Anti-2SC antibody
Description
Application Data
Description
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Detects succinated cysteine residues on succinated proteins with high affinity
Application Data
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Catalogue number | crb2005017 |
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Antibody | Anti-2SC antibody |
Antigen Peptide | KLH conjugated S-(2-succinyl)-cysteine |
Aliases | S-(2-succinyl)-cysteine |
Host Species | Anti-Rabbit |
Antibody Type | Polyclonal |
Concentration | 1mg/ml TEA eluate (Rb 6773), 0.4mg/ml TEA (Rb 6772), 2mg/ml Glycine (Rb 6774) |
Validation | Rb 6773: WB (1:200), ELISA (I:1000), IHC (1:2000), Rb 6772: IHC (1:400), Rb 6774: ELISA (1:1000) |
Target | 2SC |
Storage Stabilisers | This material is supplied in PBS containing 0.01% sodium azide and 1% trehalose. The product should be stored at +4°C for short term storage and -20°C for long term storage. Avoid repeated freeze/ thaw cycles. |
Disease Area | Cancer Biology, Diabetes, Obesity, Renal cancer |
Specificity | Succinated cysteine residues |
Post-translational Modification | Succination |
Citations | Burgener et al., (2019). SDHA gain-of-function engages inflammatory mitochondrial retrograde signaling via KEAP1-Nrf2. Nat Immunol. 20(10):1311-1321. PMID: 31527833 Casey et al., (2020). Fumarate Metabolic Signature for the Detection of Reed Syndrome in Humans.Clin Cancer Res. 26(2):391-396. PMID: 31636096. doi: 10.1158/1078-0432. Hum Pathol. PMID: 32681944. doi: 10.1016/j.humpath.2020.07.014. Secondary Renal Neoplasia Following Chemotherapy or Radiation in Pediatric Patients.Äyräväinen et al., (2020). Systematic molecular and clinical analysis of uterine leiomyomas from fertile-aged women undergoing myomectomy. Human Reproduction. deaa187, https://doi.org/10.1093/humrep/deaa187 Kiyozawa et al., (2022) Approach for reclassification of collecting duct carcinoma and comparative histopathological analysis with SMARCB1/INI1-deficient renal cell carcinoma and fumarate hydratase-deficient renal cell carcinoma. Hum Pathol. https://doi.org/10.1016/j.humpath.2022.03.002
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References | Alderson, N., Wang, Y., Blatnik, M., Frizzell, N., Walla, M., Lyons, T., Alt, N., Carson, J., Nagai, R., Thorpe, S. and Baynes, J. (2006). S-(2-Succinyl)cysteine: A novel chemical modification of tissue proteins by a Krebs cycle intermediate. Arch Biochem Biophys, 450(1), 1-8. PMID: 16624247
Nagai, R., Brock, J., Blatnik, M., Baatz, J., Bethard, J., Walla, M., Thorpe, S., Baynes, J. and Frizzell, N. (2007). Succination of Protein Thiols during Adipocyte Maturation: a biomarker of mitochondrial stress. J Biol Chem, 282(47), 34219-34228. PMID: 17726021
Merkley, E., Metz, T., Smith, R., Baynes, J. and Frizzell, N. (2013). The succinated proteome. Mass Spectrom Rev, 33(2), 98-109. PMID: 24115015
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Succination is a stable post-translational modification of cysteine residues, which modifies protein function or turnover in response to a changing intracellular redox environment. Succination occurs when the Krebs cycle intermediate, fumarate, reacts with cysteine yielding S-(2-succino)cysteine (2SC).
A wide range of proteins are subject to succination, including enzymes, adipokines, cytoskeletal proteins and ER chaperones and succination has been shown to have roles in regulatory biology.
An increase in succination of adipocyte proteins is seen in diabetes mellitus and results from nutrient excess derived mitochondrial stress. 2SC therefore serves as a biomarker of mitochondrial stress or dysfunction in chronic diseases, such as obesity, diabetes, and cancer.