Abcam, ab227565, Anti-PDHA1 (phospho S293) antibody [EPR12200] - BSA and Azide free

Size: 100µg / 1mg
Rabbit Recombinant Monoclonal PDHA1 phospho S293 antibody. Carrier free. Suitable for IHC-P, IP, ELISA, WB and reacts with Mouse, Human, Rat samples. Cited in 6 publications.
Key facts
Host species:Rabbit,
Clonality:Monoclonal,
Clone number:EPR12200,
Isotype:IgG,
Carrier free:Yes,
Reacts with:Mouse, Rat, Human,
Applications:IHC-P, ELISA, IP, WBSee 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:
ab227565 is the carrier-free version of
ab177461
Conjugation ready
Our carrier-free antibodies are typically supplied in a PBS-only formulation, purified and free of BSA, sodium azide and glycerol. This conjugation-ready format is designed for use with fluorochromes, metal isotopes, oligonucleotides, and enzymes, which makes them ideal for antibody labelling, functional and cell-based assays, flow-based assays (e.g. mass cytometry) and Multiplex Imaging applications.
Use our
conjugation kits
for antibody conjugates that are ready-to-use in as little as 20 minutes with 1 minute hands-on-time and 100% antibody recovery: available for fluorescent dyes, HRP, biotin and gold.
Compatibility
This product is compatible with the Maxpar
Antibody Labeling Kit from Fluidigm, without the need for antibody preparation. Maxpar
is a trademark of Fluidigm Canada Inc.

Properties and Storage Information:
Form-Liquid, Purification technique-Affinity purification Protein A, Storage buffer-pH: 7.2 - 7.4Constituents: PBS, 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.