Analytical Data
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Gene name
PELI2
- Application
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Alternative Names
PELI2; E3 ubiquitin-protein ligase pellino homolog 2; Pellino-2; RING-type E3 ubiquitin transferase pellino homolog 2
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Species
Human
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HAT8
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Expression Region
F2-D420
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Protein Length
Partial
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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
PELI2, or Pellino E3 Ubiquitin Ligase 2, is a member of the Pellino family of E3 ubiquitin ligases that play a crucial role in the regulation of immune responses and cellular signaling pathways. Research on PELI2 has gained momentum due to its involvement in various biological processes, including inflammation, apoptosis, and cell proliferation. Given its pivotal role in the immune system, dysregulation of PELI2 has been linked to autoimmune diseases, cancers, and infectious diseases. The protein mediates the ubiquitination of target proteins, thereby influencing their stability, localization, and function. PELI2 has been shown to interact with key signaling molecules in pathways such as Toll-like receptor (TLR) signaling, which is essential for pathogen recognition and the subsequent activation of immune responses. Understanding the structure and function of PELI2, along with its interacting partners, may provide insights into its role as a potential therapeutic target. Researchers have been focusing on the development of recombinant PELI2 proteins to study its biochemical properties and to evaluate its regulatory mechanisms in immune signaling. Overall, the study of PELI2 not only enhances our understanding of immune regulation but also holds promise for novel therapeutic approaches in treating diseases characterized by immune dysregulation.
