Analytical Data
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Gene name
PHGDH
- Application
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Alternative Names
/
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O43175
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Expression Region
2-251aa
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Molecular Weight
53.8 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
PHGDH (Phosphoglycerate Dehydrogenase) is an essential enzyme involved in the serine biosynthetic pathway, converting 3-phosphoglycerate to 3-phosphoserine, a precursor for the amino acid serine. Research on PHGDH has gained significant attention due to its pivotal role in cancer metabolism, particularly in numerous malignancies where it is often found to be overexpressed. Elevated levels of serine have been shown to support rapid cell proliferation and tumor growth, making PHGDH a potential target for therapeutic intervention. Additionally, PHGDH has been implicated in neurodevelopmental disorders and other metabolic diseases, further underscoring its biological importance. The generation of recombinant PHGDH proteins through methods such as heterologous expression in microbial systems allows for extensive biochemical characterization, structure-function studies, and potential drug discovery efforts aimed at modulating its activity. Overall, the investigation of PHGDH and its recombinant proteins represents a promising avenue for understanding metabolic regulation in health and disease, as well as for developing novel therapeutic strategies targeting cancer and other disorders linked to altered serine metabolism.
