is ubiquitously expressed, with highest levels observed in the brain, spleen, bone marrow, testis, and placenta. In the blood-brain barrier, LAT1 is localized on both apical and basolateral membranes. In other polarized epithelia, it is mainly localized in basolateral membranes. In the placenta, LAT1 is present on both, the maternal and fetal surfaces of the syncytiotrophoblasts (1, 2).
Like all members of the heteromeric amino acid transporter (HAT, SLC7) family, LAT1 resides in the plasma membrane in a heterodimeric form. The LAT1 holotransporter consists of a 55-kDa light chain, SCL7A5 (LAT1 proper), and an escort protein called the heavy chain covalently linked to the light chain via a disulfide bond. LAT1 heterodimerizes with the 4F2hc (SLC3A2) heavy chain, an N-glycosylated ~68-kD transmembrane protein with one membrane-spanning domain. While transport carried out by either chain alone is negligible, the heavy chain is only needed to stabilize the dimer and facilitate its translocation to the plasma membrane, and the actual transport is carried out by the light chain (3).
LAT1 takes part in the transport of a wide range of neutral amino acids, especially ones with large branched or aromatic side chains. Tryptophan, phenylalanine, leucine, and histidine are transported with high affinity. Glutamine as an uptake substrate has a low affinity toward LAT1. Histidine and tyrosine are transported bidirectionally, whereas the others are preferentially transported in the inward direction only. LAT1 displays asymmetrical affinity towards bidirectionally transported substrates, with extracellular versus intracellular Km values being in the micromolar versus millimolar range (4). The generally accepted mode of function of LAT1 is obligatory antiport, i.e. the exchange of a large and neutral extracellular substrate for an abundant intracellular amino acid such as glutamine (5).