SRP0328
PADI-3 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥60% (SDS-PAGE)
Synonym(s):
Peptidyl arginine deiminase, type III
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About This Item
UNSPSC Code:
12352200
NACRES:
NA.32
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥60% (SDS-PAGE)
form
aqueous solution
mol wt
75 kDa
packaging
pkg of 10 μg
storage condition
avoid repeated freeze/thaw cycles
concentration
0.25 mg/mL
NCBI accession no.
UniProt accession no.
shipped in
dry ice
storage temp.
−70°C
Gene Information
human ... PADI3(51702)
General description
Human PADI-3, also known as Peptidyl arginine deiminase, type III, (GenBank Accession No. NM_016233), amino acids 1-664 (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
Certificates of Analysis (COA)
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Sijun Dong et al.
The Biochemical journal, 397(3), 449-459 (2006-05-05)
Human peptidylarginine deiminase type III gene (PADI3) encodes a crucial post-translational modification enzyme that converts protein-bound arginine residues into citrulline residues. Its expression is restricted to a few cell types, including keratinocytes in the granular layer of the epidermis and
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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