SAE0086
Peptidyl Arginine Deiminase Type 4
human recombinant, expressed in E. coli, aqueous solution
Synonym(s):
Peptidyl Arginine Deiminase Type 4, PAD4, PADI4, Protein arginine iminohydrolase 4
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About This Item
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biological source
human
Quality Level
recombinant
expressed in E. coli
assay
≥90% (SDS-PAGE)
form
aqueous solution
specific activity
≥200 units/mg protein
mol wt
74 kDa
UniProt accession no.
application(s)
genomic analysis
shipped in
dry ice
storage temp.
−20°C
Gene Information
human ... PADI4(23569)
General description
Peptidyl Arginine Deiminases (PADs) perform post-translational deiminations of proteins. PADs are calcium-dependent enzymes that catalyze the conversion of L-arginine residues to L-citrulline. The catalyzed reaction is as follows:
2+
Ca Protein--[L-arginine] + H2O ––––> Protein--[L-citrulline]
There are five mammalian PADs sub-types, which differ in substrate specificity and tissue distribution. PAD enzymes are highly homologous, with 50–60% sequence similarity.1 PADs play important roles in gene regulation by citrullination of arginine residues on histones H3, H2A, and H4. Overexpression of PADs has been found in conditions such as rheumatoid arthritis, Alzheimer′s disease, multiple sclerosis, lupus,Parkinson′s disease, and cancer.2,3
PAD4 is widely expressed in the immune system with expression pathology in various tumor and cancer cell lines.5 In cells, PAD4 can be found in the cytoplasm and nucleus. PAD4 activity has been correlated to the development and progress of Rheumatoid Arthritis (RA).2,5 A study in mice has indicated a mechanism for the development of RA by anticitrullin autoimmunity.6
This recombinant human PAD4 is expressed in Escherichia coli as a fusion protein. The fusion partner is removed by HRV3C protease digestion, followed by chromatographic purification.
2+
There are five mammalian PADs sub-types, which differ in substrate specificity and tissue distribution. PAD enzymes are highly homologous, with 50–60% sequence similarity.1 PADs play important roles in gene regulation by citrullination of arginine residues on histones H3, H2A, and H4. Overexpression of PADs has been found in conditions such as rheumatoid arthritis, Alzheimer′s disease, multiple sclerosis, lupus,Parkinson′s disease, and cancer.2,3
PAD4 is widely expressed in the immune system with expression pathology in various tumor and cancer cell lines.5 In cells, PAD4 can be found in the cytoplasm and nucleus. PAD4 activity has been correlated to the development and progress of Rheumatoid Arthritis (RA).2,5 A study in mice has indicated a mechanism for the development of RA by anticitrullin autoimmunity.6
This recombinant human PAD4 is expressed in Escherichia coli as a fusion protein. The fusion partner is removed by HRV3C protease digestion, followed by chromatographic purification.
Biochem/physiol Actions
Calcium is required for peptidylarginine deiminase activity in vitro.
Unit Definition
One unit will produce 1 μmole of N-a-benzoylcitrulline ethyl ester from BAEE per hour at 37 °C at pH 7.7.
Physical form
Supplied as an aqueous solution in 10 mM Tris (pH 7.5), 500 mM NaCl, 1 mM EDTA, and 1 mM DTT.
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Frontiers in oncology, 12, 1035188-1035188 (2022-12-20)
Protein arginine deiminases (PADs) are intracellular enzymes that may, especially in pathological conditions, also citrullinate extracellular substrates, including matrisome proteins such as structural proteins in extracellular matrix (ECM). PADs are abundantly expressed in human cancer cells. Citrullination of matrisome proteins
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