Analytical Data
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Gene name
Glucose-6-phosphate isomerase
- Application
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Alternative Names
AMF; NLK; PHI; SA36; Phosphoglucose Isomerase; Autocrine motility factor; Neuroleukin; Phosphohexose isomerase; Sperm antigen 36
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Species
Rat
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q6P6V0
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Expression Region
Thr335~Asp558
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Molecular Weight
29kDa
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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
Glucose-6-phosphate isomerase (GPI), also known as phosphoglucose isomerase, is an enzyme that plays a crucial role in the glycolytic and gluconeogenic pathways by catalyzing the reversible conversion of glucose-6-phosphate to fructose-6-phosphate. This enzyme not only participates in carbohydrate metabolism but also has functions beyond metabolism, including involvement in cellular signaling, tumor progression, and inflammation. Its significance in health and disease has driven the demand for detailed studies of its structure and function. Recombinant GPI proteins are essential for investigating its biochemical properties, understanding its regulatory mechanisms, and exploring its potential as a therapeutic target. Advances in molecular cloning and expression techniques have facilitated the production of high-purity recombinant GPI, allowing for extensive biochemical characterization, including enzymatic activity assays, structural studies via X-ray crystallography, and binding affinity analyses. Research into GPI also extends to its role in various diseases, such as cancer, where altered GPI expression may influence tumor growth and metastasis. Consequently, recombinant GPI is not only a valuable tool for fundamental research in enzymology and metabolic pathways but also a promising avenue for developing targeted therapies, making its study highly relevant in both basic and applied life sciences.
