Analytical Data
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Gene name
IP6K1
- Application
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Alternative Names
Inositol hexaphosphate kinase 1
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92551
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Expression Region
1-441aa
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Molecular Weight
66.2 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
IP6K1, or Inositol Hexaphosphate Kinase 1, is an enzyme that plays a critical role in cellular signaling and metabolism by phosphorylating inositol phosphates. Its significance has gained attention due to its involvement in various biological processes, including cell growth, differentiation, and apoptosis. Recent studies have indicated that IP6K1 may influence cancer progression and metabolic disorders, making it a potential target for therapeutic intervention. The enzyme is known to regulate the levels of inositol pyrophosphates, which are important mediators in energy homeostasis and cellular stress responses. Understanding the structural and functional properties of IP6K1, especially through recombinant protein studies, is essential for elucidating its mechanisms of action and potential involvement in disease. Research has focused on generating recombinant IP6K1 to explore its enzymatic activity, interaction with other cellular proteins, and regulation by various metabolic pathways. By dissecting the roles of this kinase, researchers aim to develop targeted therapies that modulate its activity, providing insights into novel treatment strategies for related diseases. Overall, the study of recombinant IP6K1 represents a promising avenue for advancing our knowledge of cellular signaling networks and their implications in health and disease.
