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SRP0329

Sigma-Aldrich

PADI-4 human

recombinant, expressed in baculovirus infected Sf9 cells, ≥65% (SDS-PAGE)

Synonym(s):

Peptidyl arginine deiminase, type IV

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About This Item

UNSPSC Code:
12352200
NACRES:
NA.32

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)

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.

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.

WGK

WGK 3

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Regulatory Information

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Certificates of Analysis (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.
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)
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)
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

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