Analytical Data
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Gene name
PRKY
- Application
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Alternative Names
PRKY; Putative serine/threonine-protein kinase PRKY; EC 2.7.11.1
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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
O43930
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Expression Region
1-277 aa
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AA Sequence
MEAPGPAQAA AAESNSREVT EDAADWAPAL CPSPEARSPE APAYRLQDCD ALVTMGTGTF GRVHLVKEKT AKHFFALKVM SIPDVIRRKQ EQHVHNEKSV LKEVSHPFLI RLFWTWHEER FLYMLMEYVP GGELFSYLRN RGHFSSTTGL FYSAEIICAI EYLHSKEIVY RDLKPENILL DRDGHIKLTD FGFAKKLVDR TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG FPPFFDDNPF GIYQKILAGK LYFPRHLDFH VKTGRMM
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Molecular Weight
31.7 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
PRKY (Protein kinase, cAMP-dependent, regulatory, type II, alpha) is a serine/threonine kinase that plays a crucial role in cellular signaling pathways, particularly those mediated by cyclic AMP (cAMP). Understanding the structure and function of PRKY is essential for elucidating its involvement in various physiological processes, including metabolism, cell growth, and differentiation. Research has shown that PRKY is implicated in several diseases, including metabolic disorders and cancers, making it a significant target for therapeutic intervention. The ability to produce recombinant PRKY proteins allows researchers to study its biochemical properties, functional mechanisms, and interactions with other cellular components in a controlled environment. Recombinant PRKY can be used to investigate its role in signal transduction, kinase activity, and its impact on downstream targets. Additionally, insights gained from PRKY studies could contribute to the development of novel interventions in diseases associated with its dysregulation. Thus, research on recombinant PRKY proteins is pivotal for advancing our understanding of cAMP-related signaling mechanisms and their implications in health and disease.
