SAE0061
Peptidyl arginine deiminase type-2 (PAD2) human
recombinant, expressed in E. coli
Synonym(s):
PAD-2, PAD2, PADI-2, PADI2
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About This Item
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recombinant
expressed in E. coli
Quality Level
specific activity
≥40 units/mg protein
shipped in
dry ice
storage temp.
−20°C
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 reaction catalyzed is as follows:
Protein--[L-arginine] + H2O+Ca+2→Protein--[L-citrulline]+ NH4
This deimination provides another level of regulating protein function.
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. PADenzymes play important roles in gene regulation by citrullination of arginine residues on histones H3, H2A, and H4. Overexpression of these enzymes has been found in several diseases such as rheumatoid arthritis, Alzheimer′s disease, multiple sclerosis, lupus, Parkinson′s disease, and cancer. PAD2 is widely expressed in the brain, secretory glands, and skeletal muscles. The enzyme was found to be responsible for hyper-citrullination of myelin basic protein, which is suspected to lead to multiple sclerosis. The product is supplied in 20 mM Tris, pH 7.5, 200 mM NaCl, 10% (w/v) glycerol, 10 mM 2-mercaptoethanol, 1 mM EDTA, 1 mM DTT, 10 mM CaCl2, 10 mM arginine, 30 mM maltose, and 0.6 mg/ml dodecyl−β-D-maltoside. Enzymatic activity: Activity is measured by a colorimetric method with the synthetic substrate benzoyl arginine ethyl ester (BAEE).
Protein--[L-arginine] + H2O+Ca+2→Protein--[L-citrulline]+ NH4
This deimination provides another level of regulating protein function.
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. PADenzymes play important roles in gene regulation by citrullination of arginine residues on histones H3, H2A, and H4. Overexpression of these enzymes has been found in several diseases such as rheumatoid arthritis, Alzheimer′s disease, multiple sclerosis, lupus, Parkinson′s disease, and cancer. PAD2 is widely expressed in the brain, secretory glands, and skeletal muscles. The enzyme was found to be responsible for hyper-citrullination of myelin basic protein, which is suspected to lead to multiple sclerosis. The product is supplied in 20 mM Tris, pH 7.5, 200 mM NaCl, 10% (w/v) glycerol, 10 mM 2-mercaptoethanol, 1 mM EDTA, 1 mM DTT, 10 mM CaCl2, 10 mM arginine, 30 mM maltose, and 0.6 mg/ml dodecyl−β-D-maltoside. Enzymatic activity: Activity is measured by a colorimetric method with the synthetic substrate benzoyl arginine ethyl ester (BAEE).
Unit Definition
One unit will produce 1.0 μmole of N-a-benzoylcitrulline ethyl ester from BAEE per hr at 55 °C at pH 7.2.
Physical form
Supplied as a buffered aqueous solution containing Trizma, NaCl, glycerol, mercaptoethanol, EDTA, DTT, CaCl2, arginine, maltose, and dodecyl-β-D-maltoside.
Preparation Note
Contains a maltose-binding protein fusion tag.
Storage Class Code
11 - Combustible Solids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
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