Anti-SLC38A9 / URLC11

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Solute carrier family 38 member 9 is a protein that in humans is encoded by the SLC38A9 gene. Sodium-coupled neutral amino acid transporter 9 (SLC38A9) is a lysosomal amino acid transporter, involved in the regulation of mechanistic target of rapamycin complex 1 (mTORC1) activity in response to amino acid levels within the lysosomal lumen. A sodium-couple amino acid transporter at the lysosome, SLC38A9, senses arginine from within the lysosome to convey arginine sufficiency to mTORC1. SLC38A9 forms a complex with other lysosomal resident proteins including the v-ATPase and a pentameric complex called Ragulator. v-ATPase function is necessary for mTORC1 activation, but the molecular mechanism of this regulation is currently unclear2. Ragulator binds strongly to the Rag GTPases and was shown to function as a guanine exchange factor (GEF) for RagA/B. Potentially SLC38A9 and the v-ATPase are able to regulate mTORC1 activity by modulating Ragulator?s GEF activity. RagA/B is not the only Rag GTPase that is regulated, but a Folliculin-FNIP2 complex is a GAP for RagC/D. In short, SLC38A9 is a functional component of the lysosomal amino acid sensing machinery involved in the control of mTORC1 activity, that underlies the regulation of the metabolic status and cellular responses to growth factors, energy, glucose and amino acid levels. Protein function: Lysosomal amino acid transporter involved in the activation of mTORC1 in response to amino acid levels (PubMed:25561175, PubMed:25567906, PubMed:29053970). Probably acts as an amino acid sensor of the Rag GTPases and Ragulator complexes, 2 complexes involved in amino acid sensing and activation of mTORC1, a signaling complex promoting cell growth in response to growth factors, energy levels, and amino acids (PubMed:25567906, PubMed:29053970). Following activation by amino acids, the Ragulator and Rag GTPases function as a scaffold recruiting mTORC1 to lysosomes where it is in turn activated (PubMed:25561175, PubMed:25567906). SLC38A9 mediates transport of amino acids with low capacity and specificity with a slight preference for polar amino acids (PubMed:25561175, PubMed:25567906). Acts as an arginine sensor (PubMed:25567906, PubMed:29053970, PubMed:31295473). Following activation by arginine binding, mediates transport of L- glutamine, leucine and tyrosine with high efficiency, and is required for the efficient utilization of these amino acids after lysosomal protein degradation (PubMed:29053970, PubMed:31295473). However, the transport mechanism is not well defined and the role of sodium is not clear (PubMed:25561175, PubMed:31295473). Can disassemble the lysosomal folliculin complex (LFC), and thereby triggers GAP activity of FLCN:FNIP2 toward RRAGC (PubMed:32868926). Acts as an cholesterol sensor that conveys increases in lysosomal cholesterol, leading to lysosomal recruitment and activation of mTORC1 via the Rag GTPases (PubMed:28336668). Guanine exchange factor (GEF) that, upon arginine binding, stimulates GDP release from RRAGA and therefore activates the Rag GTPase heterodimer and the mTORC1 pathway in response to nutrient sufficiency (PubMed:30181260). [The UniProt Consortium]