Analytical Data
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Gene name
PK
- Application
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Alternative Names
PK；PIP1；WDR84；p21-activated Protein kinase-interacting Protein 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
Q9NWT1
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Expression Region
1-392aa
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AA Sequence
MELVAGCYEQVLFGFAVHPEPEACGDHEQWTLVADFTHHAHTASLSAVAVNSRFVVTGSKDETIHIYDMKKKIEHGALVHHSGTITCLKFYGNRHLISGAEDGLICIWDAKKWECLKSIKAHKGQVTFLSIHPSGKLALSVGTDKTLRTWNLVEGRSAFIKNIKQNAHIVEWSPRGEQYVVIIQNKIDIYQLDTASISGTITNEKRISSVKFLSESVLAVAGDEEVIRFFDCDSLVCLCEFKAHENRVKDMFSFEIPEHHVIVSASSDGFIKMWKLKQDKKVPPSLLCEINTNARLTCLGVWLDKVADMKESLPPAAEPSPVSKEQSKIGKKEPGDTVHKEEKRSKPNTKKRGLTGDSKKATKESGLISTKKRKMVEMLEKKRKKKKIKTMQ
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Molecular Weight
43.9 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
PK (protein kinase) recombinant proteins have gained significant attention in the field of molecular biology and biochemistry due to their critical roles in cellular signaling pathways that regulate various physiological processes, including cell growth, differentiation, and metabolism. Protein kinases are enzymes that catalyze the phosphorylation of specific target proteins, thereby modifying their activity, localization, or interactions with other biomolecules. The dysregulation of kinase activity is often linked to various diseases, including cancer, diabetes, and neurodegenerative disorders, making them important targets for therapeutic intervention. Researchers have developed recombinant protein technologies to produce these enzymes in a controlled manner, facilitating the study of their structure, function, and regulatory mechanisms. By utilizing techniques such as cloning, expression in host systems (e.g., bacteria, yeast, or mammalian cells), and purification methods, scientists can obtain large quantities of biologically active PKs. This enables the exploration of their enzymatic properties, identification of substrates, and investigation of their roles in signaling cascades. Advances in recombinant protein technologies also promote the development of kinase inhibitors and other drugs that may offer novel treatment strategies for kinase-related diseases. Therefore, the study of PK recombinant proteins is essential for understanding cellular processes and developing targeted therapeutic approaches in various biomedical fields.
