| Field | Specification |
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| Activity | |
| Alternative Names | E3 ubiquitin-protein ligase HUWE1 (HUWE1); partial; (ARF-binding protein 1)(ARF-BP1)(HECT; UBA and WWE domain-containing protein 1)(HECT-type E3 ubiquitin transferase HUWE1)(Homologous to E6AP carboxyl terminus homologous protein 9)(HectH9)(Large structure of UREB1)(LASU1)(Mcl-1 ubiquitin ligase E3)(Mule)(Upstream regulatory element-binding protein 1)(URE-B1)(URE-binding protein 1) |
| Conjugate | |
| Endotoxin Level | |
| Expression System | |
| Form | Liquid or Lyophilized powder |
| Molecular Weight | |
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| Reconstitution | |
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| UniProt # |
Overview
Recombinant Human E3 ubiquitin-protein ligase HUWE1 (HUWE1), partial is a recombinant protein reagent derived from Homo sapiens (Human) and produced in E.coli. It is commonly used to support Cell Biology research by enabling enzyme activity assays, kinetics/structure–function studies and inhibitor or substrate screening in controlled in vitro settings.
Key elements and design rationale
- Expressed region: 4005-4374aa. Region selection can focus on functional domains, improve solubility, or isolate interaction surfaces for targeted studies.
- Expression system: E.coli. Expression host can influence folding and the presence/absence of post-translational modifications.
- Tag / fusion: N-terminal 10xHis-tagged and C-terminal Myc-tagged. Tags can support purification and detection; evaluate potential tag effects when studying sensitive interactions.
- Molecular weight (reported): 50.7 kDa. Apparent size may vary with tags, processing, and gel conditions.
When comparing results across batches or platforms, interpret signals in the context of construct design (region, tags) and expression host, especially for modification-dependent interactions.
Biological background
The gene commonly associated with this target is HUWE1. HUWE1 refers to a protein target that is studied across multiple biological contexts; annotations and nomenclature can vary by species and isoform. This product corresponds to the Homo sapiens (Human) sequence context, which can be important when comparing homologs or orthologs across model systems. For curated functional annotations, domains, and sequence features, consult primary databases (e.g., UniProt/NCBI) and the recent literature for the specific organism and isoform.
Research relevance and current trends
- Using recombinant proteins to enable quantitative binding measurements and reagent benchmarking.
- Studying domain- and isoform-specific effects in pathway models and interaction networks.
- Developing robust, reproducible assays that connect molecular readouts to cellular phenotypes.
Relevance: E3 ubiquitin-protein ligase which mediates ubiquitination and subsequent proteasomal degradation of target proteins. Regulates apoptosis by catalyzing the polyubiquitination and degradation of MCL1. Mediates monoubiquitination of DNA polymerase beta (POLB) at 'Lys-41', 'Lys-61' and 'Lys-81', thereby playing a role in base-excision repair. Also ubiquitinates the p53/TP53 tumor suppressor and core histones including H1, H2A, H2B, H3 and H4. Ubiquitinates MFN2 to negatively regulate mitochondrial fusion in response to decreased stearoylation of TFRC. Ubiquitination of MFN2 also takes place following induction of mitophagy; AMBRA1 acts as a cofactor for HUWE1-mediated ubiquitination. Regulates neural differentiation and proliferation by catalyzing the polyubiquitination and degradation of MYCN. May regulate abundance of CDC6 after DNA damage by polyubiquitinating and targeting CDC6 to degradation. Mediates polyubiquitination of isoform 2 of PA2G4. Acts in concert with MYCBP2 to regulate the circadian clock gene expression by promoting the lithium-induced ubiquination and degradation of NR1D1. Binds to an upstream initiator-like sequence in the preprodynorphin gene.
Common research applications
- Enzyme activity assays and kinetics measurements with defined substrates/cofactors.
- Inhibitor, activator, or substrate screening in biochemical assay formats.
- Structure–function analysis to interpret how sequence changes impact catalytic performance.
In quantitative assay development, changes in binding or activity readouts are typically interpreted relative to appropriate negative/positive controls and, where possible, orthogonal assay formats that support the same conclusion.
Notes for experimental interpretation
- Recombinant constructs may represent a defined region (domain) rather than the full-length protein; interpret results in the context of the expressed region.
- Tag or fusion elements can aid purification and detection but may influence binding surfaces or oligomerization; consider tag controls when relevant.
- Species and isoform differences can affect interaction partners and post-translational modifications; align experimental controls to the intended biological context.
- E. coli expression can limit eukaryotic post-translational modifications; for modification-dependent biology, interpret results accordingly.
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