PADI4 Protein, Human (Biotinylated, His)

The PADI4 protein catalyzes the citrullination of arginine residues in proteins such as histones, contributing to the histone code and stem cell regulation. PADI4 Protein, Human (Biotinylated, His) is the recombinant human-derived PADI4 protein, expressed by E. coli , with N-His labeled tag. The total length of PADI4 Protein, Human (Biotinylated, His) is 663 a.a., with molecular weight of 76.6 kDa.

PADI4, a protein crucial for the histone code, catalyzes the citrullination/deimination of arginine residues in various proteins, including histones. Specifically, it citrullinates histone H1 at 'Arg-54' (forming H1R54ci), histone H3 at 'Arg-2,' 'Arg-8,' 'Arg-17,' and/or 'Arg-26' (forming H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively), and histone H4 at 'Arg-3' (forming H4R3ci). This enzymatic activity plays a key role in the regulation of stem cell maintenance by inducing chromatin decondensation and pluripotency through the displacement of H1 from chromatin. Additionally, PADI4 is involved in the innate immune response, mediating chromatin decondensation in neutrophils during infection and contributing to the formation of neutrophil extracellular traps (NETs). Furthermore, it prevents the methylation of histone H3 by CARM1 and HRMT1L2/PRMT1, thereby repressing transcription. Notably, PADI4 citrullinates EP300/P300 at 'Arg-2142,' promoting its interaction with NCOA2/GRIP1.

Human

E. coli

N-His

Q9UM07 (M1-P663)

23569  [NCBI]

76.6 kDa

Greater than 95% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.