Analytical Data
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Gene name
FN3K
- Application
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Alternative Names
FN3K;Fructosamine-3-kinase
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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
Q9H479
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Expression Region
1-309aa
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AA Sequence
MGSSHHHHHH SSGLVPRGSH MGSMEQLLRA ELRTATLRAF GGPGAGCISE GRAYDTDAGP VFVKVNRRTQ ARQMFEGEVA SLEALRSTGL VRVPRPMKVI DLPGGGAAFV MEHLKMKSLS SQASKLGEQM ADLHLYNQKL REKLKEEENT VGRRGEGAEP QYVDKFGFHT VTCCGFIPQV NEWQDDWPTF FARHRLQAQL DLIEKDYADR EARELWSRLQ VKIPDLFCGL EIVPALLHGD LWSGNVAEDD VGPIIYDPAS FYGHSEFELA IALMFGGFPR SFFTAYHRKI PKAPGFDQRL LLYQLFNYLN HWNHFGREYR SPSLGTMRRL LK
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Molecular Weight
37 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
FN3K (fructosamine-3-kinase) is an enzyme that plays a crucial role in the metabolism of advanced glycation end-products (AGEs), which are formed when sugars react with proteins and lipids. This process is particularly relevant in the context of diabetes, where elevated levels of fructosamine can indicate poor glycemic control and increased risk of complications. Research on FN3K has gained momentum due to its potential implications in diseases associated with chronic hyperglycemia, such as diabetic neuropathy and retinopathy. The enzyme functions by phosphorylating fructosamine, a stable marker of glycemic exposure, thereby facilitating its degradation and modulating the accumulation of AGEs. Understanding the structure and function of FN3K through biochemical and structural biology techniques is essential for elucidating its biological significance and therapeutic potential. Additionally, FN3K's involvement in oxidative stress and cellular signaling pathways presents opportunities for novel interventions in managing diabetes-related complications. As a result, the study of FN3K not only contributes to our understanding of metabolic disorders but also raises the potential for developing therapeutic strategies aimed at targeting glycation-related changes in various diseases. The recombinant form of FN3K has opened up avenues for in-depth functional studies and drug development, highlighting the significance of this enzyme in both fundamental research and clinical applications.
