LAT2 Polyclonal Antibody
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The sequence shown here is derived from an Ensembl automatic analysis pipeline and should be considered as preliminary data.,Sodium-independent, high-affinity transport of small and large neutral amino acids such as alanine, serine, threonine, cysteine, phenylalanine, tyrosine, leucine, arginine and tryptophan, when associated with SLC3A2/4F2hc. Acts as an amino acid exchanger. Has higher affinity for L-phenylalanine than LAT1 but lower affinity for glutamine and serine. L-alanine is transported at physiological concentrations. Plays a role in basolateral (re)absorption of neutral amino acids. Involved in the uptake of methylmercury (MeHg) when administered as the L-cysteine or D,L-homocysteine complexes, and hence plays a role in metal ion homeostasis and toxicity. Involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L-nitrosocysteine (L-CNSO) across the transmembrane. Plays an essential role in the reabsorption of neutral amino acids from the epithelial cells to the bloodstream in the kidney.,induction:Activity in polarized intestinal cells is regulated by the association between SLC3A2/4F2 (in the SLC3A2/4F2-LAT2 heterodimer) and ICAM1.,miscellaneous:L-leucine transport activity inhibited by small zwitterionic amino acids (i.e. glycine, alanine, serine, threonine asparginine, glutamine, methionine, leucine, isoleucine, valine, phenylalanine, tyrosine, tryptophan, histidine and cysteine) and by glutamine and asparginine. Methionine uptake was inhibited by the L-system substrates L-leucine, 2-amino-bicyclo-(2,2,1)-heptane-2-carboxylate (BCH), L-cysteine and by the MeHg-L-cysteine complex and structurally related S-ethyl-L-cysteine. MeHg-L-cysteine uptake is inhibited by L-methionine, L-leucine, BCH and S-ethyl-L-cysteine. L-leucine uptake was inhibited by L-CNSO.,Belongs to the amino acid-polyamine-organocation (APC) superfamily. L-type amino acid transporter (LAT) (TC 2.A.3.8) family.,subcellular location:Localized to the cytoplasm when expressed alone but when coexpressed with SLC3A2/4F2hc, is localized to the plasma membrane. Colocalized with SLC3A2/4F2hc at the basolateral membrane of kidney cortex proximal tubules and small intestine epithelia of the villi.,subunit:Disulfide-linked heterodimer with the amino acid transport protein SLC3A2/4F2hc.,tissue specificity:Strongest expression is observed in kidney and moderate expression in placenta and brain, followed by liver, prostate, testis, ovary, lymph node, thymus, spleen, skeletal muscle and heart. Also expressed in fetal liver as well as in the retinal pigment epithelial cell line ARPE-19 and the intestinal epithelial cell line Caco-2.,
Fully tested in-house by ABMIUM, or supported by an advanced validation report from a partner reviewed by ABMIUM. Highest confidence. Non-conformities fully supported under the ABMIUM Product Promise.
Quality verified. Independent collaborator or expected-performance data available. Product meets ABMIUM quality standards.
Expected to work based on structural and biochemical data. Not yet directly tested by ABMIUM or a collaborator. No non-conformity support for this combination.
Not recommended for this application or species/sample combination. This may indicate either evidence of unsuitability or that the combination has not been tested and therefore cannot currently be recommended.
Evidence status by application and model.
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This product is manufactured by BT LAB and sold through ABMIUM without relabelling.
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