Analytical Data
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Gene name
TPI1
- Application
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Alternative Names
TPI1；TPI；Triosephosphate isomerase
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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
P60174-1
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Expression Region
1-249aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMAPSRKFFVGGNWKMNGRKQSLGELIGTLN AAKVPADTEVVCAPPTAYIDFARQKLDPKIAVAAQNCYKVTNGAFTGEIS PGMIKDCGATWVVLGHSERRHVFGESDELIGQKVAHALAEGLGVIACIGE KLDEREAGITEKVVFEQTKVIADNVKDWSKVVLAYEPVWAIGTGKTATPQ QAQEVHEKLRGWLKSNVSDAVAQSTRIIYGGSVTGATCKELASQPDVDGF LVGGASLKPEFVDIINAKQ
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Molecular Weight
29 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
TPI1 (Triosephosphate Isomerase 1) is an essential enzyme involved in the glycolytic and gluconeogenic pathways, catalyzing the interconversion between dihydroxyacetone phosphate and glyceraldehyde-3-phosphate. This enzyme plays a critical role in cellular metabolism and energy production, making it pivotal for maintaining glucose homeostasis. Mutations in the TPI1 gene can lead to TPI deficiency, a rare autosomal recessive disorder characterized by severe neurological complications and hemolytic anemia. Given its fundamental biological functions, TPI1 has garnered significant interest for research focused on metabolic diseases and potential therapeutic applications. The production of recombinant TPI1 protein allows for in-depth studies of its enzymatic properties, structural characteristics, and interactions with other biomolecules. Furthermore, recombinant TPI1 can be used to explore the effects of specific mutations on enzyme activity and stability, providing insights into the molecular mechanisms underlying TPI deficiency. These studies not only enhance our understanding of TPI1 and its dysfunction but also pave the way for developing targeted therapies that could alleviate symptoms associated with TPI deficiency and related metabolic disorders. Overall, the investigation of TPI1 as a recombinant protein holds substantial promise in elucidating both basic metabolic processes and potential clinical applications in managing metabolic diseases.
