(+/-)-alpha-Lipoamide - CAS 940-69-2
Catalog number: 940-69-2
Category: Inhibitor
Please be kindly noted products are not for therapeutic use. We do not sell to patients.
Molecular Formula:
Molecular Weight:
(+/-)-alpha-Lipoamide is a coenzyme, which transfer acetyl and hydrogen in Pyruvate deacylation oxidation process. It may be used in treatment of insulin resistance by stimulating mitochondrial biogenesis. It has shown to have a good therapeutic effect on early diabetic nephropathy when used in combination with Alprostadil.
>98 %
Light Yellow Solid
Lipoamide; Lipoacin; NSC 90787; NSC-90787; NSC90787; Lipoamide;Thioctamide;Thioctic acid amide;Vitamin N;Alpha-Lipoic acid amide;5-(Dithiolan-3-yl)pentanamide;(±)-α-Lipoamide;DL-Lipoamide;DL-6,8-Thioctamide;1,2-Dithiolane-3-pentanamide
10 mM in DMSO
(+/-)-alpha-Lipoamide may be used in treatment of insulin resistance by stimulating mitochondrial biogenesis. It has shown to have a good therapeutic effect on early diabetic nephropathy.
Quality Standard:
In-house standard
Shelf Life:
2 month in rt, long time
Kilogram to ton
Boiling Point:
399.2±11.0 °C | Condition: Press: 760 Torr
Melting Point:
124-126 °C | Condition: Solv: ethanol (64-17-5)
1.169±0.06 g/cm3 | Condition: Temp: 20 °C Press: 760 Tor
Canonical SMILES:
1.Liquid chromatographic determination of polythiols based on pre-column excimer fluorescence derivatization and its application to alpha-lipoic acid analysis.
Inoue T;Sudo M;Yoshida H;Todoroki K;Nohta H;Yamaguchi M J Chromatogr A. 2009 Oct 30;1216(44):7564-9. doi: 10.1016/j.chroma.2009.02.035. Epub 2009 Feb 21.
We developed an LC method for the sensitive and selective fluorometric determination of polythiols. This method employs pre-column intramolecular excimer-forming fluorescence derivatization with N-(1-pyrene)iodoacetamide followed by LC separation. Polythiols were converted to the corresponding dipyrene-labeled derivatives, and the derivatives afforded intramolecular excimer fluorescence (440-540 nm). After the optimization using dithiothreitol and dimercaprol as model polythiols, alpha-lipoic acid (LA) and alpha-lipoamide were determined with high sensitivity and selectivity. The detection limits for polythiols were 0.6-3.5 fmol on column. Furthermore, this method could be successfully applied to the determination of LA in commercial dietary supplements and in human urine.
2.TGL-mediated lipolysis in Manduca sexta fat body: possible roles for lipoamide-dehydrogenase (LipDH) and high-density lipophorin (HDLp).
Wu Z;Soulages JL;Joshi BD;Daniel SM;Hager ZJ;Arrese EL Insect Biochem Mol Biol. 2014 Feb;45:58-68. doi: 10.1016/j.ibmb.2013.12.001. Epub 2013 Dec 12.
Triglyceride-lipase (TGL) is a major fat body lipase in Manduca sexta. The knowledge of how TGL activity is regulated is very limited. A WWE domain, presumably involved in protein-protein interactions, has been previously identified in the N-terminal region of TGL. In this study, we searched for proteins partners that interact with the N-terminal region of TGL. Thirteen proteins were identified by mass spectrometry, and the interaction with four of these proteins was confirmed by immunoblot. The oxidoreductase lipoamide-dehydrogenase (LipDH) and the apolipoprotein components of the lipid transporter, HDLp, were among these proteins. LipDH is the common component of the mitochondrial α-keto acid dehydrogenase complexes whereas HDLp occurs in the hemolymph. However, subcellular fractionation demonstrated that these two proteins are relatively abundant in the soluble fraction of fat body adipocytes. The cofactor lipoate found in typical LipDH substrates was not detected in TGL. However, TGL proved to have critical thiol groups. Additional studies with inhibitors are consistent with the notion that LipDH acting as a diaphorase could preserve the activity of TGL by controlling the redox state of thiol groups.
3.Mycobacterium tuberculosis appears to lack alpha-ketoglutarate dehydrogenase and encodes pyruvate dehydrogenase in widely separated genes.
Tian J;Bryk R;Shi S;Erdjument-Bromage H;Tempst P;Nathan C Mol Microbiol. 2005 Aug;57(3):859-68.
Mycobacterium tuberculosis (Mtb) persists for prolonged periods in macrophages, where it must adapt to metabolic limitations and oxidative/nitrosative stress. However, little is known about Mtb's intermediary metabolism or antioxidant defences. We recently identified a peroxynitrite reductase-peroxidase complex in Mtb that included products of the genes sucB and lpd, which are annotated to encode the dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) components of alpha-ketoglutarate dehydrogenase (KDH). However, we could detect no KDH activity in Mtb lysates, nor could we reconstitute KDH by combining the recombinant proteins SucA (annotated as the E1 component of KDH), SucB and Lpd. We therefore renamed the sucB product dihydrolipoamide acyltransferase (DlaT). Mtb lysates contained pyruvate dehydrogenase (PDH) activity, which was lost when the dlaT gene (formerly, sucB) was disrupted. Purification of PDH from Mtb yielded AceE, annotated as an E1 component of PDH, along with DlaT and Lpd. Moreover, anti-DlaT antibody coimmunoprecipitated AceE. Finally, recombinant AceE, DlaT and Lpd, although encoded by genes that are widely separated on the chromosome, reconstituted PDH in vitro with Km values typical of bacterial PDH complexes.
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CAS 940-69-2 (+/-)-alpha-Lipoamide

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