Analytical Data
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Gene name
LIPT1
- Application
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Alternative Names
Lipoate biosynthesis protein Lipoate-protein ligase Lipoyl ligase
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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
Q9Y234
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Expression Region
26-373aa
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Molecular Weight
45.7 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
Related Products
Protein Description
LIPT1 (lipoyltransferase 1) is a crucial enzyme involved in the post-translational modification of mitochondrial proteins through the addition of lipoic acid, a cofactor essential for proper mitochondrial function and energy metabolism. Research into LIPT1 has gained significant attention due to its role in various biological processes and disease mechanisms. Dysfunction of LIPT1 has been implicated in metabolic disorders, neurodegenerative diseases, and certain types of cancer, prompting scientists to investigate its structure and function. The recombinant production of LIPT1 protein enables detailed biochemical studies, allowing researchers to dissect its enzymatic mechanism and interactions with substrate proteins. Understanding LIPT1's role can reveal insights into mitochondrial biology and potentially lead to novel therapeutic strategies for diseases associated with mitochondrial dysfunction. The development of efficient expression systems for LIPT1 and the exploration of its enzymatic properties are critical steps in elucidating its biological significance and therapeutic potential.
