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SRP0326

Sigma-Aldrich

PADI-1 human

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

Sinónimos:

Peptidyl arginine deiminase, type I

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

biological source

human

recombinant

expressed in baculovirus infected Sf9 cells

assay

≥70% (SDS-PAGE)

form

aqueous solution

mol wt

75 kDa

packaging

pkg of 10 μg

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... PADI1(29943)

General description

Human PADI-1, also known as Peptidyl arginine deiminase, type I, (GenBank Accession No. NM_013358), amino acids 1-663 (end) with C-terminal FLAG-tag, MW= 75 kDa, expressed in a Baculovirus infected Sf9 cell expression system.

Application

Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.

Storage Class

10 - Combustible liquids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable


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Marina Guerrin et al.
The Biochemical journal, 370(Pt 1), 167-174 (2002-11-06)
Peptidylarginine deiminases (PADs) catalyse a post-translational modification of proteins through the conversion of arginine residues into citrullines. The existence of four isoforms of PAD (types I, II, III and IV) encoded by four different genes, which are distinct in their
T Kanno et al.
The Journal of investigative dermatology, 115(5), 813-823 (2000-11-09)
Peptidylarginine deiminase catalyzes the post-translational modification of proteins through the conversion of arginine to citrulline in the presence of calcium ions. In rodents, peptidylarginine deiminase has been classified into four isoforms, types I, II, III, and IV, which are distinct
Rachida Nachat et al.
The Journal of investigative dermatology, 124(2), 384-393 (2005-01-29)
Post-translational conversion of arginine to citrulline residues is catalyzed by peptidylarginine deiminases (PAD). Although the existence of five isoforms of PAD has been reported in rodents and humans, their tissue distribution, substrate specificity, and physiological function have yet to be

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