Analytical Data
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Gene name
FN3K
- Application
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H479
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Expression Region
Met1~Lys309
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Molecular Weight
40kDa
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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
FN3K (Fructosamine-3-kinase) is an important enzyme involved in the metabolism of glycated proteins, playing a crucial role in the body's response to chronic hyperglycemia. The enzyme catalyzes the phosphorylation of fructosamine, a compound formed when glucose reacts with proteins, thereby preventing the non-enzymatic glycation of proteins and potentially reducing the complications associated with diabetes. Research on FN3K has gained traction due to its promising therapeutic implications in managing diabetes-related disorders. Elevated levels of fructosamine are associated with the development of diabetic complications, including neuropathy and retinopathy. Understanding the biochemical mechanisms of FN3K and its regulatory pathways can provide insights into novel treatment strategies to mitigate these complications. Additionally, FN3K's involvement in glucose metabolism suggests its potential as a biomarker for glycemic control and a target for drug development. Recent studies have demonstrated that the modulation of FN3K activity can influence the levels of glycated proteins, making it a candidate for therapeutic intervention. Researchers are now focusing on the structural characterization of FN3K, the identification of its inhibitors, and its role in the metabolic dysfunction associated with diabetes. The ongoing exploration of FN3K not only enhances our understanding of protein glycation and its consequences but also paves the way for innovative approaches in diabetes management and related metabolic diseases.
