Analytical Data
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Gene name
E3
- Application
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Alternative Names
E3；BLOV1；Solute carrier family 35 member E3
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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
Q7Z769
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Expression Region
1-313aa
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AA Sequence
MALLVDRVRGHWRIAAGLLFNLLVSICIVFLNKWIYVYHGFPNMSLTLVHFVVTWLGLYICQKLDIFAPKSLPPSRLLLLALSFCGFVVFTNLSLQNNTIGTYQLAKAMTTPVIIAIQTFCYQKTFSTRIQLTLIPITLGVILNSYYDVKFNFLGMVFAALGVLVTSLYQVWVGAKQHELQVNSMQLLYYQAPMSSAMLLVAVPFFEPVFGEGGIFGPWSVSALLMVLLSGVIAFMVNLSIYWIIGNTSPVTYNMFGHFKFCITLFGGYVLFKDPLSINQALGILCTLFGILAYTHFKLSEQEGSRSKLAQRP
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Molecular Weight
35 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
E3 ligases, a crucial component of the ubiquitin-proteasome system, play a significant role in post-translational modifications by catalyzing the transfer of ubiquitin to target proteins, thus regulating their stability, localization, and activity. The diversity and specificity of E3 ligases, with hundreds of distinct types identified in humans, enable them to facilitate the degradation of various substrates involved in key cellular processes. Research on E3 ligases has gained momentum due to their involvement in numerous diseases, including cancer, neurodegenerative disorders, and infectious diseases. The ability of E3 ligases to modulate protein levels presents opportunities for therapeutic interventions, as manipulating their activity could restore normal cellular functions or target specific disease-causing proteins for degradation. Recent advancements in structural biology and proteomics have provided insights into the mechanisms by which E3 ligases recognize their substrates, enhancing our understanding of their roles in cellular homeostasis and disease progression. Furthermore, the development of small molecules or peptides that can inhibit or enhance E3 ligase activity is an emerging area of drug development, holding promise for innovative treatment strategies. Consequently, ongoing research into E3 ligases not only deepens our understanding of fundamental biological processes but also paves the way for novel therapeutic approaches in treating diverse diseases.
