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PADI2 encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. Additionally we are shipping Peptidyl Arginine Deiminase, Type II Proteins (18) and Peptidyl Arginine Deiminase, Type II Kits (14) and many more products for this protein.
Showing 10 out of 67 products:
Human Monoclonal PADI2 Primary Antibody for ELISA, WB - ABIN564891
Blachère, Parveen, Fak, Frank, Orange: Inflammatory but not apoptotic death of granulocytes citrullinates fibrinogen. in Arthritis research & therapy 2015
Data suggest that protein-arginine deiminase 2 (PADI2) suppresses the proliferation of colonic epithelial cells through catalysis of protein citrullination, and that downregulation of PADI2 expression might therefore contribute to colon carcinogenesis.
Downregulation of PADI2 is an early event in the pathogenesis of colorectal cancer associated with poor prognosis and points toward a possible role of citrullination in modulating tumor cells and their microenvironment.
Multiple proteins citrullinated by hypoxia-induced PADs were identified. In addition, the extracellular domain of vascular endothelial growth factor receptor 2 was citrullinated by human PAD2 in vitro. CONCLUSION: Our data may contribute to understanding of pathophysiology of malignant gliomas from the aspects of protein citrullination.
Deimination of myelin basic protein (MBP) by peptidylarginine deiminase (PAD) prevents its binding to the proteasome and decelerates its degradation by the proteasome in mammalian cells. Potential anticancer drug tetrazole analogue of chloramidine 2, at concentrations greater than 1 microM inhibits the enzymatic activity of PAD in vitro.
this study shows that a miR (show MLXIP Antibodies)-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene
We identified the presence of PADI3 (show PADI3 Antibodies) mRNA expression in synovial tissue and PADI2 and PADI4 (show PADI4 Antibodies) mRNA expressions in fibroblast-like synoviocytes from patients with rheumatoid arthritis.
Protein arginine deiminase 2 binds six calcium ions in an ordered fashion.
PAD2 activity was significantly higher in cell-free synovial fluid of rheumatoid arthritis patients compared to osteoarthritis patients.
PAD2 activity was detected in synovial fluid samples from patients with rheumatoid arthritis.
Report increased levels of extracellular PAD2 in the lungs of smokers.
Taken together, our study is the first to indicate the potential role of Padi2 as an angiogenesis-regulating gene. The characterization of Padi2 and other genes in associated pathways may provide new understanding of angiogenesis regulation and novel targets for diagnosis and treatment of a wide variety of angiogenesis-dependent diseases.
GPx7 (show GPX7 Antibodies) is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys (show DNAJC5 Antibodies) mechanism in which GSH and PDI (show PDIA3 Antibodies) are alternative substrates.
Results suggest that PADI2 may function as an important new biomarker for HER2/ERBB2 (show ERBB2 Antibodies)+ tumors and that Cl-amidine represents a new candidate for breast cancer therapy.
Activation of the P2X7 purinergic receptor (P2X7 (show P2RX7 Antibodies)) by the inflammatory danger signal ATP induces PAD2 activity and robust protein citrullination in mast cells.
different subcellular compartmentalization of PADi2 and citrullinated proteins may have different physiological roles in normal and neurodegenerative conditions
PAD2 interacts with IKKgamma (show IKBKG Antibodies) and suppresses NF-kappaB (show NFKB1 Antibodies) activity.
Results suggest that peptidylarginine deiminase 2-catalyzed citrullination is not essential to the development of experimental autoimmune encephalomyelitis.
An increase in citrullinated proteins resulting from increased PAD2 and 4 is an important change in the pathogenesis of multiple sclerosis.
This study suggests that accumulated citrullinated proteins and abnormal activation of PAD2 may function in the pathogenesis of prion (show PRNP Antibodies) diseases and serve as potential therapeutic targets.
elevated levels of the pro-inflammatory cytokine TNF-alpha and nuclear histone deimination support initiation of demyelination by increased PAD activity
This gene encodes a member of the peptidyl arginine deiminase family of enzymes, which catalyze the post-translational deimination of proteins by converting arginine residues into citrullines in the presence of calcium ions. The family members have distinct substrate specificities and tissue-specific expression patterns. The type II enzyme is the most widely expressed family member. Known substrates for this enzyme include myelin basic protein in the central nervous system and vimentin in skeletal muscle and macrophages. This enzyme is thought to play a role in the onset and progression of neurodegenerative human disorders, including Alzheimer disease and multiple sclerosis, and it has also been implicated in glaucoma pathogenesis. This gene exists in a cluster with four other paralogous genes.
peptidyl arginine deiminase, type II
, protein-arginine deiminase type-2-like
, peptidlyarginine deiminase type II
, peptidylarginine deiminase II
, protein arginine deiminase
, protein-arginine deiminase type II
, protein-arginine deiminase type-2
, peptidyl arginine deiminase, type 2
, PAD type II
, peptidyl arginine deiminase, type II; PAD type II