Analytical Data
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Gene name
SMURF2
- Application
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Alternative Names
SMAD ubiquitination regulatory factor 2SMAD-specific E3 ubiquitin-protein ligase 2
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HAU4
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Expression Region
1-748aa
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Molecular Weight
113.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
SMURF2 (SMAD Ubiquitination Regulatory Factor 2) is a pivotal component of the TGF-β signaling pathway, playing a crucial role in regulating the ubiquitination and degradation of SMAD proteins, which are key mediators of this pathway. Research on SMURF2 has gained significant attention due to its involvement in various biological processes, including cellular differentiation, epithelial-to-mesenchymal transition (EMT), and oncogenesis. Dysregulation of SMURF2 has been implicated in several diseases, particularly in cancer, where it can influence tumor progression and metastasis by modulating TGF-β signaling. Consequently, the study of SMURF2 recombinant proteins has become increasingly important for understanding its functional mechanisms, interactions with other proteins, and potential as a therapeutic target. By expressing and purifying SMURF2 as a recombinant protein, researchers can investigate its structure, study its enzymatic activity, and elucidate its role in cellular signaling pathways. This approach facilitates the development of small molecules or antibodies aimed at modulating SMURF2 activity, which could lead to novel strategies for cancer treatment and other diseases associated with TGF-β signaling dysregulation. Overall, the robust study of SMURF2 recombinant proteins holds promise for advancing our understanding of its biological roles and potential therapeutic implications.
