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Recombinant Human Pellino 1 protein is a Human Fragment protein, in the 145 to 404 aa range, expressed in Escherichia coli, with =80% purity and suitable for SDS-PAGE.
Alternative names=E3 ubiquitin-protein ligase pellino homolog 1, Pellino-1, Pellino-related intracellular-signaling molecule, RING-type E3 ubiquitin transferase pellino homolog 1, PELI1, PRISM
=80% SDS-PAGE
Escherichia coli
His-DHFR tag N-Terminus
SDS-PAGE
No
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Recombinant Human Pellino 1 protein is a Human Fragment protein, in the 145 to 404 aa range, expressed in Escherichia coli, with =80% purity and suitable for SDS-PAGE.
Alternative names=E3 ubiquitin-protein ligase pellino homolog 1, Pellino-1, Pellino-related intracellular-signaling molecule, RING-type E3 ubiquitin transferase pellino homolog 1, PELI1, PRISM
=80% SDS-PAGE
Escherichia coli
His-DHFR tag N-Terminus
SDS-PAGE
No
28.9 kDa
145 to 404
Fragment
No
Recombinant
Human
Reconstitute with water to desired concentration
Constituents: 0.58% Sodium chloride, 0.32% Tris HCl
Lyophilized
Purified via His tag
E3 ubiquitin ligase catalyzing the covalent attachment of ubiquitin moieties onto substrate proteins. Involved in the TLR and IL-1 signaling pathways via interaction with the complex containing IRAK kinases and TRAF6. Mediates 'Lys-63'-linked polyubiquitination of IRAK1 allowing subsequent NF-kappa-B activation (PubMed:12496252, PubMed:17675297). Mediates 'Lys-48'-linked polyubiquitination of RIPK3 leading to its subsequent proteasome-dependent degradation; preferentially recognizes and mediates the degradation of the 'Thr-182' phosphorylated form of RIPK3 (PubMed:29883609). Negatively regulates necroptosis by reducing RIPK3 expression (PubMed:29883609). Mediates 'Lys-63'-linked ubiquitination of RIPK1 (PubMed:29883609).
Belongs to the pellino family.
Phosphorylation by IRAK1 and IRAK4 enhances its E3 ligase activity.
Blue Ice
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
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