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Key Documents

SRP5224

Sigma-Aldrich

PAD2, GST tagged from mouse

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

Synonyme(s) :

PADI2, mKIAA0994

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About This Item

Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32

Source biologique

mouse

Produit recombinant

expressed in baculovirus infected Sf9 cells

Pureté

≥70% (SDS-PAGE)

Forme

buffered aqueous glycerol solution

Poids mol.

~99 kDa

Numéro d'accès NCBI

Application(s)

cell analysis

Conditions d'expédition

dry ice

Température de stockage

−70°C

Informations sur le gène

mouse ... Padi2(18600)

Description générale

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.

Forme physique

Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.

Notes préparatoires

after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles

Remarque sur l'analyse

This protein is not assayed for enzymatic activity.

Code de la classe de stockage

10 - Combustible liquids

Classe de danger pour l'eau (WGK)

WGK 1

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable


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Consulter la Bibliothèque de documents

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
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
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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