SLC26A7 is encoded by the SLC26A7 gene and is also known as Anion exchange transporter and Solute carrier family 26 member 7. SLC26A7 is a member of the SLC26 transporter family, which have limited expression in different tissues to support critical physiological functions. It has been reported that SKC26A7 functions as a Cl-/HCO3- exchanger and/or as a Cl- channel. SLC26A7 is abundantly expressed in the stomach and mediates Cl-/HCO3- exchange and the expression is limited to the basolateral membrane of gastric parietal cells.
|Basic Information of SLC26A7|
|Protein Name||Anion exchange transporter|
|Aliases||olute carrier family 26 member 7|
|Organism||Homo sapiens (Human)|
SLC26A7 shows very restricted distribution, and so far it has been found only in gastric parietal cells and the intercalated cells of the outer medullary collecting duct. Unlike other members of the family that are expressed at the luminal membrane of epithelial cells, SLC26A7 was found at the basolateral membrane of both parietal cells and intercalated cells. It was reported that SLC26A7 functions as a coupled Formula exchanger and was thus suggested to play an important role in clearing formula from the parietal cells during acid secretion. Furthermore, SLC26A7 was reported to be markedly activated by cell shrinkage and thus to mediate formula efflux into the hypertonic fluid of the collecting duct. Meanwhile, SLC26A7 is reported to be involved in cellular pH regulation in other epithelial cells leaves open the possibility that SLC26A7 is needed in Reissner’s membrane cells during perturbations of pH in either intracellular or extracellular pH.
Fig.1 Proposed structure of SLC26A7 membrane protein. (Chang, 2017)
This article reports that SLC26A7 participates in Cl- transport in Reissner’s membrane epithelial cells. Meanwhile, SLC26A7 is also involved in cellular pH regulation in other epithelial cells leaves open the possibility that SLC26A7 is needed in Reissner’s membrane cells during local perturbations of pH.
This article proposes that SLC26A7 is a basolateral Cl-/HCO3- exchanger in intercalated cells of the outer medullary collecting duct and may play an important role in bicarbonate reabsorption in the medullary collecting duct.
This article suggests that the activity of SLC26A7 was inhibited by all inhibitors of anion transporters tested, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid, diphenylamine-2-carboxylic acid, and glybenclamide. These findings reveal that SLC26A7 functions as a unique Cl- channel that is regulated by intracellular H+.
The data of this article indicate that SLC26A7 play an important role in ion transporters in the pH regulatory network during enamel maturation. The data obtained from double mutant animals (Slc26a1−/− and Slc26a7−/−) provide new evidence from a functional perspective to support the hypothesis that SLC26A1/SAT1 and SLC26A7/SUT1 are actively involved in ameloblast mediated pH regulation during maturation-stage amelogenesis.
This article shows that SLC26A1, SLC26A6, and SLC26A7 are novel participants in the extracellular transport of bicarbonate during enamel maturation and that their functional roles may be achieved by forming interaction units with Cftr.
To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC26A7 antibody development services.
Creative Biolabs has accomplished numerous challenging projects including generation of many functional membrane proteins successfully, we have won good reputation among our worldwide customers as a forward-looking research institute as well as a leading customer service provider in the field of membrane protein. Please feel free to contact us for more information.