Arg2 Antibody

Code CSB-PA002006LA01MO
Size US$166
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  • Western blot
    All lanes: Arg2 antibody at 10µg/ml + Jurkat whole cell lysate
    Secondary
    Goat polyclonal to rabbit IgG at 1/10000 dilution
    Predicted band size: 39 kDa
    Observed band size: 39 kDa
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Product Details

Full Product Name
Rabbit anti-Mus musculus (Mouse) Arg2 Polyclonal antibody
Uniprot No.
Target Names
Arg2
Alternative Names
Arg2Arginase-2 antibody; mitochondrial antibody; EC 3.5.3.1 antibody; Arginase II antibody; Kidney-type arginase antibody; Non-hepatic arginase antibody; Type II arginase antibody
Raised in
Rabbit
Species Reactivity
Mouse, Human
Immunogen
Recombinant Mouse Arginase-2, mitochondrial protein (23-354AA)
Immunogen Species
Mus musculus (Mouse)
Conjugate
Non-conjugated

The Arg2 Antibody (Product code: CSB-PA002006LA01MO) is Non-conjugated. For Arg2 Antibody with conjugates, please check the following table.

Available Conjugates
Conjugate Product Code Product Name Application
HRP CSB-PA002006LB01MO Arg2 Antibody, HRP conjugated ELISA
FITC CSB-PA002006LC01MO Arg2 Antibody, FITC conjugated
Biotin CSB-PA002006LD01MO Arg2 Antibody, Biotin conjugated ELISA
Clonality
Polyclonal
Isotype
IgG
Purification Method
>95%, Protein G purified
Concentration
It differs from different batches. Please contact us to confirm it.
Buffer
Preservative: 0.03% Proclin 300
Constituents: 50% Glycerol, 0.01M PBS, PH 7.4
Form
Liquid
Tested Applications
ELISA, WB
Recommended Dilution
Application Recommended Dilution
WB 1:500-1:2000
Troubleshooting and FAQs
Storage
Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.
Lead Time
Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Customer Reviews and Q&A

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Target Background

Function
May play a role in the regulation of extra-urea cycle arginine metabolism and also in down-regulation of nitric oxide synthesis. Extrahepatic arginase functions to regulate L-arginine bioavailability to nitric oxid synthase (NOS). Arginine metabolism is a critical regulator of innate and adaptive immune responses. Seems to be involved in negative regulation of the survival capacity of activated CD4(+) and CD8(+) T cells. May suppress inflammation-related signaling in asthmatic airway epithelium. May contribute to the immune evasion of H.pylori by restricting M1 macrophage activation and polyamine metabolism. May play a role in promoting prenatal immune suppression. Regulates RPS6KB1 signaling, which promotes endothelial cell senescence and inflammation and implicates NOS3/eNOS dysfunction. Can inhibit endothelial autophagy independently of its enzymatic activity implicating mTORC2 signaling. Involved in vascular smooth muscle cell senescence and apoptosis independently of its enzymatic activity.
Gene References into Functions
  1. The possibility that the Gas6-Mer-PI3K/Akt-STAT1-LXR-Arg2 pathway plays an essential role for resolving inflammatory response in acute lung injury. PMID: 27406916
  2. ARG2 which hydrolyzes arginine into ornithine and urea, is induced upon obesity, and silencing or loss of ARG2 markedly suppresses pancreatic ductal adenocarcinoma. PMID: 28808255
  3. the finding of this study is that ARG2 contributes to the immune evasion of H. pylori by restricting M1 macrophage activation and polyamine metabolism. PMID: 27074721
  4. Arginase II expression is reduced in aortic endothelial cells and macrophages following PARP-1 knockout. PMID: 27757983
  5. This study shows for the first time that neurovascular injury after retinal ischemia/reperfusion is mediated through increased expression of Arginase 2. PMID: 27882947
  6. Arg2 KO female (not male) mice are protected from age-associated glucose intolerance and reveal greater glucose induced-insulin release, larger islet size and beta-cell mass, and more proliferative and less apoptotic beta-cells compared with the age-matched WT controls. Arg2 is mainly expressed in acinar cells and is upregulated with aging, which enhances p38 MAPK activation and release of TNF-alpha. PMID: 28356309
  7. arginase 2 impairs endothelial autophagy independently of the L-arginine ureahydrolase activity through activation of RPS6KB1 and inhibition of PRKAA, which is implicated in atherogenesis PMID: 25484082
  8. high fat diet enhanced arginase-II expression/activity and p38mapk activity, which was associated with eNOS-uncoupling as revealed by decreased nitric oxide PMID: 25034973
  9. Arg-II, p38, and S6K1 form a positive circuit which regulates endothelial senescence and cardiovascular aging. PMID: 25635535
  10. Arginase 2 deletion prevents hyperoxia-induced retinal vascular injury by preventing NOS uncoupling resulting in decreased reactive oxygen species formation and increased nitric oxide bioavailability. PMID: 25375125
  11. ERK2 and p38 regulate arginase II induction in LPS-stimulated macrophages, but iNOS induction by LPS is dependent on p38 activation PMID: 25451938
  12. OxLDL triggers retrograde translocation of arginase2 in aortic endothelial cells via ROCK and mitochondrial processing peptidase. PMID: 24903103
  13. Suggest that retinal arginase is involved in the hyperoxia-induced neuronal degeneration in the OIR model, through the regulation of polyamine metabolism. PMID: 24556690
  14. miR155-induced repression of Arg2 expression is critical for the ability of dendritic cells to drive T cell activation by controlling arginine availability in the extracellular environment. PMID: 25009204
  15. HDAC2 is a critical regulator of Arg2 expression and thereby endothelial nitric oxide and endothelial function. PMID: 24833798
  16. Arginase inhibition mediates renal tissue protection in diabetic nephropathy by an eNOS-dependent mechanism and has an eNOS-independent effect on kidney macrophage recruitment. PMID: 23760286
  17. ROCK 2, p38 MAPK and arginase play key roles in diabetes-induced impairment of corpora cavernosa relaxation. PMID: 23566117
  18. Arg-II promotes mitochondrial dysfunction leading to VSMC senescence/apoptosis through complex positive crosstalk among S6K1-JNK, ERK, p66Shc, and p53, contributing to atherosclerotic vulnerability phenotype. PMID: 23832324
  19. Studied thoracic aorta from ApoE-/- mice, and found the high-cholesterol diet (HCD) induced an increase in arginase activity, a decrease in NO release and an increase in reactive oxygen species generation that was reversed by treatment with PG. PMID: 23443634
  20. Arginase II is upregulated in aortic vessels of aged mice and contributes to decreased nitric oxide generation and increased reactive oxygen species production via endothelial nitric oxide synthase uncoupling. PMID: 22854495
  21. A novel mechanism has been uncovered for mutual positive regulation between S6K1 and Arg-II in endothelial inflammation and aging. PMID: 22928666
  22. IL-13 contributes to the development of pulmonary hypertension via an IL-13receptor alpha2-arginase 2-dependent pathway. PMID: 23125252
  23. inhibition of Arg2 increases L-arginine levels, diminishes ROS production and ameliorates nitrate tolerance PMID: 22288373
  24. In diabetes models, kidney Arg2 increases as diabetes develops (but not in diabetic Arg2-deficient mice). Increase in kidney arginase activity is associated with loss of renal function; such function loss is not seen in diabetic Arg2-deficient mice. PMID: 21926276
  25. Data suggest that the in vivo source for the essential urea utilized by H. pylori urease is neither bacterial arginase nor host arginase II; instead, either residual host arginase I or agmatinase is probably responsible. PMID: 21876618
  26. data implicate Arg2 in neurodegeneration during retinopathy of prematurity; deletion significantly improves neuronal survival and function, possibly through the regulation of mitochondrial membrane permeability mediated apoptosis during retinal ischemia PMID: 21811615
  27. a high fat diet affects arginase activities and global arginine bioavailability in wild-type and ApoE-deficient mice PMID: 21151916
  28. Helicobacter infection induces Arg2 (but not Arg1) in gastric lamina propria macrophages. PMID: 21296975
  29. Delineate a clearer path from OxLDL through the endothelial cell LOX-1 receptor, RhoA, and ROCK, to the activation of arginase II, downregulation of NO, and vascular dysfunction in atherosclerosis. PMID: 21130456
  30. Data suggest that arginase II present in the small intestinal mucosa has the role of providing ornithine for citrulline synthesis. PMID: 20978229
  31. arginase II deficiency leads to a better CBF recovery after TBI and implicates arginase II in hemodynamic processes. PMID: 20372170
  32. Studies implicate Arg2 in the immune evasion of H. pylori by causing intracellular depletion of l-arginine and thus reduction of NO-dependent bactericidal activity. PMID: 20097867
  33. Arginase II expression in mouse embryonic development PMID: 12049781
  34. Arginase II mRNA levels and enzyme activity in macrophages from Trypanosoma brucei brucei-infected mice are higher in susceptible BALB/c mice compared with resistant C57BL/6 mice. PMID: 15128819
  35. Variations of the levels of OAT protein and arginase II mRNA and protein were strongly correlated with testosteronemia. PMID: 15539552
  36. AII was expressed in the cortex and the outer stripe of outer medulla, urea was produced mainly in the proximal tubules, the 38-kDa AII protein was more abundant in the mitochondria than the cytosol, and AII was three-fold higher in females than males PMID: 15616821
  37. Arg2 is an anti-inflammatory target of liver X receptor in macrophages. PMID: 16943198
  38. Endothelial cell mitochondrial arginase II regulates NO production, vascular endothelial function, and vascular stiffness by modulating NOS-3 activity. PMID: 17827260
  39. These results suggested that an increase in arginase may lead to decreased availability of arginine for nitric oxide synthase and may contribute to the remodeling of the lung. PMID: 17890324
  40. arginase II plays a critical role in the pathophysiology of cholesterol-mediated endothelial dysfunction PMID: 18309100
  41. Lack of arginase II in the TRAMP model seems to speed up the tumor progression process leading to a more aadvanced cancer state in these mice. PMID: 18663728

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Subcellular Location
Mitochondrion.
Protein Families
Arginase family
Database Links
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