Analytical Data
-
Gene name
LIAS
- Application
-
Alternative Names
LIAS；LAS；Lipoyl synthase. mitochondrial
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
O43766
-
Expression Region
28-372aa
-
AA Sequence
LSSLPDKKKELLQNGPDLQDFVSGDLADRSTWDEYKGNLKRQKGERLRLPPWLKTEIPMGKNYNKLKNTLRNLNLHTVCEEARCPNIGECWGGGEYATATATIMLMGDTCTRGCRFCSVKTARNPPPLDASEPYNTAKAIAEWGLDYVVLTSVDRDDMPDGGAEHIAKTVSYLKERNPKILVECLTPDFRGDLKAIEKVALSGLDVYAHNVETVPELQSKVRDPRANFDQSLRVLKHAKKVQPDVISKTSIMLGLGENDEQVYATMKALREADVDCLTLGQYMQPTRRHLKVEEYITPEKFKYWEKVGNELGFHYTASGPLVRSSYKAGEFFLKNLVAKRKTKDL
-
Molecular Weight
45.8 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
LIAS, or Lipoic Acid Synthetase, is an important enzyme involved in the biosynthesis of lipoic acid, a vital cofactor required for various metabolic processes, particularly in the mitochondrial multienzyme complexes. The understanding of LIAS has garnered significant attention in recent years due to its crucial role in energy metabolism and its implications in health and disease. Dysfunctions in the LIAS enzyme have been linked to neuromuscular disorders and metabolic syndromes, highlighting the need for a detailed study of its structure and function. Research on recombinant LIAS proteins has become a focal point for elucidating the enzyme's mechanisms and exploring potential therapeutic targets. By studying the properties of LIAS through recombinant techniques, researchers aim to characterize its enzymatic activity, interaction with other proteins, and regulatory pathways. Additionally, this research holds promise for the development of novel strategies to mitigate lipoic acid-related deficiencies and their associated disorders. As the biotechnology field progresses, the recombinant expression of LIAS in various model organisms and systems provides a platform for further understanding its biological significance and potential applications in medicine. This research not only enriches our knowledge of metabolic pathways but also opens new avenues for biotechnological innovations, making LIAS an essential focus in the study of bioenergetics and related fields.
