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Merck

SRP5224

Sigma-Aldrich

PAD2, GST tagged from mouse

recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution

Sinónimos:

PADI2, mKIAA0994

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

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

10 - Combustible liquids

wgk_germany

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Akihito Ishigami et al.
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
K Watanabe et al.
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
Miranda M Standiford et al.
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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