Analytical Data
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Gene name
PSAT1
- Application
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Alternative Names
Endometrial progesterone-induced protein Short name: EPIP Phosphohydroxythreonine aminotransferase
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Species
Mouse
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q99K85
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Expression Region
1-370aa
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Molecular Weight
56.5 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
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Protein Description
The PSAT1 protein, or Phosphoserine Aminotransferase 1, plays a crucial role in the serine biosynthesis pathway, which is essential for various cellular processes, including amino acid metabolism and cell proliferation. Research has highlighted its involvement in cancer biology, where altered serine metabolism is linked to tumor growth and survival. Elevated PSAT1 levels have been observed in several cancer types, suggesting that it may serve as a potential biomarker for cancer diagnosis and prognosis. Moreover, targeting PSAT1 may offer therapeutic opportunities, as inhibiting its activity can disrupt the serine supply to cancer cells, leading to impaired growth. Understanding the structure and function of PSAT1 at the molecular level is vital for developing targeted strategies against malignant tumors. Recent studies utilizing recombinant PSAT1 have focused on elucidating its enzymatic properties and regulatory mechanisms, providing insights into its role in metabolic reprogramming in cancer. The growing interest in PSAT1 not only sheds light on its biological significance but also paves the way for novel interventions in cancer treatment, making it a key focus in the field of cancer metabolism research.
