Analytical Data
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Gene name
P2RX5
- Application
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Alternative Names
P2X5; P2X5R; P2X Purinoceptor 5; ATP receptor; Purinergic receptor
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Species
Human
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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
Q93086
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Expression Region
Lys52~Arg319
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Molecular Weight
34kDa
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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
P2RX5, or purinergic receptor P2X5, is a member of the P2X family of receptors that are ion channels activated by ATP. Research on P2RX5 is significant because it plays a crucial role in various physiological and pathological processes, including neuronal signaling, immune response, and pain perception. Abnormal functioning of P2RX5 has been implicated in several diseases, including cancer and chronic pain disorders. The recombinant protein of P2RX5 offers a valuable tool for molecular studies, allowing researchers to investigate its structure-function relationships, pharmacological properties, and interactions with other cellular components. Furthermore, the availability of purified P2RX5 protein facilitates the development of potential therapeutic agents that can modulate its activity, providing insights into novel treatment strategies for diseases associated with dysregulated purinergic signaling. By generating and studying recombinant P2RX5, scientists aim to enhance the understanding of purinergic mechanisms and identify pathways that might be targeted for therapeutic intervention, thereby opening new avenues in drug discovery and development aimed at addressing disorders linked to this receptor.
