SRP0329
PADI-4 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥65% (SDS-PAGE)
Synonym(e):
Peptidyl arginine deiminase, type IV
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Alle Fotos(2)
About This Item
UNSPSC-Code:
12352200
NACRES:
NA.32
Empfohlene Produkte
Biologische Quelle
human
Rekombinant
expressed in baculovirus infected Sf9 cells
Assay
≥65% (SDS-PAGE)
Form
aqueous solution
Mol-Gew.
75 kDa
Verpackung
pkg of 10 μg
NCBI-Hinterlegungsnummer
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Lagertemp.
−70°C
Angaben zum Gen
human ... PADI4(23569)
Allgemeine Beschreibung
PADI4 (peptidyl arginine deiminase 4) gene is localized to human chromosome 1p36, and is one of the four PADIs found in humans. PADI4 protein is composed of 663 amino acids encoded by 2238 base pairs of PADI4 cDNA. This protein is expressed in peripheral blood CD3+ T cells, CD20+ B cells, CD15+ neutrophils and CD68+ monocytes. It is expressed in haematopoietic tissues, such as spleen, thymus, peripheral blood leucocytes, fetal liver and bone marrow.
Anwendung
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem./physiol. Wirkung
PADIs (peptidyl arginine deiminases) are responsible for the post-translational conversion of peptidylarginine to citrulline, in the presence of calcium ions. Citrullination can result in changes in conformational and functional characteristics of target proteins. In individuals with rheumatoid arthritis (RA), this gene is expressed in hematological cells and synovial tissues, and variant in this gene is linked with susceptibility to RA. The expression of this protein is linked with DNA hypermethylation in acute promyelocytic leukemia (APL), and PAD4/SOX4/PU.1 signaling pathway plays a role in committed differentiation of APL cells into granulocytic cells.
Lagerklassenschlüssel
10 - Combustible liquids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Analysenzertifikate (COA)
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Lise Boon et al.
Matrix biology : journal of the International Society for Matrix Biology, 95, 68-83 (2020-11-07)
Matrix metalloproteinases (MMPs) are enzymes with critical roles in biology and pathology. Glycosylation, nitrosylation and proteolysis are known posttranslational modifications (PTMs) regulating intrinsically the activities of MMPs. We discovered MMP citrullination by peptidyl arginine deiminases (PADs) as a new PTM.
Functional haplotypes of PADI4, encoding citrullinating enzyme peptidylarginine deiminase 4, are associated with rheumatoid arthritis.
Suzuki A et al
Nature Genetics, 34(4), 395-402 (2003)
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
A novel PAD4/SOX4/PU.1 signaling pathway is involved in the committed differentiation of acute promyelocytic leukemia cells into granulocytic cells.
Song G et al
Oncotarget, 7(3), 3144-3157 (2016)
Localization of peptidylarginine deiminase 4 (PADI4) and citrullinated protein in synovial tissue of rheumatoid arthritis.
Chang X et al
Rheumatology (Oxford, England), 44(1), 40-50 (2005)
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