Recombinant Mouse Glucagon Receptor (GCGR) Protein (His)

Name: Recombinant Mouse Glucagon Receptor (GCGR) Protein (His)
Brand: Beta LifeScience
SKU: BLC-09598P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

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Product Overview

Description	Recombinant Mouse Glucagon Receptor (GCGR) Protein (His) is produced by our Yeast expression system. This is a extracellular protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q61606
Target Symbol	GCGR
Synonyms	GcgrGlucagon receptor; GL-R
Species	Mus musculus (Mouse)
Expression System	Yeast
Tag	N-6His
Target Protein Sequence	AQVMDFLFEKWKLYSDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPPNTTANISCPWYLPWYHKVQHRLVFKRCGPDGQWVRGPRGQPWRNASQCQLDDEEIEVQKGVAKMYSSQQ
Expression Range	27-143aa
Protein Length	Extracellular Domain
Mol. Weight	15.8 kDa
Research Area	Others
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 that plays a central role in the regulation of blood glucose levels and glucose homeostasis. Regulates the rate of hepatic glucose production by promoting glycogen hydrolysis and gluconeogenesis. Plays an important role in mediating the responses to fasting. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and modulates the activity of down-stream effectors, such as adenylate cyclase. Promotes activation of adenylate cyclase. Besides, plays a role in signaling via a phosphatidylinositol-calcium second messenger system.
Subcellular Location	Cell membrane; Multi-pass membrane protein.
Protein Families	G-protein coupled receptor 2 family
Database References	KEGG: mmu:14527 STRING: 10090.ENSMUSP00000026119 UniGene: Mm.22329
Tissue Specificity	Expressed predominantly in liver, kidney, adrenal, lung and stomach, while lower levels of expression are detected in brown and white adipose tissue, cerebellum, duodenum and heart.

Gene Functions References

Data, including data from studies using knockout mice, suggest that control of whole-body energy expenditure by Gcgr agonism requires intact Fxr signaling and Fgf21 secretion in liver. (Gcgr = glucagon receptor glucagon; Fxr = farnesoid X receptor; Fgf21 = fibroblast growth factor-21) PMID: 29925501
we show that glucagon receptor (GCGR) inhibition with a monoclonal antibody normalized blood glucose and beta-hydroxybutyrate levels. Insulin receptor antagonism increased pancreatic beta-cell mass threefold. Normalization of blood glucose levels with GCGR-blocking antibody unexpectedly doubled beta-cell mass relative to that observed with S961 alone and 5.8-fold over control PMID: 28115707
These results show that Slc38a5 is a key component of the feedback circuit between glucagon receptor signaling in the liver and amino-acid-dependent regulation of pancreatic alpha cell mass in mice. PMID: 28591637
GcgR knockout (Gcgr(-/-)) mice displayed lower blood glucose levels accompanied by elevated plasma ghrelin levels. Hyperglycemia was averted in streptozocin treated Gcgr(-/-) mice and the plasma ghrelin level was further increased. PMID: 28487437
glucagon receptor antagonist improves glycemia in diet-induced obese angptl4 knockout mice without increasing glucagon levels or alpha-cell proliferation, underscoring the importance of this protein. PMID: 26621734
Data indicate that the exocrine pancreas in the glucagon receptor Gcgr-/- mice exhibited larger nuclear size than in WT or heterozygous controls, most obviously at old ages. PMID: 24326371
Simultaneous and sufficient activation of GLP1R is required to reduce GCCR mediated blood glucose elevation following administration of a GLP1R/GCGR co-agonist. PMID: 23203689
Knockdown of liver glucagon receptor in mice reduces blood glucose and increases blood LDL levels. PMID: 23828778
Gcgr(-/-) mice became lethargic & cachexic & died early. Autopsy revealed numerous PNETs up to 15 mm in diameter in most well-preserved Gcgr(-/-) pancreata. PMID: 22951296
Data suggest that GcgR activation raises hepatic expression of fibroblast growth factor 21 (FGF21) and increases circulating levels of FGF21; GcgR activation induces body weight loss and stimulates lipid metabolism. PMID: 23305646
These results suggest that a circulating factor generated after disruption of hepatic Gcgr signaling can increase alpha-cell proliferation independent of direct pancreatic input. PMID: 23160527
GRA1 is a potent glucagon receptor antagonist with strong antihyperglycemic efficacy in preclinical models and prominent effects on hepatic gene-expression related to amino acid metabolism PMID: 23185367
Data suggest that both Gcgr activity and glucagon-like peptide 1/Glp1r signal transduction in central nervous system are involved in control of interscapular brown adipose tissue thermogenesis. PMID: 22933116
A novel transgenic mouse was generated which had muscle specific expression of glucagon receptor. The transgenic mice maintained an appropriate ratio of glucagon to insulin, which appears important in maintaining glucose homeostasis. PMID: 22318544
in addition to activation of the classic cAMP/protein kinase A (PKA) pathway, activation of GCGR also induced beta-catenin stabilization and activated beta-catenin-mediated transcription PMID: 22438981
Data from glucagon receptor knockout mice suggest that glucagon receptor action and glucagon/glucagon receptor signaling contribute to normal female reproductive function (i.e., normal ovulation, placentation, and fetal development). PMID: 22167521
ChREBP directly regulates rat Gcgr expression in INS-1E cells. PMID: 22198437
Defective glucagon signaling causes pancreatic neuroendocrine tumors in the Gcgr(-/-) mice. PMID: 21853126
complete ablation of hepatic glucagon receptor function results in major metabolic alterations in the liver PMID: 21631939
functional plasticity in the enteroinsular axis involves GLP1R and GcgR and induction of compensatory mechanisms that control nutrient-dependent regulation of insulin secretion PMID: 21540554
Blocking glucagon action by knocking out glucagon receptors prevents type 1 diabetes mellitus in mice. PMID: 21270251
glucagon receptor has a role in maintenance of normal glycemia and postnatal regulation of islet and alpha and delta cell numbers PMID: 12552113
glucagon were unaffected by the GLP-1 receptor antagonist exendin-(9-39) but abolished by des-His1-[Glu9]-glucagon-amide, a specific blocker of the glucagon receptor PMID: 15459251
Glucagon signaling is required for normal beta-cell function and that insulin action is improved when disrupting the signal by glucagon receptor knockout. PMID: 17130493
Blocking glucagon signalling by targeted Gcgr gene deletion leads to an improvement in metabolic control in this mouse model of streptozotocin-mediated beta cell loss and hyperglycaemia. PMID: 17131145
Nestin expression is regulated by glucagon signaling. PMID: 17366624
Glucagon receptor has a role in islet function in mice with insulin resistance PMID: 17479245
Restoration of hepatic Gcgr expression in Gcgr-/- mice attenuated the development of hepatocellular injury. PMID: 18809404
Gcgr receptor is required for control of lipid metabolism during the adaptive metabolic response to fasting. PMID: 19046568
Oxyntomodulin, a glucagon receptor agonist, reverses obesity in diet-induced obese mice, and may be a novel therapeutic approach to the treatment of obesity. PMID: 19602537
Increased pancreatic beta-cell expression of the Gcgr increased insulin secretion, pancreatic insulin content, beta-cell mass, and, when mice were fed a HFD, partially protected against hyperglycemia and IGT. PMID: 19602585
These results suggest that GLP-1 may affect the maturation of postnatal but not prenatal beta cells. PMID: 19647035
hepatic energy state is sensitive to glucagon receptor activation and requires PEPCK-C, thus providing new insights into liver metabolism. PMID: 19662685

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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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