Lane 1: human liver
Lane 2: mouse liver
Lane 3: rat liver
Lane 4: rat liver, preincubated with the immunization protein.
Rabbit polyclonal primary
SDHB Antibody (ER1803-63)
Recombinant protein within human sdhb aa 100-300.
Rat liver tissue, human liver tissue, mouse liver tissue, 293T, HT-29, rat heart tissue, human kidney tissue, human skin tissue, mouse colon tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Protein affinity purified.
CWS2 antibody; DHSB_HUMAN antibody; FLJ92337 antibody; Ip antibody; Iron sulfur subunit antibody; Iron sulfur subunit of complex II antibody; Iron-sulfur subunit of complex II antibody; mitochondrial antibody; PGL 4 antibody; PGL4 antibody; SDH 1 antibody; SDH antibody; SDH1 antibody; SDH2 antibody; SDH2, homolog of antibody; SdhB antibody; SDHIP antibody; Succinate dehydrogenase [ubiquinone] iron sulfur protein mitochondrial antibody; Succinate dehydrogenase [ubiquinone] iron sulfur subunit antibody; Succinate dehydrogenase [ubiquinone] iron-sulfur subunit antibody; succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial antibody; Succinate Dehydrogenase 1 Iron Sulfur Subunit antibody; Succinate Dehydrogenase 2, S. cerevisiae, homolog of antibody; Succinate dehydrogenase complex iron sulfur subunit B antibody; Succinate dehydrogenase complex subunit B iron sulfur antibody; Succinate Dehydrogenase Complex Subunit B Iron Sulfur Protein antibody; succinate dehydrogenase complex, subunit B, iron sulfur (Ip) antibody; Succinate dehydrogenase iron sulfur protein antibody
Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.
In aerobic respiration reactions, succinate dehydrogenase (SDH) catalyzes the oxidation of succinate and ubiquinone to fumarate and ubiquinol. Four subunits comprise the SDH protein complex: a flavochrome subunit (SDHA), an iron-sulfur protein (SDHB) and two membrane-bound subunits (SDHC and SDHD) anchored to the inner mitochondrial membrane. Mutations to these subunits cause mitochondrial dysfunction, corresponding to several distinct disorders. Mutations in the membrane bound components may cause hereditary paraganglioma, while SDHA mutations associate with juvenile encephalopathy as well as Leigh syndrome, a severe neurological disorder. Inactivating mutations in SDHB correlate with inherited, but not necessarily sporadic, cases of pheochromocytoma.