P1584
Peptidyl Arginine Deiminase from rabbit skeletal muscle
buffered aqueous glycerol solution, ≥200 units/mg protein (Bradford)
Sinónimos:
Protein arginine iminohydrolase
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About This Item
Número de CAS:
MDL number:
UNSPSC Code:
12352204
NACRES:
NA.54
Productos recomendados
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
Certificados de análisis (COA)
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Los clientes también vieron
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
Murat Bozdag et al.
Bioorganic & medicinal chemistry letters, 23(3), 715-719 (2012-12-26)
Protein arginin deaminase 4 (PAD4) is a calcium dependent enzyme which catalyses the conversion of peptidyl-arginine into peptidyl-citrulline and is implicated in several diseases such as rheumatoid arthritis (RA) and cancer. Herein we report the discovery of novel small-molecule, non
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
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