A 15-aa peptide sequence from the N-terminal domain of mouse RSSG or RS1 . The kidneys play a major role in the regulation of glucose levels. Kidneys filter approx. 180 g of glucose per day from the blood, and this is mostly reabsorbed back into the blood in the proximal tubules. Typically, glucose is first absorbed within epithelium by a specific transporter protein, Sodium glucose co transporters (SGLT), in the brush-border membrane and then it is transported out of the cell across the basolateral membranes by a facilitated sugar transporter (GLUTs). At least 3 members of SGLTs (SGLT1-3) have been cloned and characterized from various species. Individual member of this family have identical predicted secondary structures with up to 14 transmembrane domains. SGLT1-3 genes code for protein of approx 659-672 residues (calculated size of ~75kD). Both N and C-termini are predicted to be extracellualr. There is approx 60-70% homology between SGLT1-3. SGLTs transport a-methyl-D-glucoside (a-MDG), a non-metabolized model substrate, in Na-dependent manner. SGLT1 does not discriminate a-MDG, glucose, and galactose. SGLT2/3 do not transport D-galactose efficiently. Recently, a cDNA (pRS1 from pig and hRS1 from human) has been cloned and expressed that encodes a membrane-associated protein that alters sugar transport by SGLT1 and SMIT. RS1 (mouse 582 aa, pig 623 aa, 617 aa, chromosome 1p36.1, ~67kD) is also described as regulatoru subunit or beta-subunit of SGLT (RSSG) or regulatory solute carrier protein. RS1 is expressed in renal outer cortex, outer medulla, small intestine, liver, and LLCPK1 cells. Coexpression of hRS1 and SGLT1 in oocytes inhibits SGLT1 expression.
Purity:
Highly purified
Form:
Supplied as a liquid in PBS, pH 7.2
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