Analytical Data
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Gene name
GFPT2
- Application
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Alternative Names
GFAT2; Glutamine Fructose 6-Phosphate Aminotransferase 2; Hexosephosphate aminotransferase 2; D-fructose-6-phosphate amidotransferase 2
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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
O94808
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Expression Region
Cys2~Gly288
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Molecular Weight
36kDa
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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
GFPT2, or Glutamine Fructose-6-Phosphate Transaminase 2, is an enzyme that plays a pivotal role in the hexosamine biosynthetic pathway, which is crucial for the production of uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), a key building block for glycoproteins and glycolipids. Research has highlighted the importance of GFPT2 in cellular processes, particularly in cancer biology, as its overexpression has been linked to tumor progression and metastasis. Moreover, GFPT2 is believed to influence cellular signaling pathways, including those related to insulin resistance and metabolic disorders. Understanding the function and regulatory mechanisms of GFPT2 is critical for uncovering its potential as a therapeutic target. The recombinant protein production of GFPT2 enables detailed structural and functional analyses, allowing researchers to investigate its enzymatic activity, substrate specificity, and interaction with other cellular molecules. These studies are vital for developing strategies to modulate GFPT2 activity, providing insights into its role in disease and offering avenues for novel therapeutic interventions. Overall, GFPT2 represents a significant focus of research within the fields of biochemistry, cell biology, and oncology, underlining its relevance in health and disease.
