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SAE0061

Sigma-Aldrich

Peptidyl arginine deiminase type-2 (PAD2) human

recombinant, expressed in E. coli

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Synonym(s):
PAD-2, PAD2, PADI-2, PADI2
Enzyme Commission number:
3.5.3.15 (BRENDA, IUBMB)

recombinant

expressed in E. coli

Quality Level

200

specific activity

≥40 units/mg protein

shipped in

dry ice

storage temp.

−20°C

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D3446D4943SRP0211
Peptidyl arginine deiminase type-2 (PAD2) human recombinant, expressed in E. coli

Sigma-Aldrich

SAE0061

Peptidyl arginine deiminase type-2 (PAD2) human

Dipeptidyl Peptidase IV human recombinant, expressed in Sf9 cells

Sigma-Aldrich

D3446

Dipeptidyl Peptidase IV human

Dipeptidyl Peptidase IV human recombinant, expressed in baculovirus infected Sf9 cells, pkg of ≥1.0 units/vial, ≥10 units/mg protein

Sigma-Aldrich

D4943

Dipeptidyl Peptidase IV human

Sigma-Aldrich

Sigma-Aldrich

SRP0211

PTP-D2/PTPN14 Active human

specific activity

≥40 units/mg protein

specific activity

≥4,000 units/μg protein

specific activity

≥10 units/mg protein

specific activity

-

shipped in

dry ice

shipped in

dry ice

shipped in

wet ice

shipped in

dry ice

storage temp.

−20°C

storage temp.

−70°C

storage temp.

−20°C

storage temp.

−70°C

Quality Level

200

Quality Level

200

Quality Level

200

Quality Level

-

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).

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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Kevin L Bicker et al.
Biopolymers, 99(2), 155-163 (2012-11-24)
The post-translational modification of histones has significant effects on overall chromatin function. One such modification is citrullination, which is catalyzed by the protein arginine deiminases (PADs), a unique family of enzymes that catalyzes the hydrolysis of peptidyl-arginine to form peptidyl-citrulline
H Takahara et al.
Journal of biochemistry, 94(6), 1945-1953 (1983-12-01)
The preceding paper described the identification and some properties of peptidylarginine deiminase, which catalyzes the deimination of arginyl residues in protein, from rabbit skeletal muscle, kidney, brain, and lung. In the present work we purified peptidylarginine deiminase from rabbit skeletal
Olena Mahneva et al.
PloS one, 15(1), e0227822-e0227822 (2020-01-16)
Peptidylarginine deiminase (PAD) modifies peptidylarginine and converts it to peptidylcitrulline in the presence of elevated calcium. Protein modification can lead to severe changes in protein structure and function, and aberrant PAD activity is linked to human pathologies. While PAD homologs
Sunish Mohanan et al.
Biochemistry research international, 2012, 895343-895343 (2012-09-29)
The peptidylarginine deiminases (PADs) are a family of posttranslational modification enzymes that catalyze the conversion of positively charged protein-bound arginine and methylarginine residues to the uncharged, nonstandard amino acid citrulline. This enzymatic activity is referred to as citrullination or, alternatively
Mario A Moscarello et al.
Neurochemical research, 32(2), 251-256 (2006-10-13)
The pathogenesis of MS is unknown. In our studies, we have demonstrated an important role for citrullinated myelin basic protein (MBP). The accompanying loss of positive charge compromises the ability of MBP to interact with the lipid bilayer. The conversion

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