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Validated All-in-One™ qPCR Primer for SLC5A1(NM_000343.3) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Validated result:
Summary
Glucose transporters are integral membrane proteins that mediate the transport of glucose and structurally-related substances across cellular membranes. Two families of glucose transporter have been identified: the facilitated-diffusion glucose transporter family (GLUT family), also known as 'uniporters,' and the sodium-dependent glucose transporter family (SGLT family), also known as 'cotransporters' or 'symporters' (Wright et al., 1994 [PubMed 7823022]). The SLC5A1 gene encodes a protein that is involved in the active transport of glucose and galactose into eukaryotic and some prokaryotic cells.[supplied by OMIM].
Gene References into function
- Mutations of this gene protein (mapped to Chromosome 22) causes glucose-galactose malabsorption in infants. Sugar transport is impaired mainly because the mutant proteins are either truncated or are not targeted properly to the cell membrane.
- Intracellular compartments containing SGLT1 are involved in the regulation of SGLT1 abundance at the apical cell surface.
- Taken together, these data indicate that RSC1A1 modulates dynamin-dependent trafficking of intracellular vesicles containing hSGLT1 in Xenopus oocytes, and modulates PKC-dependent short-term regulation of this transporter.
- Na+-coupled glucose transporter 1 (SGLT1) was regulated by neuronal cell expressed developmentally downregulated 4-2 (Nedd4-2) and serum- and glucocorticoid-inducible kinase 1 (SGK1)
- Aspartate residue 454 of SGLT1 is critically important for normal trafficking of the protein to the plasma membrane.
- Our results indicate that the major voltage-dependent step of the Na(+)/glucose transport cycle is the return of the empty carrier from inward to outward facing conformations.
- Thus, the C351A and C361A mutations might cause a global reorganization of the disulfide bonds of SGLT1.
- the large, hydrophilic loop near the carboxyl terminus of SGLT1 does not appear to play a major part in the binding of phlorizin
- SGLT-1 has a role in glucose uptake and in protecting intestinal epithelial cells against LPS-induced apoptosis and barrier defects
- 3 conformational states of SGLT1 differ in their packing density and surface hydrophobicity, reflecting the empty carrier, the d-glucose loaded carrier facing the outside of membrane and the complex of the outside-orientated carrier with phlorizin
- water transport across the membrane can be explained by cotransport of water in the membrane proteins and that intracellular unstirred layers effects are minute
- results indicate that cysteine residues C255 and C511 form a disulfide bridge in human SGLT1 and that this disulfide bridge is involved in the conformational change of the free carrier
- hRS1 protein exhibits glucose-dependent, short-term inhibition of hSGLT1 and hOCT2 by inhibiting the release of vesicles from the trans-Golgi network.
- description of a novel feedback mechanism in apoptotic signaling pathway for SGLT-1-dependent cytoprotection; observation suggests new function for CD14 on enterocytes involving induction of caspase-dependent SGLT-1 activity which leads to cell rescue
- study examines the conformations of the Na(+)/glucose cotransporter during sugar transport using charge and fluorescence measurements
- Results describe the effect of taurine on glucose transporter using heterologous expression of sodium-glucose transporter-1 (SGLT-1).
- These studies demonstrate the existence of different conformational states of the membrane-embedded transporter in its glucose-free form, as sodium-glucose-carrier complex and as sodium-phlorizin-carrier complex.
- Data show that hSGLT1 does not transport any of the flavonoids and seems therefore not involved in their intestinal absorption.
- Thioglycoside VII (2-hydroxymethyl-phenyl-1'-thio-beta-D-galacto-pyranoside) had a pronounced inhibitory effect on hSGLT1.
- RSC1A1 codes for a 67-kDa protein named RS1 that mediates transcriptional and post-transcriptional regulation of Na(+)-D-glucose cotransporter SGLT1.
- D28G mutation in 16 family members of a patient with typical presentation of congenital glucose-galactose malabsorption
- the native carrier ( sodium/D-glucose cotransporter 1)residues Gln at position 457 and Thr at position 460 reside in a hydrophilic access pathway extending 5-7 A into the membrane to which sugars as well as the sugar moiety of inhibitory glucosides bind
- this high-capacity functional assay should provide a means to identify novel and selective SGLT inhibitors
- Ongoing work is aimed at identifying the localization signals in the SGLT1 3'-UTR and the corresponding binding proteins.
- activation of SGLT-1 by glucose protects from damages induced by TLR ligands, in human intestinal epithelial cells and in a murine model of septic shock.
- High SGLT1 expression in pancreatic adenocarcinomas significantly correlates with DFS & a trend was found for OS, especially in younger patients. High SGLT1 expression in primary tumors correlates with high Bcl-2 expression, not p53 expression.
- Protein kinase A-mediated phosphorylation of the transporter represents a further mechanism in the regulation of SGLT1-mediated glucose transport in epithelial cells
