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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. Zusätzlich bieten wir Ihnen Peptidyl Arginine Deiminase, Type II Antikörper (67) und Peptidyl Arginine Deiminase, Type II Proteine (18) und viele weitere Produktgruppen zu diesem Protein an.
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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 (zeige MLXIP ELISA Kits)-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene
We identified the presence of PADI3 (zeige PADI3 ELISA Kits) mRNA expression in synovial tissue and PADI2 and PADI4 (zeige PADI4 ELISA Kits) 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 (zeige GPX7 ELISA Kits) is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys (zeige DNAJC5 ELISA Kits) mechanism in which GSH and PDI (zeige PDIA3 ELISA Kits) are alternative substrates.
Results suggest that PADI2 may function as an important new biomarker for HER2/ERBB2 (zeige ERBB2 ELISA Kits)+ tumors and that Cl-amidine represents a new candidate for breast cancer therapy.
Activation of the P2X7 purinergic receptor (P2X7 (zeige P2RX7 ELISA Kits)) 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 (zeige IKBKG ELISA Kits) and suppresses NF-kappaB (zeige NFKB1 ELISA Kits) 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 (zeige PRNP ELISA Kits) 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