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AB110333

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

4

(6 Reviews)

|

(62 Publications)

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

View Alternative Names

DLTA, DLAT, 70 kDa mitochondrial autoantigen of primary biliary cirrhosis, Dihydrolipoamide acetyltransferase component of pyruvate dehydrogenase complex, M2 antigen complex 70 kDa subunit, Pyruvate dehydrogenase complex component E2, PBC, PDC-E2, PDCE2

6 Images
Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • WB

Supplier Data

Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

Lanes 1 - 4 : Merged signal (red and green). Green - ab110333 observed at 72 kDa. Red - loading control, ab181602, observed at 38 kDa.

ab110333 was shown to specifically react with in wild-type HAP1 cells as signal was lost in DLAT knockout cells. Wild-type and DLAT knockout samples were subjected to SDS-PAGE. The membrane was blocked with 3% Milk. ab110333 and ab181602 (Rabbit anti-GAPDH loading control) were incubated overnight at 4°C at 1 μg/ml and 1/20000 dilution respectively. Blots were developed with Goat anti-Mouse IgG H&L (IRDye® 800CW) preabsorbed ab216772 and Goat anti-Mouse IgG H&L (IRDye® 680RD) preabsorbed ab216776 secondary antibodies at 1/20000 dilution for 1 hour at room temperature before imaging.

All lanes:

Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (ab110333) at 1 µg/mL

Lane 1:

Wild-type HAP1 whole cell lysate at 20 µg

Lane 2:

DLAT knockout HAP1 whole cell lysate at 20 µg

Lane 3:

HeLa whole cell lysate at 20 µg

Lane 4:

HL-60 whole cell lysate at 20 µg

Predicted band size: 69 kDa

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Flow Cytometry - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • Flow Cyt

Supplier Data

Flow Cytometry - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

Flow cytometric analysis using ab110333 at 1µg/ml staining Pyruvate dehydrogenase E2/E3b in HL60 cells (blue). Isotype control antibody (red).

Immunocytochemistry/ Immunofluorescence - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • ICC/IF

Unknown

Immunocytochemistry/ Immunofluorescence - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

Immunocytochemistry analysis using ab110333 at 1μg/ml staining Pyruvate dehydrogenase E2/E3bp in cultured, normal Human embryonic lung fibroblasts and an AlexaFluor® 488 goat anti-mouse IgG2a secondary antibody (2 ug/ml).

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • IHC-P

Unknown

Immunohistochemistry (Formalin/PFA-fixed paraffin-embedded sections) - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

Immunohistological analysis using ab110333 at 1/1000 dilution staining Pyruvate dehydrogenase E2/E3bp in Human cerebellum tissue (Formalin-fixed, Paraffin-embedded).
Note : Immunoactivity is most intense in neuronal cell bodies, most notably in the large Purkinje cells.

Immunocytochemistry/ Immunofluorescence - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • ICC/IF

AbReview39448****

Immunocytochemistry/ Immunofluorescence - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

ab110333 staining Pyruvate dehydrogenase E2/E3bp in Human HUVEC by ICC/IF (Immunocytochemistry/immunofluorescence). Cells were fixed with paraformaldehyde, permeabilized with 0.1% Triton X-100 pH 7.4 for 5 minutes and blocked with 5% BSA for 20 minutes at room temperature. Samples were incubated with primary antibody (1/1000 in PBS) for 1 hour. A CF568-conjugated Goat anti-mouse IgG polyclonal (1/500) was used as the secondary antibody.

This image is courtesy of an Abreview submitted by Dimitra Kalamida

Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)
  • WB

Unknown

Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (AB110333)

All lanes:

Western blot - Anti-Pyruvate dehydrogenase E2/E3bp antibody [13G2AE2BH5] (ab110333) at 1 µg/mL

Lane 1:

Isolated mitochondria from Human heart at 5 µg

Lane 2:

Isolated mitochondria from Bovine heart at 1 µg

Lane 3:

Isolated mitochondria from Rat heart at 10 µg

Lane 4:

Isolated mitochondria from Mouse heart at 10 µg

Lane 5:

HepG2 cell lysate at 20 µg

Predicted band size: 69 kDa

false

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

WB, ICC/IF, IHC-P, Flow Cyt

applications

Immunogen

The exact immunogen used to generate this antibody is proprietary information.

Reactivity data

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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: 7.5 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.

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.

Product protocols

For this product, it's our understanding that no specific protocols are required. You can visit:

Target data

As part of the pyruvate dehydrogenase complex, catalyzes the transfers of an acetyl group to a lipoic acid moiety (Probable). The pyruvate dehydrogenase complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle (Probable).
See full target information DLAT

Publications (62)

Recent publications for all applications. Explore the full list and refine your search

Journal of extracellular vesicles 14:e70140 PubMed40767334

2025

ATP Synthase Abundance in Neuronal Extracellular Vesicles Reflects Changes in the Mitochondria of Parent Neurons.

Applications

Unspecified application

Species

Unspecified reactive species

Pamela J Yao,Carlos Nogueras-Ortiz,Krishna Ananthu Pucha,Dimitrios Kapogiannis

FASEB bioAdvances 7:e70030 PubMed40641845

2025

PINK1 Loss of Function Selectively Alters the Mitochondrial-Derived Vesicle Pathway.

Applications

Unspecified application

Species

Unspecified reactive species

Charlotte L Collier,Colleen Ruedi,Naomi J Thorne,David A Tumbarello

Theranostics 15:5499-5517 PubMed40303326

2025

Nitric oxide-primed engineered extracellular vesicles restore bioenergetics in acute kidney injury via mitochondrial transfer.

Applications

Unspecified application

Species

Unspecified reactive species

Fei Peng,Xiaoniao Chen,Lingling Wu,Jiayi He,Zongjin Li,Quan Hong,Qiang Zhao,Meng Qian,Xu Wang,Wanjun Shen,Tingting Qi,Yiyu Huang,Guangyan Cai,Chuyue Zhang,Xiangmei Chen

Cell death and differentiation 32:1200-1213 PubMed40050422

2025

Cancer-intrinsic Cxcl5 orchestrates a global metabolic reprogramming for resistance to oxidative cell death in 3D.

Applications

Unspecified application

Species

Unspecified reactive species

Ramin Seo,Arvie Camille V de Guzman,Sunghyouk Park,Ji Youn Lee,Suk-Jo Kang

Nature 639:776-783 PubMed39972141

2025

Dual regulation of mitochondrial fusion by Parkin-PINK1 and OMA1.

Applications

Unspecified application

Species

Unspecified reactive species

Tatsuya Yamada,Arisa Ikeda,Daisuke Murata,Hu Wang,Cissy Zhang,Pratik Khare,Yoshihiro Adachi,Fumiya Ito,Pedro M Quirós,Seth Blackshaw,Carlos López-Otín,Thomas Langer,David C Chan,Anne Le,Valina L Dawson,Ted M Dawson,Miho Iijima,Hiromi Sesaki

iScience 27:110880 PubMed39310760

2024

mCAUSE: Prioritizing mitochondrial targets that alleviate pancreatic cancer cell phenotypes.

Applications

Unspecified application

Species

Unspecified reactive species

Daisuke Murata,Fumiya Ito,Gongyu Tang,Wakiko Iwata,Nelson Yeung,Junior J West,Andrew J Ewald,Xiaowei Wang,Miho Iijima,Hiromi Sesaki

The Journal of neuroscience : the official journal of the Society for Neuroscience 44: PubMed39266301

2024

A miR-383-5p Signaling Hub Coordinates the Axon Regeneration Response to Inflammation.

Applications

Unspecified application

Species

Unspecified reactive species

Matthew A Hintermayer,Camille A Juźwik,Barbara Morquette,Elizabeth Hua,Julia Zhang,Sienna Drake,Shan Shan Shi,Isabel Rambaldi,Vamshi Vangoor,Jeroen Pasterkamp,Craig Moore,Alyson E Fournier

iScience 27:110510 PubMed39175772

2024

BCL2L13 at endoplasmic reticulum-mitochondria contact sites regulates calcium homeostasis to maintain skeletal muscle function.

Applications

Unspecified application

Species

Unspecified reactive species

Dogan Grepper,Cassandra Tabasso,Nadège Zanou,Axel K F Aguettaz,Mauricio Castro-Sepulveda,Dorian V Ziegler,Sylviane Lagarrigue,Yoan Arribat,Adrien Martinotti,Ammar Ebrahimi,Jean Daraspe,Lluis Fajas,Francesca Amati

Nature 632:1110-1117 PubMed39169179

2024

Lysosomes drive the piecemeal removal of mitochondrial inner membrane.

Applications

Unspecified application

Species

Unspecified reactive species

Akriti Prashar,Claudio Bussi,Antony Fearns,Mariana I Capurro,Xiaodong Gao,Hiromi Sesaki,Maximiliano G Gutierrez,Nicola L Jones

iScience 27:109874 PubMed38784001

2024

Systemic phospho-defective and phospho-mimetic Drp1 mice exhibit normal growth and development with altered anxiety-like behavior.

Applications

Unspecified application

Species

Unspecified reactive species

Arisa Ikeda,Miho Iijima,Hiromi Sesaki
View all publications

Product promise

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