Abcam, ab110333, Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5]

Size: 100µg
Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (ab110333) is a mouse monoclonal antibody detecting PDHX in Western Blot, Flow Cytometry, IHC-P, ICC/IF . Suitable for Cow, Human, Mouse, Rat . - KO validated for confirmed specificity - Over 40 publications
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:13G2AE2BH5,
Isotype:IgG2a,
Light chain type:kappa,
Carrier free:No,
Reacts with:Mouse, Rat, Cow, Human,
Applications:Flow Cyt, WB, ICC/IF, IHC-PSee reactivity dataSee the reactivity data table below for information on validated species and application combinations.,
Immunogen:The exact immunogen used to generate this antibody is proprietary information.

Product details:
What is this antibody validated in?
Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (ab110333) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Flow Cytometry (Flow Cyt), Immunohistochemistry (IHC-P), Immunocytochemistry/immunofluorescence (ICC/IF) in Cow, Human, Mouse, Rat samples.
What is the molecular weight of PDHX?
Anti-Pyruvate dehydrogenase E2/E3bp [13G2AE2BH5] (ab110333) specifically detects a band for PDHX (UniProt: O00330) at a molecular weight of 54 , 69kDa.
Trusted by the scientific community
Anti-Pyruvate dehydrogenase E2/E3bp [13G2AE2BH5] (ab110333) was first used in a scientific publication in 2011 and has been cited over 40 times in peer-reviewed journals.
Reviewed by scientists
Anti-Pyruvate dehydrogenase E2/E3bp [13G2AE2BH5] (ab110333) has over 5 independent reviews from customers.
Specificity confirmed
The specificity of Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (ab110333) has been confirmed by Western blot testing in DLAT Knockout HAP1 cells.
Want a custom formulation?
This antibody clone is manufactured by Abcam. If you require a custom buffer formulation or conjugation for your experiments, please contact orders@abcam.com

Properties and Storage Information:
Form-Liquid, Purity-IgG fraction, Purification notes-ab110333 was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation., Storage buffer-pH: 7.5Preservative: 0.02% Sodium azideConstituents: HEPES buffered saline, Shipped at conditions-Blue Ice, Appropriate short-term storage conditions-+4°C, Appropriate long-term storage conditions-+4°C, Storage information-Do Not Freeze

Supplementary Information:
This supplementary information is collated from multiple sources and compiled automatically.
PDHX also known as pyruvate dehydrogenase protein X is a part of the pyruvate dehydrogenase complex. It has a molecular mass of about 54 kDa. PDHX is expressed mostly in tissues with high energy demands such as the heart and skeletal muscle. The protein has a critical role in linking glycolysis and the Krebs cycle by transferring the lipoamide group in the pyruvate dehydrogenase complex.
Biological function summary
PDHX functions as a component of the multi-enzyme pyruvate dehydrogenase complex (PDC). This complex is essential for the oxidative decarboxylation of pyruvate to acetyl-CoA within the mitochondria. PDHX coordinates with other enzymes such as E1 E2 and E3 carrying out its function by acting as an anchor to stabilize the PDC enhancing the efficiency of the catalytic process.
Pathways
PDHX participates in important metabolic pathways like glycolysis and the Krebs cycle. It relates closely with proteins such as E1 (pyruvate dehydrogenase) and E2 (dihydrolipoamide acetyltransferase) due to its role in facilitating the transition of energy substrates into the cycle. Its activity helps in the regulation of energy production within cells and impacts processes that depend on efficient energy conversion.
Mutations or deficiencies in PDHX have connections with pyruvate dehydrogenase deficiency and metabolic disorders like Leigh syndrome. These conditions affect energy metabolism and can lead to severe neurological problems. The malfunction of PDHX impacts the pyruvate dehydrogenase complex as a whole leading to an increase of pyruvate levels and a decrease in ATP production linking it also with other involved proteins like E1 and E2.