PPIL1 Protein, Human (His)

The PPIL1 protein is a spliceosome component that coordinates pre-mRNA splicing and controls RNA processing. As a peptidylprolyl cis-trans isomerase (PPIase), PPIL1 accelerates protein folding by catalyzing the cis-trans isomerization of proline imide peptide bonds. PPIL1 Protein, Human (His) is the recombinant human-derived PPIL1 protein, expressed by E. coli , with N-6*His labeled tag. The total length of PPIL1 Protein, Human (His) is 166 a.a., with molecular weight of ~19.0 kDa.

PPIL1 protein is intricately involved in pre-mRNA splicing as a vital component of the spliceosome, contributing to the complex machinery that governs RNA processing. Beyond its role in splicing regulation, PPIL1, as a peptidyl-prolyl cis-trans isomerase (PPIase), plays a key role in accelerating the folding of proteins. Notably, it catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides, showcasing its involvement in protein conformational changes. Specifically, PPIL1 catalyzes prolyl peptide bond isomerization in CDC40/PRP17, underscoring its specificity in mediating these crucial molecular interactions. Moreover, PPIL1 contributes to embryonic brain development, with its function in this context being independent of its isomerase activity, highlighting its multifaceted role in cellular processes.

Human

E. coli

N-6*His

Q9Y3C6 (M1-G166)

51645  [NCBI]

MAAIPPDSWQPPNVYLETSMGIIVLELYWKHAPKTCKNFAELARRGYYNGTKFHRIIKDFMIQGGDPTGTGRGGASIYGKQFEDELHPDLKFTGAGILAMANAGPDTNGSQFFVTLAPTQWLDGKHTIFGRVCQGIGMVNRVGMVETNSQDRPVDDVKIIKAYPSG

Approximately 19.0 kDa

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.