Recombinant Human SDHAF1 protein is a Human Full Length protein, in the 1 to 115 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
M G S S H H H H H H S S G L V P R G S H M G S M S R H S R L Q R Q V L S L Y R D L L R A G R G K P G A E A R V R A E F R Q H A G L P R S D V L R I E Y L Y R R G R R Q L Q L L R S G H A T A M G A F V R P R A P T G E P G G V G S Q P D D G D S P R N P H D S T G A P E T R P D G R
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Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:19465911, PubMed:24954417). Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants (PubMed:24954417). May act together with SDHAF3 (PubMed:24954417). Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241).
LYRM8, SDHAF1, SDH assembly factor 1, LYR motif-containing protein 8
Recombinant Human SDHAF1 protein is a Human Full Length protein, in the 1 to 115 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE, MS.
pH: 7.4
Constituents: 69% PBS, 30% Glycerol (glycerin, glycerine), 0.03% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.002% PMSF
ab187429 was purified using conventional chromatography techniques.
Plays an essential role in the assembly of succinate dehydrogenase (SDH), an enzyme complex (also referred to as respiratory complex II) that is a component of both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, and which couples the oxidation of succinate to fumarate with the reduction of ubiquinone (coenzyme Q) to ubiquinol (PubMed:19465911, PubMed:24954417). Promotes maturation of the iron-sulfur protein subunit SDHB of the SDH catalytic dimer, protecting it from the deleterious effects of oxidants (PubMed:24954417). May act together with SDHAF3 (PubMed:24954417). Contributes to iron-sulfur cluster incorporation into SDHB by binding to SDHB and recruiting the iron-sulfur transfer complex formed by HSC20, HSPA9 and ISCU through direct binding to HSC20 (PubMed:26749241).
Belongs to the complex I LYR family. SDHAF1 subfamily.
SDHAF1 also known as Succinate Dehydrogenase Complex Assembly Factor 1 plays an important role in the assembly and maturation of succinate dehydrogenase (SDH) which is part of Complex II in the mitochondrial respiratory chain. This protein with a molecular mass of approximately 13 kDa is found primarily in the mitochondria. Its expression is necessary for the proper function of SDH which catalyzes the oxidation of succinate to fumarate in the tricarboxylic acid (TCA) cycle and participates in the electron transport chain.
The interaction between SDHAF1 and other mitochondrial proteins ensures the correct assembly of the SDH complex. SDHAF1 acts as a chaperone in this process making sure that the flavoprotein subunit of SDH acquires its FAD cofactor. This assembly process is essential for maintaining cellular energy metabolism. By ensuring proper SDH complex formation SDHAF1 contributes to efficient energy production and cellular respiration.
SDHAF1's role affects both the TCA cycle and the mitochondrial electron transport chain. The protein supports the efficient execution of these two significant pathways. Through its regulation of SDH activity SDHAF1 impacts the pathway's ability to produce ATP from the reduction of electron carriers. It interacts closely with other mitochondrial proteins involved in these pathways including SDHA SDHB SDHC and SDHD the structural subunits of SDH complex ensuring cohesive function of this energy-producing sequence.
Defective function or mutations in SDHAF1 can lead to metabolic disorders such as Leigh syndrome which is a severe neurological disorder. Mutations might impair the formation of the SDH complex disrupting the mitochondrial energy production process. Alongside SDH subunits SDHAF1 dysfunction may also contribute to disorders linked to complex II deficiencies and associated with mitochondrial myopathies. Understanding the role of SDHAF1 offers significant insight into the pathogenesis and potential treatments of these mitochondrial-related conditions.
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15% SDS-PAGE analysis of ab187429 (3 μg).
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