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AB228560

Succinate Dehydrogenase Activity Assay Kit (Colorimetric)

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(25 Publications)

Succinate Dehydrogenase Activity Assay Kit (Colorimetric) ab228560 is a simple and rapid assay for the measurement of Succinate Dehydrogenase activity. Readout on any colorimetric (650 nm) plate reader.

- Kit includes standard curve for quantitation, and SDH enzyme positive control

View Alternative Names

SDH2, SDHF, SDHA, Flavoprotein subunit of complex II, Malate dehydrogenase [quinone] flavoprotein subunit, Fp

2 Images
Functional Studies - Succinate Dehydrogenase Activity Assay Kit (Colorimetric) (AB228560)
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Supplier Data

Functional Studies - Succinate Dehydrogenase Activity Assay Kit (Colorimetric) (AB228560)

Typical standard curve and assay data.

(a) DCIP standard curve, (b) typical assay data and (c) succinate dehydrogenase activity in mitochondria isolated from mouse heart (24 μg) and liver (70 μg).

Schematic Diagram - Succinate Dehydrogenase Activity Assay Kit (Colorimetric) (AB228560)
  • Schematic Diagram

Supplier Data

Schematic Diagram - Succinate Dehydrogenase Activity Assay Kit (Colorimetric) (AB228560)

Representative image of Succinate Dehydrogenase Activity Assay Kit (Colorimetric) ab228560

Components shown from left to right :

- DCIP Standard

- Electron Probe

- SDH Positive Control

- SDH Substrate Mix

- SDH Assay Buffer

Note : The vial labels shown in this image use generic names for illustrative purposes only and may not exactly match the specific component names included in the kit.

Note : Colors of solutions in image may not precisely match the shade of colors in the actual kit.

Key facts

Detection method

Colorimetric

Sample types

Cell culture extracts, Tissue Homogenate

Assay type

Enzyme activity (quantitative)

Sensitivity

< 0.1 mU/well

Assay Platform

Microplate reader

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "Enzyme activity assay": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Product details

How the assay works

In Succinate Dehydrogenase Activity Assay Kit (Colorimetric), Succinate Dehydrogenase converts succinate to fumarate, and transfers the electron to an artificial electron acceptor (Probe), which changes the color from blue to a colorless product (depending upon the sample enzymatic activity).

Succinate Dehydrogenase Activity Assay Kit (Colorimetric) protocol summary:

- Rapidly homogenize sample tissue / cells in assay buffer
- Centrifuge sample and transfer supernatant to fresh tube
- Add sample to plate well
- Add reaction buffer and mix well
- Immediately measure absorbance (600 nm) in kinetic mode for 10 –30 minutes at 25°C

The kit provides enough reagents for 100 assays.

How other researchers are using

Succinate Dehydrogenase Activity Assay Kit (Colorimetric) has been used in a variety of sample type including:
- Mouse liver mitochondria 1
- Rat brain tissues 2
- HepG2 and MCF-7 cells 3
References: 1-Rome F al. 2022
2 Almohaimeed H et al. 2022
3- Liu X et al. 2021

This product is manufactured by BioVision, an Abcam company and was previously called K660 Succinate Dehydrogenase Activity Colorimetric Assay Kit. K660-100 is the same size as the 100 test size of ab228560.

Succinate Dehydrogenase (SDH) (EC 1.3.5.1) or succinate-coenzyme Q reductase (SQR) or respiratory complex II is an enzyme complex, which is bound to the inner mitochondrial membrane. SDH participates in both the citric acid cycle and electron transport chain. In mammals and many bacteria, SDH consists of 2 hydrophilic subunits, SDHA (flavoprotein) and SDHB (iron-sulfur protein) and 2 hydrophobic membrane anchor subunits: SDHC and SDHD. SDH oxidizes succinate to fumarate and transfers the electrons to ubiquinone. SDH deficiency in humans leads to a variety of phenotypes including Leigh syndrome, a neurometabolic disorder, tumor formation, and myopathy. Recent studies show that SDH can prevent the generation of ROS (reactive oxygen species); therefore, measurement of succinate dehydrogenase activity has wide applications.

The Safety Datasheet for this product has been updated for certain countries. Please check the current version in the Support and downloads section.

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What's included?

{ "values": { "100Test": { "sellingSize": "100 Test", "publicAssetCode":"ab228560-100Test", "assetComponentDetails": [ { "size":"1 x 1 Vial", "name":"SDH Positive Control", "number":"AB228560-CMP03", "productcode":"" }, { "size":"1 x 0.4 mL", "name":"DCIP Standard", "number":"AB228560-CMP01", "productcode":"" }, { "size":"1 x 1 Each", "name":"SDH Substrate Mix", "number":"AB228560-CMP05", "productcode":"" }, { "size":"1 x 0.2 mL", "name":"Electron Probe", "number":"AB228560-CMP04", "productcode":"" }, { "size":"1 x 25 mL", "name":"SDH Assay Buffer", "number":"AB228560-CMP02", "productcode":"" } ] } } }
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Storage information
-20°C
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

Complex II also known as succinate dehydrogenase (SDH) or succinate-ubiquinone oxidoreductase plays an important mechanical role in the mitochondrial electron transport chain. It catalyzes the oxidation of succinate to fumarate while reducing ubiquinone to ubiquinol. The enzyme complex is approximately 140 kDa in mass and resides in the inner mitochondrial membrane. Complex II is expressed in most tissues particularly in high-energy demand tissues such as the heart and skeletal muscles.
Biological function summary

Complex II functions as part of the larger electron transport chain complex and plays a role in the Krebs cycle. It links two critical metabolic pathways converting succinate to fumarate while transferring electrons to the electron transport chain. This makes it integral for proper cellular respiration and energy production. The complex consists of multiple subunits and utilizes co-factors like FAD and iron-sulfur clusters for enzymatic activity. It is also a part of the supercomplexes that optimize the efficiency of oxidative phosphorylation.

Pathways

Complex II plays a significant role in both the citric acid cycle and oxidative phosphorylation. It acts as a connecting bridge between these two pathways facilitating the flow of electrons. Complex II works alongside other proteins such as complex I and complex III to maintain the electron transport chain's function and energy production. Succinate dehydrogenase transfers electrons within the chain directly affecting the generation of ATP by complex V (ATP synthase).

Dysfunction of complex II is associated with mitochondrial diseases and cancers. Mutations or deficiencies in its subunits can lead to conditions like Leigh syndrome and hereditary paraganglioma. These conditions frequently involve other mitochondrial proteins and complexes such as complex I which can exacerbate the electron transport chain dysfunction. In cancers alterations in succinate dehydrogenase activity can result in oncogenic metabolisms by falsely stabilizing hypoxia-inducible factors linking it further with the genetic and metabolic regulation.
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Product protocols

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Target data

Flavoprotein (FP) subunit of succinate dehydrogenase (SDH) that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from succinate to ubiquinone (coenzyme Q) (PubMed : 10746566, PubMed : 24781757). SDH also oxidizes malate to the non-canonical enol form of oxaloacetate, enol-oxaloacetate (By similarity). Enol-oxaloacetate, which is a potent inhibitor of the succinate dehydrogenase activity, is further isomerized into keto-oxaloacetate (By similarity). Can act as a tumor suppressor (PubMed : 20484225).
See full target information SDHA
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Publications (25)

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

Nature communications 16:3373 PubMed40204764

2025

Cross-talks between Metabolic and Translational Controls during Beige Adipocyte Differentiation.

Applications

Unspecified application

Species

Unspecified reactive species

Daehwa Youn,Boseon Kim,Dahee Jeong,Ju Yeon Lee,Seha Kim,Dulguun Sumberzul,Rehna Paula Ginting,Min-Woo Lee,Ju Hwan Song,Ye Seul Park,Yumin Kim,Chang-Myung Oh,Mihye Lee,Jun Cho

Nature cardiovascular research 3:1123-1139 PubMed39195859

2024

An engineered human cardiac tissue model reveals contributions of systemic lupus erythematosus autoantibodies to myocardial injury.

Applications

Unspecified application

Species

Unspecified reactive species

Sharon Fleischer,Trevor R Nash,Manuel A Tamargo,Roberta I Lock,Gabriela Venturini,Margaretha Morsink,Pamela L Graney,Vanessa Li,Morgan J Lamberti,Martin Liberman,Youngbin Kim,Daniel N Tavakol,Richard Z Zhuang,Jaron Whitehead,Richard A Friedman,Rajesh K Soni,Jonathan G Seidman,Christine E Seidman,Laura Geraldino-Pardilla,Robert Winchester,Gordana Vunjak-Novakovic

FASEB journal : official publication of the Federation of American Societies for Experimental Biology 38:e23718 PubMed38847487

2024

Loss of endogenous estrogen alters mitochondrial metabolism and muscle clock-related protein Rbm20 in female mdx mice.

Applications

Unspecified application

Species

Unspecified reactive species

Cara A Timpani,Didier Debrincat,Stephanie Kourakis,Rebecca Boyer,Luke E Formosa,Joel R Steele,Haijian Zhang,Ralf B Schittenhelm,Aaron P Russell,Emma Rybalka,Angus Lindsay

Nature communications 15:2176 PubMed38467649

2024

YTHDF2 governs muscle size through a targeted modulation of proteostasis.

Applications

Unspecified application

Species

Unspecified reactive species

Christopher J Gilbert,Charles P Rabolli,Volha A Golubeva,Kristina M Sattler,Meifang Wang,Arsh Ketabforoush,W David Arnold,Christoph Lepper,Federica Accornero

Pflugers Archiv : European journal of physiology 476:939-948 PubMed38446167

2024

Locally applied heat stress during exercise training may promote adaptations to mitochondrial enzyme activities in skeletal muscle.

Applications

Unspecified application

Species

Unspecified reactive species

Ed Maunder,Andrew King,Jeffrey A Rothschild,Matthew J Brick,Warren B Leigh,Christopher P Hedges,Troy L Merry,Andrew E Kilding

Scientific reports 12:21213 PubMed36481816

2022

Gum Arabic nanoformulation rescues neuronal lesions in bromobenzene-challenged rats by its antioxidant, anti-apoptotic and cytoprotective potentials.

Applications

Unspecified application

Species

Unspecified reactive species

Hailah M Almohaimeed,Hanan Waly,Nasser S Abou Khalil,Khaled M A Hassanein,Basal Sulaiman M Alkhudhairy,Elham A Abd-Allah

Biotechnology and bioengineering 120:409-425 PubMed36225115

2022

Selection of synthetic proteins to modulate the human frataxin function.

Applications

Unspecified application

Species

Unspecified reactive species

María Florencia Pignataro,María Georgina Herrera,Natalia Brenda Fernández,Martín Aran,Hernán Gustavo Gentili,Fernando Battaglini,Javier Santos

Cell death & disease 13:660 PubMed35902556

2022

The hexokinase "HKDC1" interaction with the mitochondria is essential for liver cancer progression.

Applications

Unspecified application

Species

Unspecified reactive species

Md Wasim Khan,Alexander R Terry,Medha Priyadarshini,Vladimir Ilievski,Zeenat Farooq,Grace Guzman,Jose Cordoba-Chacon,Issam Ben-Sahra,Barton Wicksteed,Brian T Layden

Molecular metabolism 58:101452 PubMed35121169

2022

Disrupted liver oxidative metabolism in glycine N-methyltransferase-deficient mice is mitigated by dietary methionine restriction.

Applications

Unspecified application

Species

Unspecified reactive species

Ferrol I Rome,Curtis C Hughey

Signal transduction and targeted therapy 6:375 PubMed34728602

2021

The existence of a nonclassical TCA cycle in the nucleus that wires the metabolic-epigenetic circuitry.

Applications

Unspecified application

Species

Unspecified reactive species

Xujun Liu,Wenzhe Si,Lin He,Jianguo Yang,Yani Peng,Jie Ren,Xiaoping Liu,Tong Jin,Huajing Yu,Zihan Zhang,Xiao Cheng,Wenting Zhang,Lu Xia,Yunchao Huang,Yue Wang,Shumeng Liu,Lin Shan,Yu Zhang,Xiaohan Yang,Haixia Li,Jing Liang,Luyang Sun,Yongfeng Shang
View all publications
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