Analytical Data
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Gene name
STK16
- Application
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Alternative Names
Myristoylated and palmitoylated serine/threonine-protein kinase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O75716
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Expression Region
1-305aa
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Molecular Weight
61.5 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
STK16, a member of the Serine/Threonine Kinase family, has garnered significant attention in recent years due to its potential roles in various cellular processes, including cell growth, differentiation, and apoptosis. This kinase is primarily localized in the Golgi apparatus, implicating its involvement in intracellular signaling pathways and protein trafficking. Emerging research suggests that STK16 may play a crucial role in the regulation of glucose metabolism and has been linked to the pathophysiology of several diseases, particularly metabolic disorders and cancer. Its aberrant expression has been associated with tumorigenesis, underscoring the need for a deeper understanding of its molecular mechanisms. By utilizing recombinant protein technology, researchers aim to study STK16's structure and function in detail, enabling them to identify its substrates and interacting partners. This could reveal new therapeutic targets and contribute to the development of strategies for disease intervention. Understanding STK16’s functionality may also shed light on the broader role of serine/threonine kinases in health and disease, providing insights into their potential as drug targets in the treatment of various conditions. Overall, the investigation of STK16 as a recombinant protein stands to enhance our understanding of its biological significance and therapeutic potential.
