Datasheet

生物学的記述

Specificity	ACSF2 Antibody [F15E3] detects endogenous levels of total ACSF2 protein.
Background	ACSF2 (acyl-CoA synthetase family member 2) is a mitochondrial matrix enzyme that catalyzes the activation of medium-chain fatty acids into acyl-CoA thioesters, a crucial step for β-oxidation and maintaining lipid homeostasis. It possesses a canonical AMP-binding superfamily architecture, including an N-terminal mitochondrial targeting sequence that is cleaved upon import, an ATP-grasp domain responsible for Mg-ATP binding, an A10-like subdomain forming the substrate-binding cleft for fatty acid interaction, and a C-terminal dimerization domain that enables obligatory homodimerization. ACSF2 operates via a two-step ping-pong mechanism, where ATP thioesterification forms an acyl-AMP intermediate followed by nucleophilic displacement by the CoA thiol to generate acyl-CoA and AMP, with a marked specificity for medium-chain fatty acids. This enzyme supports mitochondrial β-oxidation by enabling CPT1-independent import of medium-chain fatty acids, bypassing carnitine shuttle limitations. Deficiency of ACSF2 leads to combined malonic and methylmalonic aciduria (CMAMMA), resulting in the accumulation of dicarboxylic acids due to impaired fatty acid catabolism and deficits in protein lipoylation, which are essential for mitochondrial enzyme complex stability. Somatic overexpression of ACSF2 is associated with non-alcoholic fatty liver disease and hepatocellular carcinoma through dysregulated hepatic VLDL secretion and increased lipid droplet accumulation.

Specificity

ACSF2 Antibody [F15E3] detects endogenous levels of total ACSF2 protein.

Background

ACSF2 (acyl-CoA synthetase family member 2) is a mitochondrial matrix enzyme that catalyzes the activation of medium-chain fatty acids into acyl-CoA thioesters, a crucial step for β-oxidation and maintaining lipid homeostasis. It possesses a canonical AMP-binding superfamily architecture, including an N-terminal mitochondrial targeting sequence that is cleaved upon import, an ATP-grasp domain responsible for Mg-ATP binding, an A10-like subdomain forming the substrate-binding cleft for fatty acid interaction, and a C-terminal dimerization domain that enables obligatory homodimerization. ACSF2 operates via a two-step ping-pong mechanism, where ATP thioesterification forms an acyl-AMP intermediate followed by nucleophilic displacement by the CoA thiol to generate acyl-CoA and AMP, with a marked specificity for medium-chain fatty acids. This enzyme supports mitochondrial β-oxidation by enabling CPT1-independent import of medium-chain fatty acids, bypassing carnitine shuttle limitations. Deficiency of ACSF2 leads to combined malonic and methylmalonic aciduria (CMAMMA), resulting in the accumulation of dicarboxylic acids due to impaired fatty acid catabolism and deficits in protein lipoylation, which are essential for mitochondrial enzyme complex stability. Somatic overexpression of ACSF2 is associated with non-alcoholic fatty liver disease and hepatocellular carcinoma through dysregulated hepatic VLDL secretion and increased lipid droplet accumulation.

使用情報

Application

WB, FCM, ELISA

Dilution

WB	FCM
1:2000-1:10000	1:8000

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

68 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/36160020/
https://www.biorxiv.org/content/10.1101/2022.03.28.486105v1.abstract

Application Data

WB

Validated by Selleck

Lane 1: Jurkat