SLC22A6 Protein, Human (Sf9, His, Strep, FLAG)

The SLC22A6 protein acts as a Na(+)-independent organic anion (OA)/dicarboxylic acid antiporter and promotes renal elimination by transporting OA from proximal tubule cells into the urine. It transports coenzymes (BH4, BH2, septopterin) and determines blood biopterin levels as well as prostaglandins, cyclic nucleotides, tryptophan metabolites, uremic toxins (e.g. indoxyl sulfate) and xenobiotics (e.g. ochratoxin). SLC22A6 Protein, Human (Sf9, His, Strep, FLAG) is the recombinant human-derived SLC22A6 protein, expressed by Sf9 insect cells , with N-Strep, C-Flag, N-8*His labeled tag. The total length of SLC22A6 Protein, Human (Sf9, His, Strep, FLAG) is 562 a.a., .

SLC22A6 protein functions as a secondary active transporter, acting as a Na(+)-independent organic anion (OA)/dicarboxylate antiporter. This transporter facilitates the uptake of OAs across the basolateral side of proximal tubule epithelial cells, contributing to the renal elimination of endogenous OAs from the systemic circulation into urine. Additionally, SLC22A6 is involved in the transport of coenzymes such as tetrahydrobiopterin (BH4), dihydrobiopterin (BH2), and sepiapterin to urine, determining baseline levels of blood biopterins. It also plays a role in the transport of prostaglandins, cyclic nucleotides, neuroactive tryptophan metabolites, and potentially toxic compounds like uremic toxins (e.g., indoxyl sulfate, hippurate) and xenobiotics (e.g., ochratoxin). Moreover, SLC22A6 may contribute to the disposition of uremic toxins and xenobiotics by the renal organic anion secretory pathway, reducing their undesired toxicological effects. In testes, it potentially participates in the transport of organic compounds across the blood-testis barrier.

Human

Sf9 insect cells

N-Strep;C-Flag;N-8*His

Q4U2R8 (A2-L563)

9356

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.