P1584
Peptidyl Arginine Deiminase from rabbit skeletal muscle
buffered aqueous glycerol solution, ≥200 units/mg protein (Bradford)
Synonym(s):
Protein arginine iminohydrolase
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About This Item
CAS Number:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
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form
buffered aqueous glycerol solution
Quality Level
specific activity
≥200 units/mg protein (Bradford)
relevant disease(s)
arthritis (rheumatoid )
shipped in
dry ice
storage temp.
−70°C
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General description
Peptidyl arginine deiminase is the enzyme that converts arginine into citrulline.
Application
Peptidyl arginine deiminase has been used in a study that assessed promising novel biomarkers for the early diagnosis of rheumatoid arthritis. It has also been used in a study to investigate the autopathogenic correlation of periodontitis and rheumatoid arthritis.
Biochem/physiol Actions
Calcium is required for peptidylarginine deiminase activity in vitro.
Unit Definition
One unit will produce 1 μmole of N-α-benzoylcitrulline ethyl ester from BAEE per hr at 55 °C at pH 7.2.
Physical form
Solution in 20 mM Tris-HCl, pH 7.4, containing 10 mM 2-mercaptoethanol, 1 mM EDTA and 10% glycerol
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
Storage Class
10 - Combustible liquids
wgk_germany
WGK 2
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
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Leendert A Trouw et al.
Autoimmunity reviews, 12(2), 318-322 (2012-06-06)
Rheumatoid arthritis (RA) is a chronic autoimmune disease characterized by inflammation and damage of the joints affecting about 0.5% of the general population. Early treatment in RA is important as it can prevent disease progression and irreversible damage of the
Jason S Knight et al.
Circulation research, 114(6), 947-956 (2014-01-16)
Neutrophil extracellular trap (NET) formation promotes vascular damage, thrombosis, and activation of interferon-α-producing plasmacytoid dendritic cells in diseased arteries. Peptidylarginine deiminase inhibition is a strategy that can decrease in vivo NET formation. To test whether peptidylarginine deiminase inhibition, a novel
M Fujisaki et al.
Journal of biochemistry, 89(1), 257-263 (1981-01-01)
An enzyme which catalyzes the coversion of arginyl residues to citrullyl residues in protein was obtained from the extract of the epidermis of newborn rats. The enzyme required Ca2+ for its activity. The enzyme activity was enhanced in the presence
Maria A Christophorou et al.
Nature, 507(7490), 104-108 (2014-01-28)
Citrullination is the post-translational conversion of an arginine residue within a protein to the non-coded amino acid citrulline. This modification leads to the loss of a positive charge and reduction in hydrogen-bonding ability. It is carried out by a small
Reinout Raijmakers et al.
Journal of molecular biology, 367(4), 1118-1129 (2007-02-17)
Peptidylarginine deiminase (PAD) enzymes catalyze the conversion of arginine residues in proteins to citrulline residues. Citrulline is a non-standard amino acid that is not incorporated in proteins during translation, but can be generated post-translationally by the PAD enzymes. Although the
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