Anti-SDHB Antibody Picoband® 31.0550 Vervoeging

SDHB (Succinate Dehydrogenase Complex, Subunit B, iron sulfur protein), also known as iron-sulfur subunit of complex II (Ip) or SDH2, HOMOLOG OF, is a protein that in humans is encoded by the SDHB gene. SDHB is one of four protein subunits forming succinate dehydrogenase, the other three being SDHA, SDHC and SDHD. The SDHB subunit is connected to the SDHA subunit on the hydrophilic, catalytic end of the SDH complex. The SDHB gene is mapped on 1p36.13. The entire SDHB transcript is encoded by 8 exons within approximately 40 kb by Au et al (1995) . Pollard et al. (2005) stated that the nuclear-encoded Krebs cycle enzymes fumarate hydratase and succinate dehydrogenases like SDHB act as tumor suppressors, and germline mutations in these genes predispose individuals to leiomyomas and renal cancer and to paragangliomas, respectively. In affected members of families with paragangliomas-4, mutations were identified in the SDHB gene.

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial;1.3.5.1; Iron-sulfur subunit of complex II; Ip; SDHB; SDH, SDH1

SDHB

6390

P21912

Human, Mouse, Rat

No cross-reactivity with other proteins

A synthetic peptide corresponding to a sequence at the N-terminus of human SDHB, different from the related rat sequence by one amino acid and mouse sequence by two amino acids.

Wide tissue distribution. Undetectable in placental tissue.

Flow Cytometry

Cancer, Cancer Metabolism, Cell Biology, Metabolic Signaling Pathway, Metabolism, Metabolism Of Carbohydrates, Mitochondrial, Mitochondrial Markers, Mitochondrial Metabolism, Oxidative Phosphorylation, Oxidative Stress, Pathways and Processes, Redox Metabolism, Signal Transduction

Immunogen affinity purified.

Liquid

Iron-sulfur protein (IP) 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) .

1. Au, H. C., Ream-Robinson, D., Bellew, L. A., Broomfield, P. L. E., Saghbini, M., Scheffler, I. E. Structural organization of the gene encoding the human iron-sulfur subunit of succinate dehydrogenase. Gene 159: 249-253, 1995. 2. Brouwers, F. M., Eisenhofer, G., Tao, J. J., Kant, J. A., Adams, K. T., Linehan, W. M., Pacak, K. High frequency of SDHB germline mutations in patients with malignant catecholamine-producing paragangliomas: implications for genetic testing. J. Clin. Endocr. Metab. 91: 4505-4509, 2006. 3. Pollard, P. J., Briere, J. J., Alam, N. A., Barwell, J., Barclay, E., Wortham, N. C., Hunt, T., Mitchell, M., Olpin, S., Moat, S. J., Hargreaves, I. P., Heales, S. J., and 9 others.Accumulation of Krebs cycle intermediates and over-expression of HIF1-alpha in tumours which result from germline FH and SDH mutations. Hum. Molec. Genet. 14: 2231-2239, 2005.

At -20 ̊C for one year from date of receipt. Avoid repeated freezing and thawing. Protect from light.

31630 MW

No cross reactivity with other proteins.

6

Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial

Mitochondrion inner membrane; Peripheral membrane protein; Matrix side.

Belongs to the succinate dehydrogenase/fumarate reductase iron-sulfur protein family.

Succinate dehydrogenase[ubiquinone] iron-sulfur subunit, mitochondrial

Rabbit IgG

Each vial contains 50% glycerol, 0.9% NaCl, 0.2% Na2HPO4, 0.02% NaN3.