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SDHB Blocking Peptide (C-term)
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P21912 |
|---|---|
| Other Accession | Q007T0, Q9CQA3, Q3T189, NP_002991.2 |
| Gene ID | 6390 |
|---|---|
| Other Names | Succinate dehydrogenase [ubiquinone] iron-sulfur subunit, mitochondrial, Iron-sulfur subunit of complex II, Ip, SDHB, SDH, SDH1 |
| Target/Specificity | The synthetic peptide sequence is selected from aa 220-234 of HUMAN SDHB |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | SDHB |
|---|---|
| Synonyms | SDH, SDH1 |
| Function | Iron-sulfur protein (IP) subunit of the succinate dehydrogenase complex (mitochondrial respiratory chain complex II), responsible for transferring electrons from succinate to ubiquinone (coenzyme Q). |
| Cellular Location | Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9YHT2}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q9YHT2}; Matrix side {ECO:0000250|UniProtKB:Q9YHT2} |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Shimada, M., et al. Hum. Genet. 128(4):433-441(2010)
Bailey, S.D., et al. Diabetes Care 33(10):2250-2253(2010)
Cerecer-Gil, N.Y., et al. Clin. Cancer Res. 16(16):4148-4154(2010)
Schimke, R.N., et al. Am. J. Med. Genet. A 152A (6), 1531-1535 (2010) :
Hes, F.J., et al. BMC Med. Genet. 11, 92 (2010) :
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