Analytical Data
-
Gene name
PELI1
- Application
-
Alternative Names
PELI1；PRISM；E3 ubiquitin-Protein ligase pellino homolog 1
-
Species
Human
-
Source
E. coli
-
Tag
His tag N-Terminus
-
Purity
Greater than 90% as determined by SDS-PAGE.
-
Uniprot
Q96FA3
-
Expression Region
1-418aa
-
AA Sequence
MFSPDQENHPSKAPVKYGELIVLGYNGSLPNGDRGRRKSRFALFKRPKANGVKPSTVHIACTPQAAKAISNKDQHSISYTLSRAQTVVVEYTHDSNTDMFQIGRSTESPIDFVVTDTVPGSQSNSDTQSVQSTISRFACRIICERNPPFTARIYAAGFDSSKNIFLGEKAAKWKTSDGQMDGLTTNGVLVMHPRNGFTEDSKPGIWREISVCGNVFSLRETRSAQQRGKMVEIETNQLQDGSLIDLCGATLLWRTAEGLSHTPTVKHLEALRQEINAARPQCPVGFNTLAFPSMKRKDVVDEKQPWVYLNCGHVHGYHNWGNKEERDGKDRECPMCRSVGPYVPLWLGCEAGFYVDAGPPTHAFSPCGHVCSEKTTAYWSQIPLPHGTHTFHAACPFCAHQLAGEQGYIRLIFQGPLD
-
Molecular Weight
73.0 kDa
-
Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
-
Form
Freeze-dried powder
-
Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
-
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.
-
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.
-
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
PELI1 (pellino E3 ubiquitin protein ligase 1) is an E3 ubiquitin ligase that plays a crucial role in various cellular processes, including immune response and cell signaling. Recent studies have highlighted its importance in modulating inflammation and apoptosis, making it a significant factor in the pathogenesis of autoimmune diseases and cancer. The regulation of protein stability and degradation through ubiquitination is a key mechanism through which PELI1 exerts its effects, influencing pathways such as NF-κB signaling. Research on recombinant PELI1 protein aims to elucidate its structural features, enzymatic activity, and interaction with substrate proteins. By producing PELI1 in a recombinant system, researchers can investigate its functional roles at a molecular level, assess its potential as a therapeutic target, and explore its involvement in disease mechanisms. Understanding how PELI1 operates within the ubiquitin-proteasome system will provide insights into its contribution to cellular homeostasis and the immune response, potentially leading to new strategies for treating conditions associated with dysregulated protein ubiquitination. Therefore, the ongoing study of recombinant PELI1 protein is vital for uncovering its biological significance and therapeutic potential.
