SRP5224
PAD2, GST tagged from mouse
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Synonym(s):
PADI2, mKIAA0994
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About This Item
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biological source
mouse
recombinant
expressed in baculovirus infected Sf9 cells
Assay
≥70% (SDS-PAGE)
form
buffered aqueous glycerol solution
mol wt
~99 kDa
NCBI accession no.
application(s)
cell analysis
shipped in
dry ice
storage temp.
−70°C
Gene Information
mouse ... Padi2(18600)
General description
PAD2 is a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. PAD2 has peptidylarginine deiminase activity against synthetic substrates. PAD2 is mainly expressed in the central nervous system, skeletal muscle, spinal cord, cerebrum, cerebellum, and submaxillary gland. PAD2 play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis.
Physical form
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Preparation Note
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Analysis Note
This protein is not assayed for enzymatic activity.
Storage Class Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
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Archives of biochemistry and biophysics, 407(1), 25-31 (2002-10-24)
Peptidylarginine deiminases (PADs) are posttranslational modification enzymes that convert protein arginine to citrulline residues in a calcium ion-dependent manner. Rodents have four isoforms of PAD (types I, II, III, and IV), each of which is distinct in substrate and tissue
The Journal of biological chemistry, 264(26), 15255-15260 (1989-09-15)
Various mammalian tissues contain protein-arginine deiminases (EC 3.5.3.15), which convert the arginine residues in normal peptide bonds to the citrulline residues in calcium ion-dependent manners. Here, we describe the complete primary structure of rat skeletal muscle peptidylarginine deiminase deduced from
Journal of neuroinflammation, 18(1), 305-305 (2021-12-29)
Microglia are the primary phagocytes of the central nervous system and are responsible for removing damaged myelin following demyelination. Previous investigations exploring the consequences of myelin phagocytosis on microglial activation overlooked the biochemical modifications present on myelin debris. Such modifications
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