Recombinant human SMURF 2 protein (DDDDK tag N-Terminus)
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Recombinant human SMURF 2 protein (DDDDK tag N-Terminus) is a Human Fragment protein, in the 130 to 748 aa range, expressed in Baculovirus infected insect cells, with >80%, suitable for SDS-PAGE, FuncS.
View Alternative Names
E3 ubiquitin-protein ligase SMURF2, hSMURF2, HECT-type E3 ubiquitin transferase SMURF2, SMAD ubiquitination regulatory factor 2, SMAD-specific E3 ubiquitin-protein ligase 2, SMURF2
- FuncS
Unknown
Functional Studies - Recombinant human SMURF 2 protein (DDDDK tag N-Terminus) (AB95930)
Image showing specific activity of ab95930.
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant human SMURF 2 protein (DDDDK tag N-Terminus) (AB95930)
10% SDS-PAGE
Lane 1 : ab95930 (4μg)
Lane 2 : Molecular weight markers
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
SMURF2 regulates many cell signaling pathways including the TGF-beta/Smad pathway. It associates with SMAD proteins to control their stability and activity acting as a negative regulator to modulate TGF-beta signaling. By promoting the ubiquitination and degradation of receptor-regulated SMADs (R-SMADs) SMURF2 impacts cellular responses to growth factors. This regulatory mechanism is important for maintaining cellular proliferation differentiation and apoptosis.
Pathways
The function of SMURF2 significantly influences the TGF-beta and BMP signaling pathways both critical in controlling cell growth and differentiation. These pathways involve interactions with other proteins like SMAD7 and SMAD2. SMURF2 interacts with SMAD7 an inhibitory SMAD to regulate Smad-dependent transcriptional responses ensuring the fine-tuning of signal transduction. These pathways' balance and regulation are vital for appropriate cellular function and response.
Specifications
Form
Liquid
Additional notes
Affinity purified.
General info
Function
E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates (PubMed : 11016919, PubMed : 38016474). Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradation, thereby down-regulating TGF-beta signaling (PubMed : 11163210, PubMed : 12717440, PubMed : 21791611). In addition, interaction with SMAD7 activates autocatalytic degradation, which is prevented by interaction with AIMP1 (PubMed : 18448069). Also forms a stable complex with TGF-beta receptor-mediated phosphorylated SMAD1, SMAD2 and SMAD3, and targets SMAD1 and SMAD2 for ubiquitination and proteasome-mediated degradation (PubMed : 11016919, PubMed : 11158580, PubMed : 11389444). SMAD2 may recruit substrates, such as SNON, for ubiquitin-dependent degradation (PubMed : 11389444). Negatively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation (PubMed : 30696809). Acts as an activator of ferroptosis by mediating ubiquitination and degradation of GSTP1, thereby preventing detoxification of 4-hydroxynonenal (4-HNE) reactive aldehyde (PubMed : 38016474).. (Microbial infection) In case of filoviruses Ebola/EBOV and Marburg/MARV infection, the complex formed by viral matrix protein VP40 and SMURF2 facilitates virus budding.
Post-translational modifications
Auto-ubiquitinated and ubiquitinated in the presence of RNF11 and UBE2D1 (PubMed:19343052, PubMed:30696809). Ubiquitinated by the SCF(FBXL15) complex and TTC3, leading to its degradation by the proteasome (PubMed:21572392, PubMed:30696809). 'Lys-48'-linked polyubiquitination mediated by TRAF4 at Lys-119 leads to SMURF2 proteasomal degradation (PubMed:31076633).
Subcellular localisation
Nucleus
Target data
Product promise
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