Glucagon-like peptide-1 receptor (GLP1R) is a 7-transmembrane receptor protein found on beta cells of the pancreas. It functions as a receptor for glucagon-like peptide 1 (GLP-1) hormone, which stimulates glucose-induced insulin secretion. GLP1R functions at the cell surface and becomes internalised in response to GLP-1 and GLP-1 analogs, playing an important role in the signalling cascades leading to insulin secretion. It is a member of the glucagon receptor family of G protein-coupled receptors [1]. GLP1R is composed of two domains, an extracellular domain that binds the C-terminal helix of GLP-1 [2], and a transmembrane domain [3] that binds the N-terminal region of GLP-1 [4][5][6].
GLP1R also displays neuroprotective effects in animal models. Polymorphisms in this gene are associated with diabetes, making it an important drug target for the treatment of type 2 diabetes. Alternative splicing of the GLP1R gene results in multiple transcript variants.
If you would like us to check if this antibody is likely to bind to this protein from a different species please contact us. We are happy to check for you.
Immunogen:
A synthetic peptide from the N-terminal region of Human GLP1R
If you would like further information regarding the immunogen used in the productiion of this antibody or have a query about whether this antibody will bind to your protein/species please contact us and we can do the analysis for you.
53kDa (Intended as a general guide and does not allow for all isoforms and species variations)
Subcellular location:
Cell membrane, Multi-pass membrane protein
Purification:
Affinity purification
References:
1. Brubaker PL, Drucker DJ (2002). "Structure-function of the glucagon receptor family of the G protein-coupled receptors: the glucagon, GIP, GLP-1, and GLP-2 receptors". Recept. Channels. 8 (34): 17988.
2. Underwood CR, Garibay P, Knudsen LB, Hastrup S, Peters GH, Rudolph R, Reedtz-Runge S (June 2010). "Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor". Journal of Biological Chemistry. 285 (1): 723730.
3. Song G, Yang D, Wang Y, de Graaf C, Zhou Q, Jiang S, Liu K, Cai X, Dai A, Lin G, Liu D, Wu F, Wu Y, Zhao S, Ye L, Han GW, Lau J, Wu B, Hanson MA, Liu ZJ, Wang MW, Stevens RC (2017). "Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators)". Nature. 546: 312315.
4. Wooten D, Reynolds CA, Koole C, Smith KJ, Mobarec JC, Simms J, Quon T, Coudrat T, Furness SG, Miller LJ, Christopolous A, Sexton PM (March 2016). "A Hydrogen-Bonded Polar Network in the Core of the Glucagon-Like Peptide-1 Receptor Is a Fulcrum for Biased Agonism: Lessons from Class B Crystal Structures". Molecular Pharmacology. 89 (3): 335347.
5. Wooten D, Reynolds CA, Smith KJ, Mobarec JC, Koole C, Savage EE, Pabreja K, Simms J, Sridhar R, Furness SG, Liu M, Thompson PE, Miller LJ, Christopolous A, Sexton PM (June 2016). "The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism". Cell. 165 (7): 16321643.
6. Yang D, de Graaf C, Yang L, Song G, Dai A, Cai X, Feng Y, Reedtz-Runge S, Hanson MA, Yang H, Jiang H, Stevens RC, Wang MW (June 2016). "Structural Determinants of Binding the Seven-transmembrane Domain of the Glucagon-like Peptide-1 Receptor (GLP-1R)". Journal of Biological Chemistry. 291 (25): 129913004.
7. Wooten D, Reynolds CA, Smith KJ, Mobarec JC, Furness SG, Miller LJ, Christopolous A, Sexton PM (August 2016). "Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptor". Biochemical Pharmacology. 118: 6887.
Glucagon-like peptide-1 receptor (GLP1R) is a 7-transmembrane receptor protein found on beta cells of the pancreas. It functions as a receptor for glucagon-like peptide 1 (GLP-1) hormone, which stimulates glucose-induced insulin secretion. GLP1R functions at the cell surface and becomes internalised in response to GLP-1 and GLP-1 analogs, playing an important role in the signalling cascades leading to insulin secretion. It is a member of the glucagon receptor family of G protein-coupled receptors [1]. GLP1R is composed of two domains, an extracellular domain that binds the C-terminal helix of GLP-1 [2], and a transmembrane domain [3] that binds the N-terminal region of GLP-1 [4][5][6].
GLP1R also displays neuroprotective effects in animal models. Polymorphisms in this gene are associated with diabetes, making it an important drug target for the treatment of type 2 diabetes. Alternative splicing of the GLP1R gene results in multiple transcript variants.
Product Type:
NS Reagents Antibody
Antibody Type:
Polyclonal
Format:
100 µg in 100 µl PBS containing 0.02% sodium azide.
If you would like us to check if this antibody is likely to bind to this protein from a different species please contact us. We are happy to check for you.
Immunogen:
A synthetic peptide from the N-terminal region of Human GLP1R
If you would like further information regarding the immunogen used in the productiion of this antibody or have a query about whether this antibody will bind to your protein/species please contact us and we can do the analysis for you.
53kDa (Intended as a general guide and does not allow for all isoforms and species variations)
Subcellular location:
Cell membrane, Multi-pass membrane protein
Purification:
Affinity purification
References:
1. Brubaker PL, Drucker DJ (2002). "Structure-function of the glucagon receptor family of the G protein-coupled receptors: the glucagon, GIP, GLP-1, and GLP-2 receptors". Recept. Channels. 8 (34): 17988.
2. Underwood CR, Garibay P, Knudsen LB, Hastrup S, Peters GH, Rudolph R, Reedtz-Runge S (June 2010). "Crystal structure of glucagon-like peptide-1 in complex with the extracellular domain of the glucagon-like peptide-1 receptor". Journal of Biological Chemistry. 285 (1): 723730.
3. Song G, Yang D, Wang Y, de Graaf C, Zhou Q, Jiang S, Liu K, Cai X, Dai A, Lin G, Liu D, Wu F, Wu Y, Zhao S, Ye L, Han GW, Lau J, Wu B, Hanson MA, Liu ZJ, Wang MW, Stevens RC (2017). "Human GLP-1 receptor transmembrane domain structure in complex with allosteric modulators)". Nature. 546: 312315.
4. Wooten D, Reynolds CA, Koole C, Smith KJ, Mobarec JC, Simms J, Quon T, Coudrat T, Furness SG, Miller LJ, Christopolous A, Sexton PM (March 2016). "A Hydrogen-Bonded Polar Network in the Core of the Glucagon-Like Peptide-1 Receptor Is a Fulcrum for Biased Agonism: Lessons from Class B Crystal Structures". Molecular Pharmacology. 89 (3): 335347.
5. Wooten D, Reynolds CA, Smith KJ, Mobarec JC, Koole C, Savage EE, Pabreja K, Simms J, Sridhar R, Furness SG, Liu M, Thompson PE, Miller LJ, Christopolous A, Sexton PM (June 2016). "The extracellular surface of the GLP-1 receptor is a molecular trigger for biased agonism". Cell. 165 (7): 16321643.
6. Yang D, de Graaf C, Yang L, Song G, Dai A, Cai X, Feng Y, Reedtz-Runge S, Hanson MA, Yang H, Jiang H, Stevens RC, Wang MW (June 2016). "Structural Determinants of Binding the Seven-transmembrane Domain of the Glucagon-like Peptide-1 Receptor (GLP-1R)". Journal of Biological Chemistry. 291 (25): 129913004.
7. Wooten D, Reynolds CA, Smith KJ, Mobarec JC, Furness SG, Miller LJ, Christopolous A, Sexton PM (August 2016). "Key interactions by conserved polar amino acids located at the transmembrane helical boundaries in Class B GPCRs modulate activation, effector specificity and biased signalling in the glucagon-like peptide-1 receptor". Biochemical Pharmacology. 118: 6887.
Uniprot ID:
P43220
Gene ID:
2740
Gene symbol:
GLP1R
Release Date:
Oct-18
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