Human CD98, recombinant (C-6His)

Recombinant Human CD98 is produced by our Mammalian expression system and the target gene encoding Arg206-Ala630 is expressed with a 6His tag at the C-terminus. Protein function: Component of several heterodimeric amino acid transporter complexes (PubMed:11557028, PubMed:9829974, PubMed:9751058, PubMed:10391915, PubMed:10574970, PubMed:11311135). The precise substrate specificity depends on the other subunit in the heterodimer (PubMed:9829974, PubMed:9751058, PubMed:10391915, PubMed:10574970, PubMed:30867591, PubMed:10903140). The heterodimer with SLC3A2 functions as sodium-independent, high-affinity transporter that mediates uptake of large neutral amino acids such as phenylalanine, tyrosine, L-DOPA, leucine, histidine, methionine and tryptophan (PubMed:9751058, PubMed:11557028, PubMed:11311135, PubMed:11564694, PubMed:12117417, PubMed:12225859, PubMed:25998567, PubMed:30867591). The complexes with SLC7A6 and SLC7A7 mediate uptake of dibasic amino acids (PubMed:9829974, PubMed:10903140). The complexes function as amino acid exchangers (PubMed:11557028, PubMed:10903140, PubMed:12117417, PubMed:12225859, PubMed:30867591). Required for targeting of SLC7A5 and SLC7A8 to the plasma membrane and for channel activity (PubMed:9751058, PubMed:11311135, PubMed:30867591). Plays a role in nitric oxide synthesis in human umbilical vein endothelial cells (HUVECs) via transport of L-arginine. The heterodimer with SLC7A5/LAT1 may play a role in the transport of L-DOPA across the blood-brain barrier. May mediate blood-to-retina L- leucine transport across the inner blood-retinal barrier. The heterodimer with SLC7A5/LAT1 can mediate the transport of thyroid hormones triiodothyronine (T3) and thyroxine (T4) across the cell membrane (PubMed:11564694, PubMed:12225859). When associated with SLC7A5 or SLC7A8, involved in the cellular activity of small molecular weight nitrosothiols, via the stereoselective transport of L- nitrosocysteine (L-CNSO) across the transmembrane (PubMed:15769744). The heterodimer with SLC7A5 is involved in the uptake of toxic methylmercury (MeHg) when administered as the L-cysteine or D,L- homocysteine complexes (PubMed:12117417). Together with ICAM1, regulates the transport activity SLC7A8 in polarized intestinal cells, by generating and delivering intracellular signals. When associated with LAPTM4B, the heterodimer formed by SLC3A2 and SLC7A5 is recruited to lysosomes to promote leucine uptake into these organelles, and thereby mediates mTORC1 activation (PubMed:25998567). [The UniProt Consortium]