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During the congress, E-Posters will be accessible to all participants on the congress website 24/7, as well as in the E-poster stations in the congress center.
Preparing your E-Poster
Please review the E-Poster format requirements carefully when preparing your E-Poster. Should your E-Poster not meet the mentioned requirements, it may not be displayed as described above.
E-Poster Submission Deadline
Please prepare and upload your E-Poster no later than March 14, 2026 11.59PM CET. After this date, you will no longer be able to prepare and upload your E-poster and it will not be displayed and accessible on the congress website.
Please follow the instructions below to input your abstract title.
Abstract titles should be brief and reflect the content of the abstract.
Sodium-glucose cotransporter 2 (SGLT2) plays a central role in renal glucose reabsorption, and its inhibition confers renal and cardiovascular protection. However, reliable detection of SGLT2 protein remains challenging due to concerns regarding the specificity of anti-SGLT2 antibodies. In the present study, we characterized eight commercially available anti-SGLT2 antibodies using genetically engineered knockout rodents and human renal tissues.
Eight commercially available anti-SGLT2 antibodies, mainly selected from frequently cited sources, were evaluated by immunohistochemistry and Western blotting. Sglt2- and Sglt1-deficient mice and rats were generated using the improved genome-editing via oviductal nucleic acids delivery (i-GONAD) technique, which is a clustered regularly interspaced short palindromic repeats/CRISPR-associated protein 9 (CRISPR/Cas9)-based in vivo gene-editing approach. Wild-type, Sglt1 knockout, and Sglt2 knockout littermates were analyzed in parallel. Human kidney tissues, including renal cell carcinoma samples, were also examined to assess interspecies consistency and clinical applicability.
Among the antibodies tested, only a few exhibited high specificity, showing clear immunostaining in wild-type and Sglt1-deficient kidneys, but complete absence of staining in Sglt2-deficient samples. Ethylenediaminetetraacetic acid (EDTA)-based antigen retrieval produced optimal immunostaining, while citrate buffer resulted in weak signals. Subcellular localization analyses revealed enrichment of SGLT2 within the microvillar zone of proximal tubular cells, with partial colocalization with PDZK1IP1 (MAP17), a known SGLT2 cofactor. In contrast, LRP2 (megalin) and NHE3 localized to the microvillar base and showed no overlap with SGLT2. In human renal cell carcinoma samples, validated antibodies detected SGLT2 expression in proximal tubules of non-tumor regions, but not in carcinoma areas. In Western blot analyses, several antibodies detected a specific SGLT2 band at approximately 55 kDa in wild-type kidneys under optimized lysis conditions. Following N-glycan removal by PNGase F, the band shifted to 45 kDa. One anti-SGLT2 antibody exhibited a weak non-specific band at the same molecular mass even in Sglt2-deficient samples.
Remarkable variability exists in the specificity of commercially available anti-SGLT2 antibodies. Only a limited number enable reliable detection of SGLT2 when combined with carefully optimized procedures, including antigen retrieval in immunohistochemistry and protein extraction protocols in Western blotting. These validated antibodies and protocols will provide a robust framework for assessing SGLT2 localization, post-translational modification, and expression levels.
