Analytical Data
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Gene name
P2RY2
- Application
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Alternative Names
P2RY2；P2RU1；P2Y purinoceptor 2
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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
P41231
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Expression Region
1-377aa
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AA Sequence
MAADLGPWNDTINGTWDGDELGYRCRFNEDFKYVLLPVSYGVVCVPGLCLNAVALYIFLCRLKTWNASTTYMFHLAVSDALYAASLPLLVYYYARGDHWPFSTVLCKLVRFLFYTNLYCSILFLTCISVHRCLGVLRPLRSLRWGRARYARRVAGAVWVLVLACQAPVLYFVTTSARGGRVTCHDTSAPELFSRFVAYSSVMLGLLFAVPFAVILVCYVLMARRLLKPAYGTSGGLPRAKRKSVRTIAVVLAVFALCFLPFHVTRTLYYSFRSLDLSCHTLNAINMAYKVTRPLASANSCLDPVLYFLAGQRLVRFARDAKPPTGPSPATPARRRLGLRRSDRTDMQRIEDVLGSSEDSRRTESTPAGSENTKDIRL
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Molecular Weight
42.2 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
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Protein Description
P2RY2, a member of the purinergic receptor family, is a G protein-coupled receptor that primarily responds to extracellular nucleotides, particularly ATP. Research into P2RY2 has gained momentum due to its critical role in various physiological processes, including signal transduction, cell proliferation, and immune responses. Dysregulation of P2RY2 has been implicated in several pathological conditions, such as chronic pain, inflammation, and neurodegenerative diseases. The study of recombinant P2RY2 proteins has become essential for understanding the receptor's structure-function relationship, as well as its interactions with ligands and downstream signaling pathways. By producing P2RY2 in a recombinant system, researchers can investigate the receptor's pharmacological properties, explore its potential as a therapeutic target, and elucidate the mechanisms underlying its involvement in cellular processes. Advances in structural biology techniques, such as cryo-electron microscopy and X-ray crystallography, have further enhanced our understanding of P2RY2, paving the way for the development of selective modulators that could improve treatment strategies for diseases associated with this receptor. Ultimately, the study of recombinant P2RY2 proteins not only provides insights into its biological role but also contributes to the broader field of purinergic signaling and its implications in health and disease.
