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AB96302

Anti-LIAS antibody

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(4 Publications)

Rabbit Polyclonal LIAS antibody. Suitable for WB and reacts with Human samples. Cited in 4 publications. Immunogen corresponding to Recombinant Fragment Protein within Human LIAS aa 50-300.

View Alternative Names

LAS, HUSSY-01, LIAS, Lipoate synthase, Lipoic acid synthase, LS, Lip-syn

1 Images
Western blot - Anti-LIAS antibody (AB96302)
  • WB

Unknown

Western blot - Anti-LIAS antibody (AB96302)

All lanes:

Western blot - Anti-LIAS antibody (ab96302) at 1/1000 dilution

All lanes:

Raji whole cell lysate at 30 µg

Predicted band size: 42 kDa

false

Key facts

Host species

Rabbit

Clonality

Polyclonal

Isotype

IgG

Carrier free

No

Reacts with

Human

Applications

WB

applications

Immunogen

Recombinant Fragment Protein within Human LIAS aa 50-300. The exact immunogen used to generate this antibody is proprietary information.

O43766

Reactivity data

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Properties and storage information

Form
Liquid
Purification technique
Affinity purification Immunogen
Storage buffer
pH: 7 Preservative: 0.01% Thimerosal (merthiolate) Constituents: 20% Glycerol (glycerin, glycerine), 1.21% Tris, 0.75% Glycine
Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
+4°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle

Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

The biological target LIAS also known as lipoic acid synthase plays an important role in the synthesis of lipoic acid. LIAS is an enzyme with a molecular mass of approximately 40 kDa and it is present in many tissues showing high expression in liver and kidney. It functions as a homodimer in the mitochondria indicating its role as an important player in mitochondrial processes. The enzyme catalyzes the final step in the synthesis of lipoic acid by attaching sulfur atoms to octanoyl groups attached to protein domains.
Biological function summary

LIAS contributes to the activation of metabolic complexes by providing protein-bound lipoic acid. It integrates into multiprotein complexes facilitating their function. This lipoic acid acts as a cofactor for key mitochondrial enzyme complexes such as pyruvate dehydrogenase and α-ketoglutarate dehydrogenase which are important for energy production. These complexes are essential for the conversion of nutrients into usable energy highlighting the biochemical importance of LIAS in cellular respiration and metabolic regulation.

Pathways

Lipoic acid synthase is fundamental for mitochondrial energy metabolism and redox regulation pathways. It participates in the tricarboxylic acid cycle where it influences the activity of related enzymes. Through this activity LIAS interacts indirectly with proteins such as pyruvate dehydrogenase and dihydrolipoamide dehydrogenase both of which play a significant role in maintaining cellular energy balance. The efficient functioning of these pathways is important for cellular survival and homeostasis.

Mutations in LIAS have been linked to rare metabolic disorders like multiple mitochondrial dysfunctions syndrome. These mutations can lead to severe energy production deficits due to impaired enzyme complex assembly. In these conditions LIAS's connection to lipoic acid-dependent proteins like pyruvate dehydrogenase impacts disease progression further demonstrating its role in mitochondrial health. On a broader scale alterations in LIAS function might also relate to disorders involving energy metabolism such as neurodegenerative diseases.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

Catalyzes the radical-mediated insertion of two sulfur atoms into the C-6 and C-8 positions of the octanoyl moiety bound to the lipoyl domains of lipoate-dependent enzymes, thereby converting the octanoylated domains into lipoylated derivatives.
See full target information LIAS

Publications (4)

Recent publications for all applications. Explore the full list and refine your search

Acta pharmaceutica Sinica. B 14:4059-4072 PubMed39309486

2024

CRISPR-Cas9 gene editing strengthens cuproptosis/chemodynamic/ferroptosis synergistic cancer therapy.

Applications

Unspecified application

Species

Unspecified reactive species

Xiaoyu Wu,Zijun Bai,Hui Wang,Hanqing Wang,Dahai Hou,Yunzhu Xu,Guanqun Wo,Haibo Cheng,Dongdong Sun,Weiwei Tao

Journal of biochemical and molecular toxicology 38:e23848 PubMed39264832

2024

GAD1 ameliorates glioma progression through regulating cuproptosis via RAS/MAPK pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Zhiqiang Gao,Jing Yang

PLoS genetics 16:e1009176 PubMed33137164

2020

Dual genome-wide CRISPR knockout and CRISPR activation screens identify mechanisms that regulate the resistance to multiple ATR inhibitors.

Applications

Unspecified application

Species

Unspecified reactive species

Emily M Schleicher,Ashna Dhoonmoon,Lindsey M Jackson,Kristen E Clements,Coryn L Stump,Claudia M Nicolae,George-Lucian Moldovan

Haematologica 104:1756-1767 PubMed30765471

2019

Dimeric ferrochelatase bridges ABCB7 and ABCB10 homodimers in an architecturally defined molecular complex required for heme biosynthesis.

Applications

Unspecified application

Species

Unspecified reactive species

Nunziata Maio,Ki Soon Kim,Gregory Holmes-Hampton,Anamika Singh,Tracey A Rouault
View all publications

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