- Tel: 858.663.9055
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Email: info@nsjbio.com
- Tel: 858.663.9055
- Email: info@nsjbio.com
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SDHB Antibody / Complex II Iron-Sulfur Subunit Antibody detects SDHB, an essential component of succinate dehydrogenase, or mitochondrial respiratory Complex II. SDHB is encoded by the nuclear SDHB gene and forms the iron-sulfur subunit of the four-component succinate dehydrogenase complex located in the inner mitochondrial membrane. Complex II has the distinctive role of participating in both the tricarboxylic acid (TCA) cycle and the mitochondrial electron transport chain, linking cellular carbon metabolism directly to oxidative phosphorylation.
Succinate dehydrogenase catalyzes the oxidation of succinate to fumarate during the TCA cycle. Electrons generated during this reaction are transferred through flavin adenine dinucleotide in the SDHA catalytic subunit and subsequently through iron-sulfur clusters contained within SDHB. SDHB then facilitates electron transfer toward ubiquinone through the membrane-associated SDHC and SDHD subunits. Unlike several other respiratory chain complexes, Complex II does not directly pump protons across the inner mitochondrial membrane.
The iron-sulfur centers of SDHB are essential for efficient electron transfer through Complex II. Proper assembly and function of SDHB therefore contribute to mitochondrial respiration, cellular energy production and maintenance of metabolic homeostasis. Impaired succinate dehydrogenase activity can alter mitochondrial electron transport and lead to accumulation of succinate. Because succinate participates in metabolic signaling as well as intermediary metabolism, disruption of Complex II can have effects extending beyond ATP production.
SDHB has particular importance in cancer and mitochondrial disease research. Loss-of-function alterations affecting SDHB can impair succinate dehydrogenase activity and cause intracellular succinate accumulation. Elevated succinate can influence oxygen-sensing pathways and cellular transcriptional programs by inhibiting alpha-ketoglutarate-dependent enzymes. These metabolic changes have contributed to the classification of succinate as an oncometabolite in the context of SDH-deficient tumors.
Germline and somatic alterations affecting SDHB have been investigated extensively in pheochromocytoma, paraganglioma and several other tumor types. Loss of SDHB protein expression by immunohistochemical analysis can also serve as an indicator of dysfunction within the succinate dehydrogenase complex. Beyond oncology, SDHB and other Complex II components are studied in mitochondrial disorders, oxidative stress, metabolic regulation and mechanisms controlling cellular respiration.
NSJ Bioreagents offers SDHB Antibody reagents for investigating the expression and localization of this mitochondrial respiratory chain component. A Complex II Iron-Sulfur Subunit Antibody can support research into mitochondrial respiration, TCA cycle metabolism, electron transport, SDH-deficient tumors and the broader biological consequences of altered succinate dehydrogenase function.
Researchers studying SDHB in mitochondrial respiration and energy metabolism can explore our Mitochondria Marker Antibody page for additional targets involved in mitochondrial function, oxidative phosphorylation and cellular metabolism.
Optimal dilution of the SDHB Antibody / Complex II Iron-Sulfur Subunit Antibody should be determined by the researcher.
A recombinant human protein corresponding to amino acids A29-V280 was used as the immunogen for the SDHB antibody.
After reconstitution, the SDHB antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
SDHB antibody, Complex II Iron-Sulfur Subunit antibody, Succinate Dehydrogenase B antibody, Succinate Dehydrogenase Iron-Sulfur Subunit antibody, Iron-Sulfur Subunit of Complex II antibody, SDH2 antibody, IP antibody
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