Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human ARG1 Protein expressed in Escherichia coli (E. coli) - ABIN2666493
Babu, Kumaraswami, Nutman: Alternatively activated and immunoregulatory monocytes in human filarial infections. in The Journal of infectious diseases 2009
Show all 8 references for ABIN2666493
Human ARG1 Protein expressed in HEK-293 Cells - ABIN2180550
Ikemoto, Tabata, Miyake, Kono, Mori, Totani, Murachi: Expression of human liver arginase in Escherichia coli. Purification and properties of the product. in The Biochemical journal 1990
Show all 4 references for ABIN2180550
Human ARG1 Protein expressed in Escherichia coli (E. coli) - ABIN667001
Iyer, Yoo, Kern, Rozengurt, Tsoa, OBrien, Yu, Grody, Cederbaum: Mouse model for human arginase deficiency. in Molecular and cellular biology 2002
Show all 2 references for ABIN667001
Human ARG1 Protein expressed in Human Cells - ABIN2004367
Haffner, Teupser, Holdt, Ernst, Burkhardt, Thiery: Regulation of arginase-1 expression in macrophages by a protein kinase A type I and histone deacetylase dependent pathway. in Journal of cellular biochemistry 2008
Evidence for a negative association of arginase I with job strain and positive association with job control and social support in females.
Two argininemia patients were initially diagnosed by tandem mass spectrometry in newborn screening. Mutation analysis of the ARG1 gene was performed by direct sequencing.Two missense mutations, p.D100N and p.R71T, in Patient-1 were predicted to lower the stability of arginase Iota by analysis of 3D crystal structure, while two nonsense mutations, p.G12X and p.E42X, in Patient-2 were predicted to lead to truncated protein.
The results of this study suggested a novel relationship exists between ARG1, neutrophil-lymphocyte ratio , and stroke severity which may help guide future mechanistic studies of post-stroke immune suppression.
This study provides a molecular mechanism of the pathogenesis of systemic lupus erythematosus by demonstrating an Arg-1-dependent effect of myeloid-derived suppressor cells in the development of TH17 cell-associated autoimmunity.
ARG1 rs2781659 AA and rs2781667 TT genotypes were associated with lower IIEF scores (increased severity) in clinical erectile dysfunction (ED), whereas ARG1 GTCC haplotype is associated with higher IIEF scores in clinical ED, thus suggesting a genetic contribution of ARG1 variations to ED
These results showed that alterations in the expression levels of Arg I and iNOS (show NOS2 Proteins) in the peripheral T cells and peripheral nodes of HIV infected patients are associated with disease progression in these patients.
Increased ARG1 expression in macrophages after a single radiotherapy dose is an independent prognostic factor of skin toxicities.
Arginase inhibition arrests human pulmonary artery smooth muscle cells in the G1/G0-phase under hypoxic conditions.
Arginase from neutrophils can modulate nitric oxide production from activated macrophages which may affect the course of infection by intracellular bacteria.
Overexpression and elevated activity of arginase I are involved in tobacco-induced pulmonary endothelial dysfunction.
Arginase has a role in preventing angiogenesis in endothelial cells exposed to hypoxia
Ang II (show AGT Proteins) increases endothelial arginase activity/expression through a p38 MAPK (show MAPK14 Proteins)/ATF-2 (show ATF2 Proteins) pathway leading to reduced endothelial NO production
results indicate that arginase induction depends in part on epidermal growth factor (EGF (show EGF Proteins)) receptor (show EGFR Proteins) activity, and that EGFR (show EGFR Proteins) inhibitors may attenuate vascular remodeling without affecting nitric oxide release
high glucose (HG)-treated bovine coronary endothelial cells (BCECs) showed increased arginase activity and diminished NO production
this study shows that c-Jun (show JUN Proteins) regulates the activation state of macrophages and promotes arthritis via differentially regulating cyclooxygenase-2 (show PTGS2 Proteins) and arginase-1 levels
deletion or TNF-mediated restriction of Arg1 unleashes the production of nitric oxide by NOS2, which is critical for pathogen control.
Data indicate that transfected mouse arginase-1 (Arg-I) promotes endothelial senescence and inflammatory responses through eNOS (show NOS3 Proteins)-uncoupling in human umbilical vein endothelial cells (HUVEC cells).
Arg1 is down-regulated during osteoclast differentiation and may negatively regulate osteoclast differentiation by regulating nitric oxide production.
Results show that arginase 1 is abundantly present in the bone and bone marrow stromal cells and reveal the role of its deregulation in diabetes-induced bone complications. * HFHS diet induced Arginase activity and expression in bone and bone marrow.
T Lymphocyte Inhibition by Tumor-Infiltrating Dendritic Cells Involves Ectonucleotidase CD39 (show ENTPD1 Proteins) but Not Arginase-1.
The production of arginase-1 by tumor cells leads to an ineffective anti-tumor immune response.
Arg1+ microglia are involved in Abeta (show APP Proteins) plaque reduction during sustained, IL-1beta (show IL1B Proteins)-dependent neuroinflammation
findings suggest that increased IL-17A (show IL17A Proteins) expression by macrophages in E7-expressing skin exposed to DNCB promotes arginase-1 induction and contributes directly to the observed hyperinflammation.
Arginase 1 is crucially involved in Ang II (show AGT Proteins)-induced smooth muscle cell proliferation and arterial fibrosis and stiffness and represents a promising therapeutic target.
The immunosuppressive effect of a purified substance (ISF (show ATP6V0A2 Proteins)) in the culture medium of neonatal pig liver fragments was due to arginase activity that decreased arginine concentration in culture medium, not to another function of ISF (show ATP6V0A2 Proteins).
Results show that ischemia markedly potentiated the expression of arginase-1, and also induced the SOD2 (show SOD2 Proteins) in the wound tissue.
Arginase catalyzes the hydrolysis of arginine to ornithine and urea. At least two isoforms of mammalian arginase exist (types I and II) which differ in their tissue distribution, subcellular localization, immunologic crossreactivity and physiologic function. The type I isoform encoded by this gene, is a cytosolic enzyme and expressed predominantly in the liver as a component of the urea cycle. Inherited deficiency of this enzyme results in argininemia, an autosomal recessive disorder characterized by hyperammonemia. Two transcript variants encoding different isoforms have been found for this gene.
, liver-type arginase
, type I arginase
, arginase 1
, arginase I
, arginase 1, liver
, AI type I arginase
, arginase, hepatic