- Peptide (C)TDAPIQSYERIRN, corresponding to amino acid residues 13-25 of rat SGLT1 (Accession P53790). Extracellular, N-terminus.
- Western blot analysis of rat (lanes 1 and 3) and mouse (lanes 2 and 4) brain membranes:1,2. Anti-SGLT1 (extracellular) Antibody (#AGT-031), (1:200).
3,4. Anti-SGLT1 (extracellular) Antibody, preincubated with SGLT1 (extracellular) Blocking Peptide (#BLP-GT031).
- Western blot analysis of rat small intestine lysate:1. Anti-SGLT1 (extracellular) Antibody (#AGT-031), (1:200).
2. Anti-SGLT1 (extracellular) Antibody, preincubated with SGLT1 (extracellular) Blocking Peptide (#BLP-GT031).
- Expression of SGLT1 in rat brain sectionsImmunohistochemical staining of perfusion-fixed frozen rat brain sections using Anti-SGLT1 (extracellular) Antibody (#AGT-031), (1:400). A. SGLT1 staining in the hippocampal dentate gyrus reveals labeling of cells (red) in the granule layer (vertical arrows) and in hilar neurons (horizontal arrow). B. SGLT1 staining in the rat hypothalamic paraventricular nucleus region (in red), appears in cells lining the wall of the third ventricle (horizontal arrows) and in neurons of the paraventricular nucleus (vertical arrows). Cell nuclei are stained with DAPI (blue).
The SGLT-1 (Sodium-glucose linked transporter) is part of the SLC5 family of sodium-glucose transporters. This family has more than 220 members in human and bacterial cells and they are expressed in various tissues such as the gut, kidneys and the central nervous system. In human, these transporters are encoded by eleven genes1. SGLT-1 plays a vital role in carbohydrate metabolism and is mainly located in the brush membrane of mature enterocytes in the small intestine. It absorbs D-galactose and D-glucose derived from ingested food2.
SGLT-1 has 14 transmembrane α-helices with both the hydrophobic NH2 and hydrophilic COOH termini facing the extracellular side of the cell. SGLT-1 is a symport type transporter carrying sodium and glucose from extracellular space into the cell’s cytoplasm. It is believed that sodium binds to the hydrophobic part of the protein and causes a conformational change that enables sugar to binds to the COOH terminal3. The transporter has a number of consensus sites for glycosylation but none are required for the transporter’s function.
The transporter’s regulation was found to be modulated by PKA and PKC. PKA increases vesicle exocytosis 100-fold. Interestingly, the activation of PKC inhibits rat and rabbit SGLT-1 while stimulates human SGLT-14.
Pathologies linked to SGLT-1 include the glucose-galactose mal-absorption (GGM) disease caused by a mutation in the transporter. In mice, SGLT-1 knockout causes an inability to survive on glucose containing diets and a decreased insulin and incretin response to glucose5. SGLT-1 is also related to the successful treatment of secretory diarrhea by oral rehydration.
Species reactivity key:
Anti-SGLT1 (extracellular) Antibody (#AGT-031) is a highly specific antibody directed against an epitope of the rat sodium/glucose cotransporter 1. The antibody can be used in western blot and immunohistochemistry applications. It recognizes an extracellular epitope and is thus ideal for detecting the transporter in living cells. It has been designed to recognize SGLT1 from mouse and rat samples. The antibody is not recommended for use on human samples.