Recombinant Human Glucagon-Like Peptide 1 Receptor (GLP1R) Protein (His)

Name: Recombinant Human Glucagon-Like Peptide 1 Receptor (GLP1R) Protein (His)
Brand: Beta LifeScience
SKU: BLC-03171P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Glucagon-Like Peptide 1 Receptor (GLP1R) Protein (His) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P43220
Target Symbol	GLP1R
Synonyms	GLP1R; Glucagon-like peptide 1 receptor; GLP-1 receptor; GLP-1-R; GLP-1R
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	RPQGATVSLWETVQKWREYRRQCQRSLTEDPPPATDLFCNRTFDEYACWPDGEPGSFVNVSCPWYLPWASSVPQGHVYRFCTAEGLWLQKDNSSLPWRDLSECEESKRGERSSPEEQLLFLY
Expression Range	24-145aa
Protein Length	Partial
Mol. Weight	18.3kDa
Research Area	Cardiovascular
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function	G-protein coupled receptor for glucagon-like peptide 1 (GLP-1). Ligand binding triggers activation of a signaling cascade that leads to the activation of adenylyl cyclase and increased intracellular cAMP levels. Plays a role in regulating insulin secretion in response to GLP-1.
Subcellular Location	Cell membrane; Multi-pass membrane protein.
Protein Families	G-protein coupled receptor 2 family
Database References	HGNC: 4324 OMIM: 138032 KEGG: hsa:2740 STRING: 9606.ENSP00000362353 UniGene: PMID: 29329976 The study provides evidence that the insulinotropic action of zfGIP in mammalian systems involves activation of both the GLP-1 and the GIP receptors but not the glucagon receptor PMID: 29157578 Clinical studies in non-diabetic patients with neurodegenerative disorders showed neuroprotective effects following administration with GLP-1 receptor agonists, demonstrating that neuroprotective effects are independent of blood glucose levels. PMID: 29412810 Some GLP-1 receptor agonist (GLP-1RA) have been approved for the treatment of type 2 diabetes mellitus(T2DM) and although clinical trials may not have been designed to investigate bone fracture, first results suggest that GLP-1RA may not exacerbate abnormal bone quality observed in T2DM PMID: 29412811 Here, we discuss recent findings concerning the signalling and trafficking of the GLP-1R in pancreatic beta cells. Leveraging "bias" at the receptor towards cAMP generation versus the recruitment of beta-arrestins and extracellular signal-regulated kinases (ERK1/2) activation may allow the development of new analogues with significantly improved clinical efficacy. PMID: 29412835 This may represent a potential mechanism for GLP-1R agonist-induced cardioprotection in type 2 diabetes , as increases in fatty acid oxidation and decreases in glucose oxidation are frequently observed in the hearts of animals and human subjects with T2D. PMID: 29412838 In type 2 diabetic patients from a Han Chinese population, some variations in the GLP-1R gene were associated with a lower risk of developing coronary artery disease. PMID: 30271789 Activation of endogenous GLP-1 is associated with sepsis in patients with type 2 diabetes. PMID: 29334697 increased GLP-1R innervation in IBD bowel could mediate enhanced visceral afferent signalling, and provide a peripheral target for therapeutic intervention PMID: 29813107 GLP1R mRNA transcripts, encompassing the entire open reading frame, were detected in all four cardiac chambers from 15 hearts at levels approximating those detected in human pancreas. PMID: 29444223 Low active GLP-1 secretion is associated with hypertriglyceridaemia. PMID: 29135069 this study, we investigated whether glucagon and glucagon-like peptide-1 (GLP-1), hormones produced by alpha cells, contribute to insulin secretion in INS-1 cells, a beta cell line. Co-treatment with glucagon and exendin-4 (Ex-4), a GLP-1 receptor agonist, additively increased glucose-stimulated insulin secretion in INS-1 cells PMID: 29725251 genetic association studies in population in Republic of Korea: Data suggest that SNPs in PAX4 and GLP1R are associated with type 2 diabetes (T2D) in the population studied. In genome-wide associations, PAX4 Arg192His increased risk of T2D; GLP1R Arg131Gln decreased risk of T2D. (PAX4 = paired box 4 protein; GLP1R = glucagon-like peptide 1 receptor) PMID: 29941447 LINC01121 functions as a tumor promoter by means of its involvement in the process of translational repression of the GLP1R and inhibition of the cAMP/PKA signaling pathway. PMID: 29843149 cryo-EM structure of the human GLP-1 receptor in complex with the G protein-biased peptide exendin-P5 and a Galphas heterotrimer, determined at a global resolution of 3.3 A PMID: 29466332 The results demonstrate the exendin-4 induces a partial reduction in triglycerides in steatotic hepatocytes within 12 h via the GLP-1 receptor-mediated activation of protein kinase A. Thus, the reduction in hepatocyte triglyceride accumulation is likely driven primarily by downregulation of lipogenesis and upregulation of beta-oxidation of free fatty acids PMID: 28707223 Data (including data from studies in knockout mice) suggest that MIR204 (which is highly enriched in beta-cells) directly targets 3'-untranslated region of GLP1R and thereby down-regulates expression of GLP1R in beta-cells. Studies were also conducted in primary human and mouse beta-cells and in rat insulinoma cell line. PMID: 29101219 Data suggest that GLP1R signaling in pancreatic beta-cells leading to insulin secretion involves interactions of GLP1R with HIP1, SNX1, and SNX27; HIP1 appears to regulate coupling of cell surface GLP1R activation with endocytosis; SNX1 and SNX27 appear to control balance between GLP1R plasma membrane recycling and lysosomal degradation. PMID: 29284659 The GLP-1R was abundantly expressed in numerous regions, including the septal nucleus, hypothalamus, and brain stem. PMID: 29095968 This is the first time that human Epicardial adipose tissue is found to express both GLP-1R and GLP-2R genes. PMID: 28514806 Changes in GLP-1 levels are associated with weight loss in newly diagnosed Chinese diabetes patients receiving acarbose PMID: 27717194 the present study revealed that overexpression of GLP1R significantly reduces proliferation, migration and cytokine release in ASM cells from COPD patients; this involved a significant increase in ABCA1 expression levels. This provided evidence to suggest that GLP1R may be a potential therapeutic target for the treatment of COPD. PMID: 28560433 IL-33, GLP-1R, and CCL20 are deregulated in human inflammatory bowel disease. GLP-1 receptor agonists upregulate IL-33, mucin 5b, and CCL20 in murine Brunner's glands. GLP-1 receptor agonists affect gut homeostasis in both proximal and distal parts of the gut. PMID: 27542128 Data show that exendin-4 (Ex-4) could attenuate breast cancer cell proliferation via activation of glucagonlike peptide-1 (GLP-1) receptor (GLP-1R) and subsequent inhibition of nuclear factor kappaB (NF-kappaB ) activation. PMID: 29045658 crystal structure of the full-length GLP-1 receptor bound to a truncated peptide agonist PMID: 28562585 crystal structures of the human GLP-1R transmembrane domain in complex with two different negative allosteric modulators, PF-06372222 and NNC0640, at 2.7 and 3.0 A resolution, respectively PMID: 28514449 Data suggest that pancreatic level of GLP1R is highest in insulin-secreting cells; here, highest intensity of GLP1R immunostaining was observed in beta-cells in pancreatic tissues obtained from organ-donor cadavers with type 2 diabetes. PMID: 28094469 Data show that purified glucagon-like peptide-1 (GLP-1) receptor (GLP1R)GLP1R in nanodiscs that could bind to GLP-1 and exendin-4 and activate Gs protein. PMID: 28609478 Dapagliflozin, when added in real life to patients with T2DM treated with GLP1-R agonists, induced a further significant, albeit modest improvement in A1C and a further weight loss. PMID: 28077257 analysis of the biological binding site of exendin-4 peptide in the N-terminal domain of the intact human glucagon-like peptide-1 receptor PMID: 28283573 GLP1-R may represent a novel target for treating bronchial hyperresponsiveness. PMID: 27447052 Our studies show that GLP-1R is widely expressed throughout the human hypothalamus. The decreased expression of GLP-1R in the PVN and IFN of T2DM patients may be related to the dysregulation of feeding behavior and glucose homeostasis in type 2 diabetes mellitus. PMID: 26672638 In conclusion, exenatide significantly improves coronary endothelial function in patients with newly diagnosed type 2 diabetes. The effect may be mediated through activation of AMPK/PI3K-Akt/eNOS pathway via a GLP-1R/cAMP-dependent mechanism. PMID: 27072494 A higher likelihood of attaining A1c goal levels were observed when a GLP-1R agonists was initiated. PMID: 28230449 Immunohistochemistry of human ileum tissues was performed in this study, which showed that TAS2R38 was co-localized with glucagon-like peptide 1 (GLP-1) in enteroendocrine L-cells. PMID: 27208775 Data suggest that three conserved positively charged residues located at extracellular ends of transmembrane helices 3, 4 and 5 of GLP1R are essential for high affinity agonist binding and conformational transitions linked to pleiotropic effector coupling through stabilisation of extracellular domains. PMID: 27569426 The rate of homologous desensitization and internalization of the GLP-1R has been determined in a transgenic cell line system. PMID: 28035964 In glucagon-like peptide receptor (GLP-1R) expressing cells, small molecule agonists induced cAMP production but caused no intracellular Ca2+ accumulation, ERK phosphorylation or hGLP-1R internalisation. PMID: 27100083 We aimed to investigate whether genetic variations in glucagon-like peptide receptor are associated with responses to dipepdityl peptidase-4 inhibitors in patients with type 2 diabetes. Polymorphism in the GLP-1 receptor may influence DPP-4 inhibitor response. PMID: 27858848 Results suggest that pancreatic ductal adenocarcinoma (PDAC) cells or their precursor lesions do not overexpress glucagon-like peptide-1 receptor (GLP-1R) compared with non-neoplastic pancreatic cells. PMID: 26495786 The molecular dynamics simulations of wild-type and mutant GLP-1R.ligand complexes provided molecular insights into GLP-1R-specific recognition mechanisms for the N terminus of GLP-1 by residues in the 7TM pocket and explained how glucagon-mimicking GLP-1 mutants restored binding affinity for (glucagon receptor -mimicking) GLP-1R mutants. PMID: 27059958 NMR-determined structure of a high-potency cyclic conformationally-constrained 11-residue analogue of GLP-1 was also docked into the receptor-binding site. PMID: 26598711 Lack of association of rs6923761 GLP-1 R polymorphism with weight loss. PMID: 26015316 An association was found between the rs6923761 GLP-1 receptor polymorphism and basal GLP-1 levels in diabetes mellitus type 2 patients. PMID: 25200998 although GLP-1R is not an independent prognostic factor in PDAC patients, it appears to have some implications for pancreatic ductal adenocarcinoma metastatic ability PMID: 26238361 Retinal GLP1R expression was similar in patients with diabetes and healthy controls. PMID: 26384381 reduced level in renal arteries of hypertensive patients PMID: 25915883 these findings demonstrate the hGLP-1R has distinct regions within the C-terminal domain required for its cell surface expression, activity and agonist-induced internalisation. PMID: 26116235 GLP-1R rs10305420 polymorphism explained some of the inter-individual differences in response to liraglutide regarding weight loss in obese PCOS women. PMID: 25991051 168Ser (rs6923761) was nominally associated with alcohol use disorder. The 168 Ser/Ser genotype was associated with increased alcohol administration, and with higher BOLD response in the right globus pallidus. PMID: 26080318

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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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