Analytical Data
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Gene name
GCGR
- Application
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Alternative Names
GCGR;Glucagon receptor
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P47871
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Expression Region
26-136aa
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AA Sequence
AQVMDFLFEKWKLYGDQCHHNLSLLPPPTELVCNRTFDKYSCWPDTPANT TANISCPWYLPWHHKVQHRFVFKRCGPDGQWVRGPRGQPWRDASQCQMDG EEIEVQKEVAK
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Molecular Weight
54 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Glucagon receptor (GCGR) is a key player in glucose metabolism and is primarily involved in regulating glucose levels in the blood. Its role in the pathophysiology of diabetes and related metabolic disorders has sparked significant scientific interest. GCGR is a member of the class B G-protein coupled receptor family, and its activation by glucagon leads to an increase in hepatic glucose production, which is critical for maintaining energy homeostasis. Therefore, understanding the structure and function of GCGR is essential for developing therapeutic strategies targeting diabetes and hypoglycemia. Recent advancements in recombinant protein technology have facilitated the production of GCGR in heterologous systems, enabling detailed studies of its biochemical properties, ligand-binding dynamics, and signaling pathways. This research is crucial for elucidating GCGR's role in glucose regulation and for the discovery of novel medications that can modulate its activity to improve glycemic control in diabetic patients. Furthermore, characterized GCGR recombinant proteins serve as vital tools in drug development, aiding in the design of analogs and antagonists that could potentially lead to innovative treatments for metabolic diseases. Overall, the exploration of GCGR’s structural biology and signaling mechanisms continues to be a prominent focus within metabolic research, promising to yield significant insights into new therapeutic avenues.











