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anti-Human Glucagon Receptor Antikörper:
anti-Mouse (Murine) Glucagon Receptor Antikörper:
anti-Rat (Rattus) Glucagon Receptor Antikörper:
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Human Polyclonal Glucagon Receptor Primary Antibody für IHC (p) - ABIN271047
Mighiu, Yue, Filippi, Abraham, Chari, Lam, Yang, Christian, Charron, Lam: Hypothalamic glucagon signaling inhibits hepatic glucose production. in Nature medicine 2013
Show all 2 Pubmed References
Human Polyclonal Glucagon Receptor Primary Antibody für ELISA - ABIN314296
Sørensen, Winzell, Brand, Fosgerau, Gelling, Nishimura, Ahren: Glucagon receptor knockout mice display increased insulin sensitivity and impaired beta-cell function. in Diabetes 2006
Human Polyclonal Glucagon Receptor Primary Antibody für IF (p), IHC (p) - ABIN751528
Rafacho, Gonçalves-Neto, Santos-Silva, Alonso-Magdalena, Merino, Taboga, Carneiro, Boschero, Nadal, Quesada: Pancreatic alpha-cell dysfunction contributes to the disruption of glucose homeostasis and compensatory insulin hypersecretion in glucocorticoid-treated rats. in PLoS ONE 2014
3.0 A-resolution crystal structure of the full-length human glucagon receptor (GCGR) in complex with a glucagon analogue and partial agonist, NNC1702
work toward the mapping of interactions between the polypeptide hormone glucagon and the glucagon receptor
3.0 A crystal structure of full-length GCGR containing both the extracellular domain and transmembrane domain in an inactive conformation
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.
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.
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.
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.
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
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.
glucagon cell adenomatosis with GCGR germline mutations seems to follow an autosomal-recessive trait.
Using a real-time time-resolved FRET-based internalization assay, we show that GLP-1R, GIPR, and GCGR internalize with differential properties
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
Letter/Case Report: nonfunctional glucagon cell adenomatosis with no detectable glucagon receptor mutations.
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
F22, V23, M27, and D15 of GCGR are the most important residues for glucagon binding.
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
analysis of glucagon receptor antagonists with reduced molecular weight and lipophilicity
The P86S mutant GCGR shows abnormal receptor internalization & calcium mobilization, & causes apoptosis. It cases Mahvash disease (hyperglucagonemia, hypoglycemia, pancreatic neuroendocrine tumors).
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
The [Ca2+] response is induced by glucagon mainly via the coupling of GCGR to the Galphaq/11 and Galphai/o proteins.
Apart from their hyperaminoacidemia, Gcgr(-/-) mice display hyperglucagonemia, increased pancreatic content of glucagon and somatostatin (but not insulin), and alpha-cell hyperplasia and hypertrophy compared with WT littermates.
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)
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
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.
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.
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.
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.
Simultaneous and sufficient activation of GLP1R is required to reduce GCCR mediated blood glucose elevation following administration of a GLP1R/GCGR co-agonist.
Knockdown of liver glucagon receptor in mice reduces blood glucose and increases blood LDL levels.
Gcgr(-/-) mice became lethargic & cachexic & died early. Autopsy revealed numerous PNETs up to 15 mm in diameter in most well-preserved Gcgr(-/-) pancreata.
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.
These results suggest that a circulating factor generated after disruption of hepatic Gcgr signaling can increase alpha-cell proliferation independent of direct pancreatic input.
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.
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.
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).
ChREBP directly regulates rat Gcgr expression in INS-1E cells.
Defective glucagon signaling causes pancreatic neuroendocrine tumors in the Gcgr(-/-) mice.
complete ablation of hepatic glucagon receptor function results in major metabolic alterations in the liver
The protein encoded by this gene is a glucagon receptor that is important in controlling blood glucose levels. Defects in this gene are a cause of non-insulin-dependent diabetes mellitus (NIDDM).
, glucagon receptor-like
, glucagon receptor perhaps same as Niddm3