Recombinant Mouse Arginase-2, Mitochondrial (ARG2) Protein (His-SUMO)

Name: Recombinant Mouse Arginase-2, Mitochondrial (ARG2) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-02791P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Based on the SEQUEST from database of E.coli host and target protein, the LC-MS/MS Analysis result of this product could indicate that this peptide derived from E.coli-expressed Mus musculus (Mouse) Arg2.

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Product Overview

Description	Recombinant Mouse Arginase-2, Mitochondrial (ARG2) Protein (His-SUMO) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	O08691
Target Symbol	ARG2
Synonyms	Arg2Arginase-2; mitochondrial; EC 3.5.3.1; Arginase II; Kidney-type arginase; Non-hepatic arginase; Type II arginase
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	VHSVAIVGAPFSRGQKKLGVEYGPAAIREAGLLKRLSRLGCHLKDFGDLSFTNVPQDDPYNNLVVYPRSVGLANQELAEVVSRAVSGGYSCVTMGGDHSLAIGTIIGHARHRPDLCVIWVDAHADINTPLTTVSGNIHGQPLSFLIKELQDKVPQLPGFSWIKPCLSPPNIVYIGLRDVEPPEHFILKNYDIQYFSMREIDRLGIQKVMEQTFDRLIGKRQRPIHLSFDIDAFDPKLAPATGTPVVGGLTYREGVYITEEIHNTGLLSALDLVEVNPHLATSEEEAKATARLAVDVIASSFGQTREGGHIVYDHLPTPSSPHESENEECVRI
Expression Range	23-354aa
Protein Length	Full Length of Mature Protein
Mol. Weight	52.4kDa
Research Area	Others
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Mitochondrion.
Protein Families	Arginase family
Database References	KEGG: mmu:11847 STRING: 10090.ENSMUSP00000021550 UniGene: PMID: 27406916 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 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 Arginase II expression is reduced in aortic endothelial cells and macrophages following PARP-1 knockout. PMID: 27757983 This study shows for the first time that neurovascular injury after retinal ischemia/reperfusion is mediated through increased expression of Arginase 2. PMID: 27882947 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 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 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 Arg-II, p38, and S6K1 form a positive circuit which regulates endothelial senescence and cardiovascular aging. PMID: 25635535 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 ERK2 and p38 regulate arginase II induction in LPS-stimulated macrophages, but iNOS induction by LPS is dependent on p38 activation PMID: 25451938 OxLDL triggers retrograde translocation of arginase2 in aortic endothelial cells via ROCK and mitochondrial processing peptidase. PMID: 24903103 Suggest that retinal arginase is involved in the hyperoxia-induced neuronal degeneration in the OIR model, through the regulation of polyamine metabolism. PMID: 24556690 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 HDAC2 is a critical regulator of Arg2 expression and thereby endothelial nitric oxide and endothelial function. PMID: 24833798 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 ROCK 2, p38 MAPK and arginase play key roles in diabetes-induced impairment of corpora cavernosa relaxation. PMID: 23566117 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 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 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 A novel mechanism has been uncovered for mutual positive regulation between S6K1 and Arg-II in endothelial inflammation and aging. PMID: 22928666 IL-13 contributes to the development of pulmonary hypertension via an IL-13receptor alpha2-arginase 2-dependent pathway. PMID: 23125252 inhibition of Arg2 increases L-arginine levels, diminishes ROS production and ameliorates nitrate tolerance PMID: 22288373 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 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 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 a high fat diet affects arginase activities and global arginine bioavailability in wild-type and ApoE-deficient mice PMID: 21151916 Helicobacter infection induces Arg2 (but not Arg1) in gastric lamina propria macrophages. PMID: 21296975 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 Data suggest that arginase II present in the small intestinal mucosa has the role of providing ornithine for citrulline synthesis. PMID: 20978229 arginase II deficiency leads to a better CBF recovery after TBI and implicates arginase II in hemodynamic processes. PMID: 20372170 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 Arginase II expression in mouse embryonic development PMID: 12049781 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 Variations of the levels of OAT protein and arginase II mRNA and protein were strongly correlated with testosteronemia. PMID: 15539552 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 Arg2 is an anti-inflammatory target of liver X receptor in macrophages. PMID: 16943198 Endothelial cell mitochondrial arginase II regulates NO production, vascular endothelial function, and vascular stiffness by modulating NOS-3 activity. PMID: 17827260 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 arginase II plays a critical role in the pathophysiology of cholesterol-mediated endothelial dysfunction PMID: 18309100 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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