Analytical Data
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Gene name
PRKX
- Application
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Alternative Names
PRKX；PKX1；cAMP-dependent Protein kinase catalytic subunit PRKX
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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
P51817
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Expression Region
1-358aa
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AA Sequence
MEAPGLAQAA AAESDSRKVA EETPDGAPAL CPSPEALSPE PPVYSLQDFD TLATVGTGTF GRVHLVKEKT AKHFFALKVM SIPDVIRLKQ EQHVHNEKSV LKEVSHPFLI RLFWTWHDER FLYMLMEYVP GGELFSYLRN RGRFSSTTGL FYSAEIICAI EYLHSKEIVY RDLKPENILL DRDGHIKLTD FGFAKKLVDR TWTLCGTPEY LAPEVIQSKG HGRAVDWWAL GILIFEMLSG FPPFFDDNPF GIYQKILAGK IDFPRHLDFH VKDLIKKLLV VDRTRRLGNM KNGANDVKHH RWFRSVDWEA VPQRKLKPPI VPKIAGDGDT SNFETYPEND WDTAAPVPQK DLEIFKNF
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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
PRKX (Protein Kinase X) is a member of the protein kinase family, which plays critical roles in cellular signaling processes. Its involvement in regulating various physiological functions has garnered considerable interest within the scientific community. Research has shown that PRKX is implicated in several cellular processes, including cell proliferation, differentiation, and apoptosis. Dysregulation of PRKX has been linked to various pathological conditions, including cancer, making it a potential target for therapeutic intervention. The study of PRKX recombinant protein has become essential for understanding its biochemical properties and functional mechanisms. By expressing and purifying PRKX in recombinant systems, researchers can investigate the protein's enzymatic activity, identify its substrates, and explore its interaction with other signaling molecules. These insights are crucial for unraveling the complex signaling pathways in which PRKX is involved and could lead to the development of novel strategies for treating diseases associated with PRKX dysregulation. As such, ongoing research on PRKX recombinant protein not only enhances our theoretical understanding of protein kinases but also paves the way for potential clinical applications.
