Analytical Data
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Gene name
GLRa2
- Application
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Alternative Names
GLR
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P22771
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Expression Region
Lys28~Gln253
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Molecular Weight
30kDa
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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
GLRa2, or Glucagon-Like Receptor 2, is a G protein-coupled receptor primarily involved in regulating glucose metabolism, insulin secretion, and energy homeostasis. Research into GLRa2, particularly its recombinant proteins, has gained significant momentum due to its potential implications in treating metabolic disorders such as type 2 diabetes and obesity. Understanding the structure and function of GLRa2 can unravel its role in glucose signaling pathways and may lead to the development of novel therapeutic agents that target this receptor. Moreover, recombinant GLRa2 proteins allow for detailed studies of ligand-receptor interactions, receptor activation, and downstream signaling cascades. By employing techniques such as protein engineering and expression in suitable host systems, researchers can produce functional GLRa2 proteins in sufficient quantities for biochemical and biophysical analyses. These studies are crucial as they provide insights into the pharmacological modulation of GLRa2, guiding the design of selective agonists or antagonists. Furthermore, understanding the receptor's conformational dynamics presents opportunities for structure-based drug design. The investigation of GLRa2 recombinant proteins thus remains a focal point in biomedical research, as it holds promise not only for enhancing our comprehension of glucagon-like signaling but also for informing the development of targeted therapies for metabolic diseases.
