Analytical Data
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Gene name
SUMO2
- Application
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Alternative Names
SUMO2；SMT3B；Small ubiquitin-related modifier 2
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P61956
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Expression Region
1-93aa
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AA Sequence
MADEKPKEGVKTENNDHINLKVAGQDGSVVQFKIKRHTPLSKLMKAYCER QGLSMRQIRFRFDGQPINETDTPAQLEMEDEDTIDVFQQQTGG
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Molecular Weight
18 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
SUMO2 (Small Ubiquitin-like Modifier 2) is a member of the SUMO (Small Ubiquitin-like Modifier) protein family, which plays a critical role in various cellular processes through a post-translational modification known as SUMOylation. This modification regulates protein stability, localization, and interactions, thereby influencing numerous cellular pathways, including DNA repair, cell proliferation, and stress responses. SUMO2, in particular, has garnered attention due to its unique functional properties and involvement in the regulation of numerous target proteins under physiological and pathological conditions. Its dysregulation has been implicated in various diseases, including cancer, neurodegenerative disorders, and cardiovascular diseases. The study of SUMO2 recombinant proteins has emerged as a promising avenue for understanding the mechanisms of SUMOylation and its impact on cellular functions. By producing SUMO2 in a recombinant system, researchers can investigate its biochemical properties, interactions with specific substrates, and the effects of SUMOylation on these proteins. Furthermore, the development of SUMO2-based therapeutics is an exciting prospect, as it may enable the modulation of SUMOylation pathways to restore cellular balance in disease contexts. Overall, the research on SUMO2 recombinant proteins provides valuable insights into the fundamental biology of SUMOylation and its potential applications in disease treatment and prevention.
