Analytical Data
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Gene name
PHGDH
- Application
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Alternative Names
PHGDH；PGDH3；D-3-phosphoglycerate dehydrogenase
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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
O43175
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Expression Region
2-251aa
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AA Sequence
AFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQS
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Molecular Weight
54.3 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 a key enzyme in the serine biosynthesis pathway, facilitating the conversion of 3-phosphoglycerate to phosphoserine. Its role in cellular metabolism has garnered increasing attention, particularly due to its implications in various physiological and pathological conditions, including cancer, where elevated PHGDH expression has been linked to tumor growth and progression. Research indicates that cancer cells often reprogram their metabolic pathways to support rapid proliferation, with serine and glycine serving as crucial building blocks for macromolecules and precursors for various biosynthetic pathways. In this context, PHGDH has emerged as a potential therapeutic target, as inhibiting its activity can impair tumor growth and induce cell death in certain cancer types. Moreover, understanding the structure and function of recombinant PHGDH proteins allows researchers to delineate the nuanced biochemical mechanisms underlying its enzymatic activity and regulatory roles. This investigation not only contributes to the fundamental understanding of metabolic regulation but also holds promise for the development of novel cancer treatments, making recombinant PHGDH an important subject of study in both basic and applied biomedical research.
