Product Description
Size: 100µg
Anti-PDHA1 antibody [9H9AF5] (ab110330) is a mouse monoclonal antibody detecting PDHA1 in Western Blot, Flow Cytometry, ICC/IF . Suitable for Cow, Human, Mouse, Rat . - KO validated for confirmed specificity - Over 80 publications
Key facts
Host species:Mouse,
Clonality:Monoclonal,
Clone number:9H9AF5,
Isotype:IgG1,
Light chain type:kappa,
Carrier free:No,
Reacts with:Mouse, Rat, Cow, Human,
Applications:Flow Cyt, WB, ICC/IFSee 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-PDHA1 antibody [9H9AF5] (ab110330) is a mouse monoclonal antibody and is validated for use in Western Blot (WB), Flow Cytometry (Flow Cyt), Immunocytochemistry/immunofluorescence (ICC/IF) in Cow, Human, Mouse, Rat samples.
What is the molecular weight of PDHA1?
Anti-PDHA1 [9H9AF5] (ab110330) specifically detects a band for PDHA1 (UniProt: P08559) at a molecular weight of 43kDa.
Trusted by the scientific community
Anti-PDHA1 [9H9AF5] (ab110330) was first used in a scientific publication in 2011 and has been cited over 80 times in peer-reviewed journals.
Reviewed by scientists
Anti-PDHA1 [9H9AF5] (ab110330) has over 5 independent reviews from customers.
Specificity confirmed
The specificity of Anti-PDHA1 antibody [9H9AF5] (ab110330) has been confirmed by Western blot testing in PDHA1 Knockout HeLa cells.
Other related products
We have a range of other formats of antibody clone [9H9AF5] also available for your convenience: ab110330, HRP -
ab197956
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-ab110330 was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation., Storage buffer-pH: 7.5 Preservative: 0.02% Sodium azide Constituents: 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.
PDHA1 also known as the pyruvate dehydrogenase E1 alpha subunit plays a mechanical role in cellular metabolism. It forms part of the larger pyruvate dehydrogenase (PDH) complex where it serves as a critical catalytic component. PDHA1 is expressed ubiquitously across different tissue types reflecting its fundamental function in energy production. The molecular weight of the PDHA1 protein is approximately 43 kDa. Alternate names for this protein include the PDH E1 component and it partners closely with other components in the PDH complex to facilitate its role.
Biological function summary
PDHA1 engages in the conversion of pyruvate into acetyl-CoA an important step in cellular respiration. This protein is part of the PDH complex which consists of multiple copies of three catalytic and two regulatory subunits. The conversion process is essential for linking glycolysis to the citric acid cycle efficiently channeling energy substrates within the cell. Furthermore the functional activity of PDHA1 is regulated through phosphorylation by the pyruvate dehydrogenase kinases (PDKs) and dephosphorylation by PDH phosphatases.
Pathways
PDHA1 is integral to the metabolic pathway of cellular respiration and energy production. It enables the transition between glycolysis and the citric acid cycle by facilitating the conversion of pyruvate to acetyl-CoA which enters the citric acid cycle. Related proteins in this pathway include PDHA2 and the regulatory PDKs that modulate PDHA1 activity. These interactions ensure energy metabolism adapts to various cellular conditions influencing energy balance and substrate utilization.
Mutations or dysfunctions in PDHA1 can lead to disorders such as pyruvate dehydrogenase deficiency and Leigh syndrome. These conditions result from impaired energy metabolism leading to severe neurological symptoms and overall energy deficits in tissues with high metabolic demands. The link between PDHA1 and diseases highlights the importance of maintaining its function. Additionally altered interaction with proteins involved in phosphorylation such as the PDKs can exacerbate pathogenic conditions by further disbalancing metabolic activities.
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Collaboration
Tony Tang
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