Analytical Data
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Gene name
TALDO1
- Application
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Alternative Names
Dihydroxyacetone transferase; EC 2.2.1.2; EPS8L2 ; Glycerone transferase ; TAL; TAL H; TALDO; TALDO_HUMAN; TALDO1; TALDOR ; TALH ; Transaldolase 1; Transaldolase
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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
P37837
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Expression Region
9-337aa
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Molecular Weight
63.7 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
TALDO1, or Transaldolase 1, is a crucial enzyme in the pentose phosphate pathway, which plays a significant role in cellular metabolism and redox balance. It facilitates the transfer of carbohydrates among sugars, contributing to the synthesis of nucleotides and nucleic acids, as well as to the generation of reducing equivalents in the form of NADPH. Dysregulation of TALDO1 is implicated in several metabolic disorders and diseases, including diabetes and cancer, highlighting the importance of understanding its biological function and regulation. Recent studies have shown that the enzyme's activity not only impacts metabolic flux but also influences cellular responses to stress and proliferation. Given its potential as a therapeutic target, researchers are increasingly interested in recombinant TALDO1 for biochemical studies, structural analysis, and drug development. The recombinant protein can be utilized to elucidate its catalytic mechanisms, explore its interactions with inhibitors and substrates, and assess its role in various metabolic pathways. By investigating TALDO1, scientists aim to deepen our understanding of metabolic pathways and their implications for health and disease, ultimately leading to novel treatment strategies for metabolic dysregulation.
