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Agrisera
PDHE1-A/Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial Polyclonal Antibody
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FIGURE: 1 / 1
PDHE1-A/Pyruvate dehydrogenase E1 component subunit alpha-1, mitochondrial Antibody (AS23-4974) in WB
Samples: 1 - 40 µg of Arabidopsis thaliana Col-0 whole leaf extract. 2 - 40 µg of Arabidopsis thaliana mutant iar 4 (AT 1 G 24180), Arabidopsis thaliana pyruvate dehydrogenase E 1 a-like subunit. 3 - 40 µg of Arabidopsis thaliana mutant iar 4 l-1 (AT 1 G 59900), Arabidopsis thaliana pyruvate dehydrogenase E 1 a subunit. 4 - 40 µg of Arabidopsis thaliana mutant iar 4 l-2 (AT 1 G 59900), Arabidopsis thaliana ... View More
Product Details
AS23-4974
Product Specifications
Species Reactivity
Plant
Host/Isotype
Rabbit
Class
Polyclonal
Type
Antibody
Immunogen
KLH-conjugated, unique peptide derived from Arabidopsis thaliana PDHE1-A.
Conjugate
Form
Lyophilized
Amount
50 µg
Purification
Antigen affinity chromatography
Storage buffer
PBS, pH 7.4
Contains
no preservative
Storage conditions
-20°C, Avoid Freeze/Thaw Cycles
Shipping conditions
Ambient (domestic); Wet ice (international)
Product Specific Information
Store lyophilized/reconstituted at -20°C; once reconstituted make aliquots to avoid repeated freeze-thaw cycles. Please, remember to spin tubes briefly prior to opening them to avoid any losses that might occur from lyophilized material adhering to the cap or sides of the tubes.
For reconstitution add 50 µL of sterile water.
Specific Species Reactivity: Arabidopsis thaliana
Target Information
PDHE1-A (PDHA1) encodes the E1 component alpha subunit of the nuclear-encoded pyruvate dehydrogenase (PDH) complex and is synthesized as a mitochondrial precursor that is imported into the mitochondrial matrix after cleavage of an N-terminal targeting peptide. The mature protein assembles with the E1 beta subunit to form an alpha2beta2 heterotetrameric E1 enzyme; this thiamine diphosphate (ThDP)- and Mg2+-dependent decarboxylase provides the first catalytic step of the PDH complex, binding/coordinating ThDP and forming the active-site architecture required for pyruvate oxidative decarboxylation. Functionally, E1 (via the PDHE1-A-containing heterotetramer) catalyzes ThDP-mediated decarboxylation of pyruvate and generation of a hydroxyethyl-ThDP intermediate, enabling subsequent transfer of the acetyl group to the lipoyl moiety on the E2 component and ultimately production of acetyl-CoA and NADH; in this way it constitutes a key biochemical link between cytosolic glycolysis and the tricarboxylic acid cycle/oxidative phosphorylation. PDHE1-A activity is tightly regulated by reversible phosphorylation on serine residues located in flexible regulatory loops of the alpha subunit, where phosphorylation promotes loop disorder and/or restricts substrate-channel access, thereby inhibiting E1 catalysis and limiting acetyl transfer to the E2 lipoyl domain.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
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Bioinformatics
Protein Aliases: E1alpha; PDHA; PDHAD; PDHCE1A; PHE1A
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