Analytical Data
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Gene name
P2yr13
- Application
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Alternative Names
(P2Y13)(G-protein coupled receptor 86)
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Species
Mouse
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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
Q9D8I2
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Expression Region
1-377aa
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Molecular Weight
44.8 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
P2yr13 is a member of the P2Y family of purinergic receptors, which are G-protein-coupled receptors (GPCRs) that play crucial roles in various physiological processes by responding to extracellular nucleotides, such as ATP and ADP. These receptors are involved in numerous signaling pathways that regulate cardiovascular functions, immune responses, and neurotransmission. Research on P2yr13 specifically has garnered increasing interest due to its potential implications in various diseases, including inflammation, cancer, and cardiovascular disorders. Understanding the structural and functional characteristics of P2yr13 is essential for elucidating its role in these pathological conditions. Recombinant expression of P2yr13 allows for advanced studies on its pharmacology and signaling mechanisms, facilitating the identification of potential therapeutic targets. Current studies focus on characterizing the receptor's ligand-binding properties, its activation mechanisms, and downstream signaling pathways. The exploration of P2yr13 also aims to identify small molecule modulators that can selectively target this receptor, providing insights into developing novel treatments for diseases associated with purinergic signaling dysregulation. As research progresses, the recombinant protein's utility in drug discovery and therapeutic applications will significantly enhance our understanding of purinergic signaling mechanisms and their contributions to health and disease.
