Analytical Data
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Gene name
TMLHE
- Application
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Alternative Names
Epsilon-trimethyllysine 2-oxoglutarate dioxygenase;Epsilon-trimethyllysine hydroxylaseTML hydroxylaseTML-alpha-ketoglutarate dioxygenase ;TML dioxygenase ;TMLD
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Species
Human
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Source
E. coli
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Tag
N- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9NVH6
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Expression Region
16-376aa
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Molecular Weight
46.1 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
TMLHE (Trimethyllysine Hydroxylase) is an enzyme that plays a crucial role in the metabolism of trimethyllysine, a derivative of lysine that is important in various biological processes, including protein modification and methylation. The significance of TMLHE stems from its involvement in the carnitine biosynthesis pathway, essential for the transport of long-chain fatty acids into the mitochondria for energy production. Research has indicated that alterations in TMLHE activity may be linked to metabolic disorders and insulin resistance, thus making it a potential target for therapeutic interventions. The recombinant expression and purification of TMLHE have become crucial for understanding its enzymatic mechanisms and for developing inhibitory compounds that could modulate its activity. Additionally, studying TMLHE at the molecular level may provide insights into the regulation of lysine modifications, which have implications in epigenetics and gene expression. As such, the investigation of TMLHE and its recombinant protein is a vibrant area of research, with the potential to unravel novel biochemical pathways and therapeutic avenues in metabolic health.
