Analytical Data
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Gene name
SUMO2
- Application
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Alternative Names
HSMT3; SMT3B; SMT3H2; SUMO-3; Sentrin-2; Ubiquitin-like protein SMT3B
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
P61956
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Expression Region
Met1~Tyr95
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Molecular Weight
45kDa
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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
SUMO2 (Small Ubiquitin-like Modifier 2) is a member of the SUMO (Small Ubiquitin-like Modifier) family, which plays a crucial role in post-translational modification processes known as SUMOylation. This modification regulates various cellular functions, including protein stability, localization, and interactions, thereby influencing crucial biological processes such as DNA repair, cell cycle progression, and stress responses. Research has shown that SUMO2 is particularly involved in the regulation of transcriptional activity and has implications in various diseases, including cancer and neurodegenerative disorders. The study of SUMO2-recombinant proteins aims to elucidate its functional mechanisms, interactions with specific target proteins, and potential therapeutic applications. By generating SUMO2 in a recombinant form, researchers can investigate its structure-function relationships more effectively and determine how alterations in SUMO2 levels may contribute to disease pathogenesis. Furthermore, understanding SUMO2's role in cellular signaling pathways could reveal novel therapeutic targets and strategies for mitigating the effects of SUMOylation-related diseases. Overall, the characterization of SUMO2-recombinant proteins is pivotal for advancing our knowledge of SUMOylation and its implications in health and disease.
