Analytical Data
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Gene name
PHS
- Application
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Alternative Names
4-alpha-hydroxy-tetrahydropterin dehydrataseDimerization cofactor of hepatocyte nuclear factor 1-alpha ;DCoH ;Dimerization cofactor of HNF1;Phenylalanine hydroxylase-stimulating protein;Pterin carbinolamine dehydratase ;PCD
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Species
Human
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Source
Yeast
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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
P61457
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Expression Region
2-104aa
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Molecular Weight
13.9 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
PHS (Phosphohexose Isomerase) is an enzyme that plays a critical role in the metabolic pathway of glycolysis and gluconeogenesis, catalyzing the interconversion of glucose-6-phosphate and fructose-6-phosphate. The study of PHS, particularly its recombinant proteins, has gained significant attention due to its implications in various biological processes and potential applications in biotechnology and medicine. Recombinant PHS can be produced using recombinant DNA technology, allowing researchers to obtain large quantities of the enzyme for detailed biochemical studies. Understanding the structure and function of PHS is crucial, as it is linked to cellular metabolism and energy production. Additionally, alterations in PHS activity have been associated with various diseases, including certain cancers and metabolic disorders. By characterizing the recombinant form of this enzyme, researchers aim to elucidate its mechanisms, investigate its role in metabolic diseases, and explore its potential as a therapeutic target. The recombinant production of PHS also opens avenues for industrial applications, such as in the production of biofuels and other bioproducts, highlighting its importance in both fundamental and applied sciences. As research progresses, the insights gained from PHS recombinant proteins have the potential to revolutionize our understanding of metabolic regulation and lead to novel therapeutic strategies.
