SRP0329
PADI-4 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥65% (SDS-PAGE)
Synonyme(s) :
Peptidyl arginine deiminase, type IV
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About This Item
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.32
Produits recommandés
Source biologique
human
Produit recombinant
expressed in baculovirus infected Sf9 cells
Pureté
≥65% (SDS-PAGE)
Forme
aqueous solution
Poids mol.
75 kDa
Conditionnement
pkg of 10 μg
Numéro d'accès NCBI
Numéro d'accès UniProt
Conditions d'expédition
dry ice
Température de stockage
−70°C
Informations sur le gène
human ... PADI4(23569)
Description générale
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.
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Actions biochimiques/physiologiques
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.
Code de la classe de stockage
10 - Combustible liquids
Classe de danger pour l'eau (WGK)
WGK 3
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
Certificats d'analyse (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.
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)
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)
Yanming Wang et al.
Science (New York, N.Y.), 306(5694), 279-283 (2004-09-04)
Methylation of arginine (Arg) and lysine residues in histones has been correlated with epigenetic forms of gene regulation. Although histone methyltransferases are known, enzymes that demethylate histones have not been identified. Here, we demonstrate that human peptidylarginine deiminase 4 (PAD4)
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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