Analytical Data
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Gene name
PELI2
- Application
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Alternative Names
PELI2;E3 ubiquitin-Protein ligase pellino homolog 2
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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
Q9HAT8
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Expression Region
1-420aa
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AA Sequence
MFSPGQEEHC APNKEPVKYG ELVVLGYNGA LPNGDRGRRK SRFALYKRPK ANGVKPSTVH VISTPQASKA ISCKGQHSIS YTLSRNQTVV VEYTHDKDTD MFQVGRSTES PIDFVVTDTI SGSQNTDEAQ ITQSTISRFA CRIVCDRNEP YTARIFAAGF DSSKNIFLGE KAAKWKNPDG HMDGLTTNGV LVMHPRGGFT EESQPGVWRE ISVCGDVYTL RETRSAQQRG KLVESETNVL QDGSLIDLCG ATLLWRTADG LFHTPTQKHI EALRQEINAA RPQCPVGLNT LAFPSINRKE VVEEKQPWAY LSCGHVHGYH NWGHRSDTEA NERECPMCRT VGPYVPLWLG CEAGFYVDAG PPTHAFTPCG HVCSEKSAKY WSQIPLPHGT HAFHAACPFC ATQLVGEQNC IKLIFQGPID
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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
PELI2, a member of the Peli (Pyrin and Evin/ICE) family of proteins, is gaining attention in the field of immunology due to its potential role in regulating immune responses and inflammation. Researchers have identified PELI2 as an E3 ubiquitin ligase, which is crucial for protein ubiquitination, influencing various cellular processes such as signal transduction and apoptosis. Recent studies have highlighted PELI2’s involvement in modulating the NF-kB pathway, a key regulator of immune responses, and its potential impact on autoimmune diseases and cancer progression. The exploration of PELI2 as a recombinant protein is particularly relevant, as it offers opportunities to better understand its functional mechanisms through structural and biochemical studies. Recombinant PELI2 can be utilized to elucidate its interactions with other proteins, define its enzymatic activity, and explore its role in the context of pathogen recognition and immune system activation. Consequently, this research could pave the way for novel therapeutic strategies aimed at targeting PELI2-related pathways in inflammatory and autoimmune diseases. Understanding the biology of PELI2 not only contributes to the fundamental knowledge of immune regulation but also holds potential for the development of new interventions in diseases characterized by dysregulated immune responses.
