Recombinant Human PADI4 / PAD4 protein - BSA and Azide free is a Human Full Length protein, in the 1 to 663 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
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Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci) (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci (PubMed:18209087). Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription (PubMed:15345777). Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (PubMed:15731352).
PAD4, PADI5, PDI5, PADI4, Protein-arginine deiminase type-4, HL-60 PAD, Peptidylarginine deiminase IV, Protein-arginine deiminase type IV
Recombinant Human PADI4 / PAD4 protein - BSA and Azide free is a Human Full Length protein, in the 1 to 663 aa range, expressed in Escherichia coli, with >95% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE, HPLC.
pH: 7.5
Constituents: 2.92% Sodium chloride, 0.605% Tris
Greater than 95% as determined by SEC-HPLC and reducing SDS-PAGE.
Catalyzes the citrullination/deimination of arginine residues of proteins such as histones, thereby playing a key role in histone code and regulation of stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Citrullinates histone H1 at 'Arg-54' (to form H1R54ci), histone H3 at 'Arg-2', 'Arg-8', 'Arg-17' and/or 'Arg-26' (to form H3R2ci, H3R8ci, H3R17ci, H3R26ci, respectively) and histone H4 at 'Arg-3' (to form H4R3ci) (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Acts as a key regulator of stem cell maintenance by mediating citrullination of histone H1: citrullination of 'Arg-54' of histone H1 (H1R54ci) results in H1 displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance (PubMed:15339660, PubMed:15345777, PubMed:16567635, PubMed:21245532). Promotes profound chromatin decondensation during the innate immune response to infection in neutrophils by mediating formation of H1R54ci (PubMed:18209087). Required for the formation of neutrophil extracellular traps (NETs); NETs are mainly composed of DNA fibers and are released by neutrophils to bind pathogens during inflammation (By similarity). Citrullination of histone H3 prevents their methylation by CARM1 and HRMT1L2/PRMT1 and represses transcription (PubMed:15345777). Citrullinates EP300/P300 at 'Arg-2142', which favors its interaction with NCOA2/GRIP1 (PubMed:15731352).
Belongs to the protein arginine deiminase family.
Autocitrullination at Arg-372 and Arg-374 inactivates the enzyme.
PADI4 also known as PAD4 PADI4 protein or PAD-4 is an enzyme that plays a mechanical role in post-translational modification. It functions by catalyzing the conversion of arginine residues into citrulline in histones a process known as citrullination or deimination. This enzyme exhibits a molecular mass of approximately 74 kDa and is expressed notably in tissues like bone marrow and sites of inflammation. PADI4 shows high expression in immune cells such as neutrophils which are important for inflammatory responses.
The PADI4 protein impacts gene expression by modifying chromatin architecture making it part of chromatin remodeling activities. PADI4 is known to associate with chromatin but it does not form large stable complexes. It influences the transcriptional activity of genes by altering histone interactions which can affect immune responses and cellular differentiation. Through these chromatin changes PADI4 plays a notable role in regulating genes associated with immune function and inflammatory responses.
PADI4 integrates into the inflammatory response and apoptosis pathways. It influences apoptosis by modulating pro-inflammatory gene expression and participating in the formation of neutrophil extracellular traps (NETs). PADI4 works with other proteins such as histone H3 and histone H4 to influence immune cell pathways. These interactions underline its role in the regulation of protein expressions during inflammation and immune-mediated processes.
PADI4 connects to rheumatoid arthritis (RA) and certain cancers. In rheumatoid arthritis altered activity of PADI4 can lead to the production of autoantibodies against citrullinated proteins which exacerbates inflammation in joints. The enzyme’s dysregulation is also implicated in cancer progression where it may affect tumor growth and metastasis. PADI4’s interaction with other proteins like citrullinated histones highlights its association with pathogenic processes in such diseases.
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