Analytical Data
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Gene name
UBE2V2
- Application
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Alternative Names
DDVit 1Enterocyte differentiation-associated factor 1 ;EDAF-1Enterocyte differentiation-promoting factor 1 ;EDPF-1MMS2 homologVitamin D3-inducible protein
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q15819
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Expression Region
2-145aa
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Molecular Weight
32.2 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
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Protein Description
UBE2V2, a member of the ubiquitin-conjugating enzyme family, plays a critical role in the ubiquitin-proteasome system, which is essential for regulating protein degradation and cellular processes such as cell cycle progression, DNA repair, and apoptosis. This enzyme primarily functions as a ubiquitin-conjugating enzyme in the context of the ubiquitylation pathway, where it collaborates with other E3 ligases to facilitate the attachment of ubiquitin to substrate proteins. The study of UBE2V2 has gained attention due to its involvement in various cellular functions and potential implications in several diseases, including cancer. Research indicates that UBE2V2 is upregulated in certain tumors, suggesting its role in promoting oncogenic processes. Moreover, UBE2V2 may also modulate the stability and activity of key tumor suppressor proteins and oncogenes, further emphasizing its importance in cancer biology. Investigating the biochemical properties of recombinant UBE2V2, as well as its interactions with E3 ligases and substrate proteins, can provide valuable insights into its mechanistic functions and regulatory networks. Understanding these interactions can pave the way for novel therapeutic strategies targeting the ubiquitin-proteasome system, aiming to manipulate protein degradation pathways for cancer treatment and other diseases characterized by dysregulated protein homeostasis. Therefore, recombinant UBE2V2 serves as a crucial tool for elucidating the complexities of ubiquitin signaling and its broader implications in cellular health and disease.
