Recombinant Human SDOS protein
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Recombinant Human SDOS protein is a Human Full Length protein, in the 1 to 211 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
SDOS, TIRR, NUDT16L1, Tudor-interacting repair regulator protein, NUDT16-like protein 1, Protein syndesmos
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human SDOS protein (AB104670)
15% SDS-PAGE showing ab104670 at approximately 25.5kDa (3μg).
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The SDOS protein contributes significantly to cellular respiration and energy production. It participates in the succinate dehydrogenase complex an important component of the citric acid cycle and the mitochondrial electron transport chain. Within the complex SDOS contributes to the oxidation of succinate to fumarate and the concomitant reduction of ubiquinone. This protein interplays with other complex subunits to facilitate efficient electron flow and ATP synthesis.
Pathways
SDOS plays a significant role in the tricarboxylic acid (TCA) cycle and oxidative phosphorylation pathways. These pathways are critical for aerobic respiration and energy production. SDOS interacts with other components of the succinate dehydrogenase complex such as SDHA and SDHB to link the TCA cycle with the electron transport chain. This connection allows cells to maintain an efficient energy balance and respond to metabolic demands.
Specifications
Form
Liquid
Additional notes
ab104670 is purified by using anion-exchange chromatography (DEAE sepharose resin) and gel-filtration chromatography (Sephacryl S-200) with 20mM Tris pH 7.5, 2mM EDTA.
General info
Function
Key regulator of TP53BP1 required to stabilize TP53BP1 and regulate its recruitment to chromatin (PubMed : 28241136). In absence of DNA damage, interacts with the tandem Tudor-like domain of TP53BP1, masking the region that binds histone H4 dimethylated at 'Lys-20' (H4K20me2), thereby preventing TP53BP1 recruitment to chromatin and maintaining TP53BP1 localization to the nucleus (PubMed : 28241136). Following DNA damage, ATM-induced phosphorylation of TP53BP1 and subsequent recruitment of RIF1 leads to dissociate NUDT16L1/TIRR from TP53BP1, unmasking the tandem Tudor-like domain and allowing recruitment of TP53BP1 to DNA double strand breaks (DSBs) (PubMed : 28241136). Binds U8 snoRNA (PubMed : 18820299).
Sequence similarities
Belongs to the Nudix hydrolase family. TIRR subfamily.
Subcellular localisation
Nucleus
Target data
Product promise
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