SRP0329
PADI-4 human
recombinant, expressed in baculovirus infected Sf9 cells, ≥65% (SDS-PAGE)
别名:
Peptidyl arginine deiminase, type IV
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关于此项目
NACRES:
NA.32
UNSPSC Code:
12352200
Form:
aqueous solution
Assay:
≥65% (SDS-PAGE)
Biological source:
human
Recombinant:
expressed in baculovirus infected Sf9 cells
Mol wt:
75 kDa
产品名称
PADI-4 human, recombinant, expressed in baculovirus infected Sf9 cells, ≥65% (SDS-PAGE)
biological source
human
recombinant
expressed in baculovirus infected Sf9 cells
assay
≥65% (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 ... PADI4(23569)
Application
Useful for the study of enzyme kinetics, screening inhibitors, and selectivity profiling.
Biochem/physiol Actions
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.
General description
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.
存储类别
10 - Combustible liquids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
法规信息
新产品
此项目有
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)
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)
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)
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