Analytical Data
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Gene name
PK2
- Application
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Alternative Names
PK2；KIAA1879；PC1L2；Polycystin-1-like Protein 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
Q7Z442
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Expression Region
全长
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AA Sequence
full
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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
PK2, or Protein Kinase 2, is a crucial enzyme involved in various cellular processes, including signal transduction and regulation of cellular growth and differentiation. Research into PK2 has gained momentum due to its implications in multiple diseases, particularly cancer, where its aberrant activity contributes to tumor progression and metastasis. The enzyme is part of a larger family of serine/threonine protein kinases, playing vital roles in phosphorylation and activation of specific substrates that influence cellular responses. Advances in recombinant DNA technology have enabled scientists to produce PK2 as a recombinant protein, allowing for detailed structural and functional analyses. This has facilitated the identification of novel inhibitors and therapeutic strategies targeting PK2 activity, with the potential to expand treatment options for cancer and other PK2-related pathologies. Additionally, studying PK2 in a recombinant form aids in understanding its interactions with other proteins and cellular components, shedding light on the underlying mechanisms of cellular signaling pathways. As such, PK2 is not only a subject of interest in basic research but also a promising candidate for drug development, emphasizing its significance in biomedical research and therapeutic innovation.
