PARP14 Protein, Human (His, StrepⅡ)

The PARP14 protein is an ADP-ribosyltransferase that uniquely mono-ADP-ribosylates glutamic acid residues on target proteins such as STAT1 and STAT6, unlike PARP1 and PARP2. It catalyzes STAT1 mono-ADP ribosylation at “Glu-657” and “Glu-705”, reduces STAT1 phosphorylation and inhibits the production of pro-inflammatory cytokines in macrophages following IFNG stimulation. PARP14 Protein, Human (His, Strep) is the recombinant human-derived PARP14 protein, expressed by E. coli , with N-Strep, N-8*His labeled tag.

PARP14 Protein, an ADP-ribosyltransferase, facilitates the mono-ADP-ribosylation of glutamate residues on target proteins, distinguishing itself from PARP1 and PARP2 by its inability to mediate poly-ADP-ribosylation. Specifically, it has been shown to catalyze the mono-ADP-ribosylation of STAT1 at 'Glu-657' and 'Glu-705', leading to decreased STAT1 phosphorylation and subsequent negative regulation of pro-inflammatory cytokine production in macrophages following IFNG stimulation. However, the exact role of ADP-ribosylation in preventing STAT1 phosphorylation has been debated, with suggestions that the inhibition may be a result of STAT1 'Lys-703' sumoylation. Additionally, PARP14 mono-ADP-ribosylates STAT6, enhancing STAT6-dependent transcription, and in macrophages, it positively regulates MRC1 expression in response to IL4 stimulation by promoting STAT6 phosphorylation. Furthermore, PARP14 engages in mono-ADP-ribosylation of PARP9.

Human

E. coli

N-StrepⅡ;N-8*His

Q460N5 (F1208-E1387)

54625

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

<1 EU/μg, determined by LAL method.