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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.
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Human Monoclonal PADI2 Primary Antibody pour ELISA, WB - ABIN564891
Blachère, Parveen, Fak, Frank, Orange: Inflammatory but not apoptotic death of granulocytes citrullinates fibrinogen. dans Arthritis research & therapy 2015
the mRNA expression of PADI2, PADI4 (Montrer PADI4 Anticorps) and Sp1 (Montrer PSG1 Anticorps) is upregulated in rheumatoid arthritis bone marrow CD34 (Montrer CD34 Anticorps)+ cells independently of the systemic inflammation or treatment regimen.
These data suggest that overexpression of the human PAD2 transgene in the epidermis of transgenic mice increases the malignant conversion rate of benign tumors by promoting an inflammatory microenvironment.
Brain gene expression of PADI2, ZNF385A (Montrer ZNF385A Anticorps), PSD2, and A2ML1 (Montrer A2ML1 Anticorps) and DNA methylation (Montrer HELLS Anticorps) dysregulations are implicated in the alteration of brain tissue properties associated with late-life cognitive decline above and beyond the influence of common neuropathologic conditions.
Peptidyl arginine deiminase 2 (PADI2) is required for activation of androgen receptor (AR (Montrer AR Anticorps)) signaling under androgen-deprived condition.
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 (Montrer MLXIP Anticorps)-4728 downregulates PADI2, a novel rheumatoid arthritis risk gene
We identified the presence of PADI3 (Montrer PADI3 Anticorps) mRNA expression in synovial tissue and PADI2 and PADI4 (Montrer PADI4 Anticorps) mRNA expressions in fibroblast-like synoviocytes from patients with rheumatoid arthritis.
PADi2 contributes to TNFalpha (Montrer TNF Anticorps)-induced citrullination and arthritis, but is not required for neutrophil extracellular traps formation
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 (Montrer GPX7 Anticorps) is an unusual CysGPx catalyzing the peroxidatic cycle by a one Cys (Montrer DNAJC5 Anticorps) mechanism in which GSH and PDI (Montrer PDIA3 Anticorps) are alternative substrates.
Results suggest that PADI2 may function as an important new biomarker for HER2/ERBB2 (Montrer ERBB2 Anticorps)+ tumors and that Cl-amidine represents a new candidate for breast cancer therapy.
Activation of the P2X7 purinergic receptor (P2X7 (Montrer P2RX7 Anticorps)) 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 (Montrer IKBKG Anticorps) and suppresses NF-kappaB (Montrer NFKB1 Anticorps) 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 (Montrer PRNP Anticorps) diseases and serve as potential therapeutic targets.
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