Recombinant Human Glucagon Receptor (GCGR) Protein (His&My/His/Tag-Free)

Name: Recombinant Human Glucagon Receptor (GCGR) Protein (His&My/His/Tag-Free)
Brand: Beta LifeScience
SKU: BLC-04954P
Price: 349.0 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Other recombinant proteins, Recombinant proteins, Recombinant proteins holiday sale

Price Save $1,055

Size

100ug

Submit an inquiry or email sales for a custom bulk quote. Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Description	Recombinant Human Glucagon Receptor (GCGR) Protein (His&My/His/Tag-Free) is produced by our Baculovirus expression system. This is a protein fragment.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	P47871
Target Symbol	GCGR
Synonyms	GCGR; Glucagon receptor; GL-R
Species	Homo sapiens (Human)
Expression System	Baculovirus
Tag	N-His&C-Myc/N-His/Tag-Free
Protein Length	Partial
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.
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	HGNC: 4192 OMIM: 138033 KEGG: hsa:2642 STRING: 9606.ENSP00000383558 UniGene: Hs.208

Gene Functions References

3.0 A-resolution crystal structure of the full-length human glucagon receptor (GCGR) in complex with a glucagon analogue and partial agonist, NNC1702 PMID: 29300013
work toward the mapping of interactions between the polypeptide hormone glucagon and the glucagon receptor PMID: 28508109
3.0 A crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation PMID: 28514451
This work suggests that RAMP2 may modify the agonist activity and trafficking of the GCGR, with potential relevance to production of new peptide analogs with selective agonist activities. PMID: 28586439
Data suggest that GCGR activation proceeds via a mechanism in which transmembrane helix 6 (TM6) is held in an inactive conformation by a conserved polar core and a hydrophobic lock (involving intracellular loop 3, IC3); mutations in the corresponding polar core of GCGR disrupt these inhibitory elements, allow TM6 to swing outward, and induce constitutive G protein signaling. PMID: 28356352
The activation of the GCGR is characterized by the outward movement of the intracellular side of helix VI. In the active state of the GCGR, the Arg173(2.46)-Ser350(6.41) and Glu245(3.50)-Thr351(6.42) hydrogen bonds break, and the chi1 rotamer of Phe322(5.54) changes from perpendicular to parallel to helix VI. PMID: 27094704
In the glucagon receptor (GCGR) and glucagon-like peptide-1 receptor (GLP-1R), the extracellular domain is required for signaling even when the hormone is covalently linked to the transmembrane domain. PMID: 27226600
2.5 A crystal structure of human GCGR in complex with the antagonist MK-0893, which is found to bind to an allosteric site outside the seven transmembrane helical bundle in a position between TM6 and TM7 extending into the lipid bilayer PMID: 27111510
Molecular dynamics and disulfide crosslinking studies suggest that apo-GCGR can adopt both an open and closed conformation associated with extensive contacts between the ECD and 7TM domain. Glucagon binds to GCGR by a conformational selection mechanism. PMID: 26227798
glucagon cell adenomatosis with GCGR germline mutations seems to follow an autosomal-recessive trait. PMID: 25695890
Using a real-time time-resolved FRET-based internalization assay, we show that GLP-1R, GIPR, and GCGR internalize with differential properties PMID: 25451942
crystal structure of the seven transmembrane helical domain of human GCGR at 3.4 A resolution, and a hybrid model of glucagon bound to GCGR to understand the molecular recognition of the receptor for its native ligand PMID: 23863937
Letter/Case Report: nonfunctional glucagon cell adenomatosis with no detectable glucagon receptor mutations. PMID: 23407487
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
F22, V23, M27, and D15 of GCGR are the most important residues for glucagon binding. PMID: 22893257
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
analysis of glucagon receptor antagonists with reduced molecular weight and lipophilicity PMID: 22119466
The P86S mutant GCGR shows abnormal receptor internalization & calcium mobilization, & causes apoptosis. It cases Mahvash disease (hyperglucagonemia, hypoglycemia, pancreatic neuroendocrine tumors). PMID: 21680267
substituted cysteine accessibility method and 3D-molecular modeling to study the N-terminal domain; results showed that Asp(63), Arg(116), and Lys(98) are essential for the receptor structure and/or ligand binding PMID: 20647307
The [Ca2+] response is induced by glucagon mainly via the coupling of GCGR to the Galphaq/11 and Galphai/o proteins. PMID: 19903011
The Gly40Ser polymorphism of the GCGR gene is associated with higher risk of hypertension and with enhanced proximal tubular sodium reabsorption. PMID: 11692154
Gly40Ser mutation in the glucagon receptor gene is not associated with type 2 diabetes in a Brazilian population, but a reduction of insulin secretion was observed in Gly40Ser carriers. PMID: 11961492
Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus PMID: 12724331
Expression of peroxisome proliferator-activated receptor gamma coactivator 1alpha (PGC-1alpha), known to be upregulated in the liver by fasting, was found to abolish the cAMP-dependent downregulation of glucagon receptor mRNA expression in vitro. PMID: 17374560

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.