SLC7A9
SLC7A9 (solute carrier family 7 member 9, also known as BAT1 and CSNU3) is the light subunit of a heteromeric amino acid transporter. It works with SLC3A1 to exchange cationic and neutral amino acids and supports cystine reabsorption in the kidney. Browse Assay Genie's current range of SLC7A9 research reagents below, or read on for the biology behind the target.
SLC7A9 associates with SLC3A1 to form a functional transporter complex that mediates electrogenic exchange between cationic amino acids and neutral amino acids, with a stoichiometry of 1:1. The complex shows system b(0,+)-like activity, with high affinity for extracellular cationic amino acids and L-cystine and lower affinity for intracellular neutral amino acids. Exchange is driven by a high intracellular concentration of neutral amino acids and by the intracellular reduction of L-cystine to L-cysteine.
The protein is required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane of renal proximal tubules, and it localises to the apical cell membrane. The SLC7A9 gene encodes a member of the light subunit family of amino acid transporters and belongs to the amino acid-polyamine-organocation (APC) superfamily and the HGNC solute carrier family 7 group. Transport is high-affinity and sodium-independent, and it covers cystine as well as neutral and dibasic amino acids. Alternate transcript variants have been described that encode the same protein. Mouse and rat orthologs are both named Slc7a9.
Mutations in the SLC7A9 gene cause non-type I cystinuria, in which impaired transport of cystine and dibasic amino acids leads to cystine stones in the urinary system. This link explains the earlier names for the gene, which include solute carrier family 7 (amino acid transporter light chain, bo,+ system), member 9 and cystinuria type 3 (CSNU3). Researchers studying SLC7A9 protein expression often examine it together with its heavy-chain partner SLC3A1.
SLC7A9 is required for reabsorption of L-cystine and dibasic amino acids across the brush border membrane of renal proximal tubules.
Mutations in SLC7A9 cause non-type I cystinuria, where impaired cystine transport leads to cystine stones in the urinary system.
SLC7A9 pairs with SLC3A1 to form a functional complex, making it a model for light and heavy subunit transporter studies.
The complex exchanges cationic and neutral amino acids 1:1 in an electrogenic process driven by intracellular neutral amino acids and cystine reduction.
SLC7A9 is the light subunit of a transporter that associates with SLC3A1 to exchange cationic amino acids for neutral amino acids at a 1:1 ratio. It has high affinity for extracellular cationic amino acids and L-cystine, and it is required for cystine and dibasic amino acid reabsorption in renal proximal tubules.
SLC7A9 is also called BAT1 and CSNU3, and UniProt names the protein b(0,+)-type amino acid transporter 1. Earlier HGNC names include solute carrier family 7 (amino acid transporter light chain, bo,+ system), member 9, and cystinuria type 3. Alternate transcripts encode the same protein.
Mutations in SLC7A9 cause non-type I cystinuria, which produces cystine stones in the urinary system because cystine and dibasic amino acid transport is impaired. Mouse and rat both have an Slc7a9 ortholog; check the datasheet of any product for its validated reactivity.
Other solute carrier transporters, including amino acid and renal transport proteins, with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt P82251; product specifications from Assay Genie datasheets.