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Complex II of the respiratory chain, which is specifically involved in the oxidation of succinate, carries electrons from FADH to CoQ. Additionally we are shipping Succinate Dehydrogenase Complex, Subunit B, Iron Sulfur (Ip) Antibodies (143) and Succinate Dehydrogenase Complex, Subunit B, Iron Sulfur (Ip) Kits (9) and many more products for this protein.
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sdhB mutant is hypersensitive to oxygen and displays hallmarks of a progeroid syndrome
The overall penetrance of succinate dehydrogenase B (SDHB) mutations is estimated to be 21% at age 50 and 42% at age 70 when adequately corrected for ascertainment.
Germline SDHB mutation is associated with Pheochromocytoma and Paraganglioma.
Data suggest that low expression of SDHB in metastatic lesions is associated with longer overall survival in patients with advanced ileal well-differentiated neuroendocrine tumors with lymph node or liver metastases.
Results identified a high frequency of germline mutation in SDHB gene in patients presenting with bladder paraganglioma.
automation, reproducibility, and cost efficiency of SDHB IHC offer advantages over the labor-intensive histochemical method requiring frozen sections
We report a unique case of an SDH (show SARDH Proteins)-deficient GIST case with an activating PDGFRA (show PDGFRA Proteins) mutation. Oncogenic mutations in GIST are generally mutually exclusive; however documented exceptions exist which may have diagnostic and therapeutic implications.
Mutation in the SDHB gene is associated with mediastinal paraganglioma.
We report for the first time the presence of both TFE3 (show TFE3 Proteins) translocation and SDHB mutation in the same renal cell carcinoma (show MOK Proteins) tumor.
Heterozygous germ line mutations in SDHB neutrophil survival is independent of HIF-1alpha (show HIF1A Proteins) expression and linked to uncoupling of the mitochondrial electron transport chain.
miR (show MLXIP Proteins)-142-5p up-regulation in colorectal cancer probably facilitates generation of aerobic glycolysis by reducing SDHB expression.
tissue expression analysis indicated that that swine SDHB, SNRPA (show SNRPA Proteins) and CRYBB1 (show CRYBB1 Proteins) gene were differentially expressed in tissues including fat, lung, muscle, small intestine, kidney, large intestine, spleen and liver
Data show that lack of succinate dehydrogenase (SDH (show SDHA Proteins)) activity commits cells to consume extracellular pyruvate.
Using Sdhb(+/-) mice, we provide evidence that pituitary hyperplasia in SDHx-deficient cells may be the initial abnormality in the cascade of events leading to pituitary adenoma formation.
Tumor-derived FH and SDH (show SDS Proteins) mutations accumulate fumarate and succinate, leading to enzymatic inhibition of multiple alpha-KG-dependent dioxygenases and consequent alterations of genome-wide histone and DNA methylation (show HELLS Proteins).
Data show that two subunits of complex II (succinate dehydrogenase (show SDHD Proteins), or SDH (show SDS Proteins)), SDHA (show SDHA Proteins) and SDHB, interacted specifically with SIRT3 (show SIRT3 Proteins).
Complex II of the respiratory chain, which is specifically involved in the oxidation of succinate, carries electrons from FADH to CoQ. The complex is composed of four nuclear-encoded subunits and is localized in the mitochondrial inner membrane. The iron-sulfur subunit is highly conserved and contains three cysteine-rich clusters which may comprise the iron-sulfur centers of the enzyme. Sporadic and familial mutations in this gene result in paragangliomas and pheochromocytoma, and support a link between mitochondrial dysfunction and tumorigenesis.
succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial
, succinate dehydrogenase complex subunit B
, COMPLEX II: iron-sulfur subunit
, iron-sulfur protein subunit of succinate dehydrogenase
, succinate dehydrogenase
, succinate dehydrogenase B
, succinate dehydrogenase Iron-sulfur
, succinate dehydrogenase Iron-sulfur protein
, succinate dehydrogenase iron protein
, succinate dehydrogenase subunit b
, iron-sulfur subunit of complex II
, Iron-sulfur subunit of complex II