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
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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John G Routsias et al.
Rheumatology (Oxford, England), 50(7), 1189-1193 (2011-02-24)
Recently, a number of studies have pointed to a potential relationship between periodontitis (PO) and RA and vice versa. Both diseases are characterized by chronic inflammation, osseous destruction, damage of the supporting soft tissues, similar cellular immune responses and common
Eva A V Moelants et al.
Cytokine, 61(1), 161-167 (2012-10-19)
Citrullination, a posttranslational modification (PTM) recently discovered on inflammatory chemokines such as interleukin-8 (IL-8/CXCL8) and interferon-γ-inducible protein-10 (IP-10/CXCL10), seriously influences their biological activity. Citrullination or the deimination of arginine to citrulline is dependent on peptidylarginine deiminases (PADs) and has been
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
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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