Datasheet

Biological Description

Specificity	Citrate synthetase Antibody [K19C21] detects endogenous levels of total Citrate synthetase protein.
Background	Citrate synthase (CS) is a mitochondrial enzyme classified within the citrate synthase family, playing a crucial role in cellular metabolism as it catalyzes the first and rate-limiting step of the tricarboxylic acid (TCA) cycle, or Krebs cycle. Citrate synthase is a globular protein of approximately 433 to 437 amino acids organized mainly into two alpha-helical domains separated by a cleft that forms the enzyme’s active site. Key catalytic residues include histidine and aspartate residues (His274, His320, Asp375), which facilitate substrate interaction and catalysis. The enzyme undergoes a significant conformational change upon substrate binding, allowing oxaloacetate to bind first and induce a closed conformation that creates the binding site for acetyl-CoA, ensuring proper catalysis and prevention of premature hydrolysis. Citrate synthase catalyzes the condensation of acetyl-CoA and oxaloacetate to form citrate and coenzyme A in an aldol-Claisen condensation followed by hydrolysis, making it pivotal for energy production through ATP generation by mitochondrial respiration pathways. It acts as an important metabolic checkpoint, with citrate levels modulating further steps in the Krebs cycle and providing feedback inhibition for glycolysis. Citrate synthase’s activity influences overall metabolic rate, and its dysfunction has been linked to disease states such as cancer, where reduced citrate synthase activity is associated with more malignant cell phenotypes, metabolic disorders, including diabetes, and mitochondrial diseases affecting energy homeostasis.

Specificity

Citrate synthetase Antibody [K19C21] detects endogenous levels of total Citrate synthetase protein.

Background

Citrate synthase (CS) is a mitochondrial enzyme classified within the citrate synthase family, playing a crucial role in cellular metabolism as it catalyzes the first and rate-limiting step of the tricarboxylic acid (TCA) cycle, or Krebs cycle. Citrate synthase is a globular protein of approximately 433 to 437 amino acids organized mainly into two alpha-helical domains separated by a cleft that forms the enzyme’s active site. Key catalytic residues include histidine and aspartate residues (His274, His320, Asp375), which facilitate substrate interaction and catalysis. The enzyme undergoes a significant conformational change upon substrate binding, allowing oxaloacetate to bind first and induce a closed conformation that creates the binding site for acetyl-CoA, ensuring proper catalysis and prevention of premature hydrolysis. Citrate synthase catalyzes the condensation of acetyl-CoA and oxaloacetate to form citrate and coenzyme A in an aldol-Claisen condensation followed by hydrolysis, making it pivotal for energy production through ATP generation by mitochondrial respiration pathways. It acts as an important metabolic checkpoint, with citrate levels modulating further steps in the Krebs cycle and providing feedback inhibition for glycolysis. Citrate synthase’s activity influences overall metabolic rate, and its dysfunction has been linked to disease states such as cancer, where reduced citrate synthase activity is associated with more malignant cell phenotypes, metabolic disorders, including diabetes, and mitochondrial diseases affecting energy homeostasis.

Usage Information

Application

WB, IHC, IF, FCM

Dilution

WB	IHC	IF	FCM
1:1000 - 1:10000	1:250 - 1:500	1:100 - 1:500	1:20

Reactivity

Mouse, Rat, Human

Source

Rabbit Monoclonal Antibody

MW

51 kDa,73 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

Exprimental Methods

References

https://pubmed.ncbi.nlm.nih.gov/37393492/
https://pubmed.ncbi.nlm.nih.gov/35873436/

Application Data

WB

Validated by Selleck

Lane 1: HepG2, Lane 2: CaCo-2, Lane 3: Hela, Lane 4: 293T