Analytical Data
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Gene name
SIK3
- Application
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Alternative Names
SIK3; KIAA0999; QSK; L19Serine/threonine-protein kinase SIK3; EC 2.7.11.1; Salt-inducible kinase 3; SIK-3; Serine/threonine-protein kinase QSK
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9Y2K2
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Expression Region
1262-1371 aa
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AA Sequence
LQRHHTIQNSDDAYVQLDNLPGMSLVAGKALSSARMSDAVLSQSSLMGSQQFQDGENEECGASLGGHEHPDLSDGSQHLNSSCYPSTCITDILLSYKHPEVSFSMEQAGV
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Molecular Weight
37.51 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
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Protein Description
The study of the SIK3 (Salt-Inducible Kinase 3) recombinant protein is rooted in its significant role in various cellular processes, including metabolism, cell proliferation, and stress responses. SIK3 is a member of the AMP-activated protein kinase (AMPK) family, which regulates energy homeostasis and plays a crucial role in the oxidative stress response. Its dysregulation has been linked to various diseases, including cancer, obesity, and diabetes. As a serine/threonine kinase, SIK3 phosphorylates multiple substrates, influencing diverse signaling pathways. Given its pivotal functions, understanding SIK3's molecular mechanisms can provide insights into potential therapeutic targets for metabolic disorders and malignancies. The recombinant expression of SIK3 offers an invaluable tool for studying its enzymatic activities, interaction with substrates, and regulatory mechanisms. By producing this protein in a controlled environment, researchers can conduct detailed biochemical assays and investigate its structural properties, enabling the identification of small-molecule inhibitors or activators. Such advancements could pave the way for novel treatment strategies, contributing to better management of diseases associated with abnormal SIK3 activity. Thus, the ongoing research into SIK3 recombinant protein is not only vital for elucidating its biological roles but also for exploring its therapeutic potential, with implications that extend into various biomedical fields.
