PPIL2 Protein, Human (His)

PPIL2 exhibits ubiquitin-protein ligase activity, acting as an E3 ligase or ubiquitin-ubiquitin ligase, promoting “Lys-48”-linked polyubiquitination for proteasomal degradation of substrates.It acts as a chaperone to help transport BSG/Basigin to the cell membrane.PPIL2 Protein, Human (His) is the recombinant human-derived PPIL2 protein, expressed by E.coli , with N-His labeled tag.

PPIL2, known for its ubiquitin-protein ligase activity, functions as both an E3 ubiquitin protein ligase and an ubiquitin-ubiquitin ligase, facilitating the elongation of ubiquitin chains on substrates. Through the mediation of 'Lys-48'-linked polyubiquitination, it has the potential to target proteins for proteasomal degradation. Additionally, PPIL2 may operate as a chaperone, contributing to the transport of proteins like BSG/Basigin to the cell membrane. Despite its ubiquitin ligase function, PPIL2 is likely an inactive peptidyl-prolyl cis-trans isomerase. As part of the minor spliceosome, PPIL2 plays a role in the splicing of U12-type introns in pre-mRNAs, indicating its involvement in the intricate process of RNA splicing.

Human

E. coli

N-His

Q13356-2 (G280-P457)

23759  [NCBI]

Partial

GYVRLHTNKGDLNLELHCDLTPKTCENFIRLCKKHYYDGTIFHRSIRNFVIQGGDPTGTGTGGESYWGKPFKDEFRPNLSHTGRGILSMANSGPNSNRSQFFITFRSCAYLDKKHTIFGRVVGGFDVLTAMENVESDPKTDRPKEEIRIDATTVFVDPYEEADAQIAQERKTQLKVAP

Approximately 24 kDa

≥ 95%, as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.