Analytical Data
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Gene name
KLHDC2/EloB/EloC
- Application
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Alternative Names
TCEB1; SI; Elo-C; Transcription Elongation Factor B(SIII)Polypeptide 1; Elongin 15 kDa subunit; RNA polymerase II transcription factor SIII subunit C
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q15369
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Expression Region
Met1~Cys112
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Molecular Weight
16kDa
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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
KLHDC2, EloB, and EloC are E3 ubiquitin ligases that play critical roles in cellular processes, including protein degradation and cell signaling, which are vital for maintaining cellular homeostasis. The study of these proteins has gained attention due to their involvement in various diseases, particularly in cancers and neurodegenerative disorders, where dysregulation of ubiquitin-modified proteins is often observed. KLHDC2, known for its unique ability to recognize and bind specific protein substrates, is thought to modulate key pathways by tagging proteins for degradation, thereby influencing cellular functions. Meanwhile, EloB and EloC, part of the elongin complex, participate in the ubiquitin-proteasome system, contributing to the regulation of protein turnover and signal transduction. Research into the structural and functional aspects of KLHDC2, EloB, and EloC is essential for understanding their roles in pathological conditions and may provide insights into new therapeutic targets. Investigating the mechanisms by which these E3 ligases operate can reveal potential strategies for modulating their activity, offering promising avenues for drug development in treating diseases linked to protein mismanagement.
