Analytical Data
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Gene name
LIPT1
- Application
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Alternative Names
LIPT1；Lipoyl amidotransferase LIPT1. mitochondrial
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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
Q9Y234
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Expression Region
26-373aa
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AA Sequence
KTVKNGLILQSISNDVYQNLAVEDWIHDHMNLEGKPILFFWQNSPSVVIGRHQNPWQECNLNLMREEGIKLARRRSGGGTVYHDMGNINLTFFTTKKKYDRMENLKLIVRALNAVQPQLDVQATKRFDLLLDGQFKISGTASKIGRTTAYHHCTLLCSTDGTFLSSLLKSPYQGIRSNATASIPSLVKNLLEKDPTLTCEVLMNAVATEYAAYHQIDNHIHLINPTDETLFPGINSKAKELQTWEWIYGKTPKFSINTSFHVLYEQSHLEIKVFIDIKNGRIEICNIEAPDHWLPLEIRDKLNSSLIGSKFCPTETTMLTNILLRTCPQDHKLNSKWNILCEKIKGIM
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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 an essential enzyme involved in the post-translational modification of proteins through the attachment of lipoyl groups, which are critical for the activity of various mitochondrial enzyme complexes, including the pyruvate dehydrogenase complex and alpha-ketoglutarate dehydrogenase. This modification is pivotal for cellular metabolism, energy production, and redox homeostasis. Research has shown that LIPT1 plays a significant role in neurodegenerative diseases and metabolic disorders, where its dysfunction can lead to impaired energy metabolism and increased oxidative stress. The investigation of LIPT1, particularly through the study of its recombinant protein, offers insights into its enzymatic mechanisms, regulation, and potential as a therapeutic target. Understanding the structural and functional dynamics of LIPT1 can also enhance our knowledge of mitochondrial biology and facilitate the development of novel treatments for diseases linked to mitochondrial dysfunction. The production and characterization of recombinant LIPT1 are thus fundamental to uncovering its roles and implications in health and disease.
