Recombinant Mouse Arginase-1 (ARG1) Protein (His-SUMO)

Name: Recombinant Mouse Arginase-1 (ARG1) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-03767P
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) Arg1.

Collections: High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Arginase-1 (ARG1) 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	Q61176
Target Symbol	ARG1
Synonyms	Arg1Arginase-1; EC 3.5.3.1; Liver-type arginase; Type I arginase
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MSSKPKSLEIIGAPFSKGQPRGGVEKGPAALRKAGLLEKLKETEYDVRDHGDLAFVDVPNDSSFQIVKNPRSVGKANEELAGVVAEVQKNGRVSVVLGGDHSLAVGSISGHARVHPDLCVIWVDAHTDINTPLTTSSGNLHGQPVSFLLKELKGKFPDVPGFSWVTPCISAKDIVYIGLRDVDPGEHYIIKTLGIKYFSMTEVDKLGIGKVMEETFSYLLGRKKRPIHLSFDVDGLDPAFTPATGTPVLGGLSYREGLYITEEIYKTGLLSGLDIMEVNPTLGKTAEEVKSTVNTAVALTLACFGTQREGNHKPGTDYLKPPK
Expression Range	1-323aa
Protein Length	Full Length
Mol. Weight	50.8kDa
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	Key element of the urea cycle converting L-arginine to urea and L-ornithine, which is further metabolized into metabolites proline and polyamides that drive collagen synthesis and bioenergetic pathways critical for cell proliferation, respectively; the urea cycle takes place primarily in the liver and, to a lesser extent, in the kidneys.; Functions in L-arginine homeostasis in nonhepatic tissues characterized by the competition between nitric oxide synthase (NOS) and arginase for the available intracellular substrate arginine. Arginine metabolism is a critical regulator of innate and adaptive immune responses. Involved in an antimicrobial effector pathway in polymorphonuclear granulocytes (PMN). Upon PMN cell death is liberated from the phagolysosome and depletes arginine in the microenvironment leading to suppressed T cell and natural killer (NK) cell proliferation and cytokine secretion. In group 2 innate lymphoid cells (ILC2s) promotes acute type 2 inflammation in the lung and is involved in optimal ILC2 proliferation but not survival. Plays a role in the immune response of alternatively activated or M2 macrophages in processes such as wound healing and tissue regeneration, immune defense against multicellular pathogens and parasites, and immune suppression and allergic inflammation; the regulatory outcome seems to be organ specific. In tumor-infiltrating dendritic cells (DCs) and myeloid-derived suppressor cells (MDSCs) plays a role in suppression of T cell-mediated antitumor immunity.
Subcellular Location	Cytoplasm. Cytoplasmic granule.
Protein Families	Arginase family
Database References	KEGG: mmu:11846 STRING: 10090.ENSMUSP00000020161 UniGene: PMID: 28566761 This study shows for the first time that diabetes-induced increases in arginase 1 expression promotes endothelial cell senescence through the activation of p16INK4A and p53 signaling pathways. PMID: 29673160 findings identified a novel function of the VEGFR1 signaling in avoiding over-expression of Arginase 1 potentially to maintain the proper innate immune response. PMID: 29110610 Up-regulation of arginase 1 expression/activity in vascular endothelial cells has an integral role in diet-induced cardiovascular dysfunction and metabolic syndrome. PMID: 29048462 Complete ablation of Arg1 in the lung affects mRNA abundance of arginine-transporting and -metabolizing genes, and pro-inflammatory genes, but not methacholine responsiveness or accumulation of inflammatory cells. PMID: 29183288 Data suggest that Arg1 mRNA and protein expression in liver are significantly higher in obese mice (fed high-fat diet) than in control mice; hepatic Arg1 levels positively correlate with plasma Arg1 levels and negatively correlate with L-arginine bioavailability in plasma. Increased expression of hepatic Arg1 and reduced plasma L-arginine and NO(2)(-) may lead to vascular endothelial dysfunction even in early obesity. PMID: 29098611 Data suggest that chronic hypoxia enhances HIF-2alpha stability, which causes increased arginase expression and dysregulates normal vascular NO homeostasis. PMID: 27432976 high-fat/high-sucrose diet-induced visceral adipose tissue inflammation is mediated by endothelial cells-A1 expression/activity. PMID: 28835451 Deletion of Arg1 in hematopoietic cells adversely affects blood leukocyte counts and increases foam cell formation. However, no effects on atherosclerosis could be demonstrated, indicating that hematopoietic Arg1 function is not a decisive factor in atherosclerotic plaque formation. PMID: 27998825 diabetes-dependent increase in renal arginase-2 expression also requires arginase-1 expression in macrophages PMID: 28446459 this study shows that mice lacking Arg1 in macrophages develop increased allergic contact hypersensitivity PMID: 28747341 this study shows that Ron is expressed in a subpopulation of macrophages during chronic inflammation induced by obesity that exhibit a repair phenotype as determined by the expression of arginase 1 PMID: 27233965 Arginase 1 was highly expressed by tumor-associated Gr1+ microglia and macrophages. PMID: 27936099 This study uncovers synergistic activation of Arg1 by retinoic acid and IL-4 in M2 macrophages. PMID: 27166374 this study shows that group 2 innate lymphoid cells selectively express arginase 1 and that this is critical for their bioenergetics, proliferation and function PMID: 27043409 this study shows that c-Jun regulates the activation state of macrophages and promotes arthritis via differentially regulating cyclooxygenase-2 and arginase-1 levels PMID: 28298526 deletion or TNF-mediated restriction of Arg1 unleashes the production of nitric oxide by NOS2, which is critical for pathogen control. PMID: 27117406 Data indicate that transfected mouse arginase-1 (Arg-I) promotes endothelial senescence and inflammatory responses through eNOS-uncoupling in human umbilical vein endothelial cells (HUVEC cells). PMID: 28153047 Arg1 is down-regulated during osteoclast differentiation and may negatively regulate osteoclast differentiation by regulating nitric oxide production. PMID: 26475291 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. PMID: 26704078 T Lymphocyte Inhibition by Tumor-Infiltrating Dendritic Cells Involves Ectonucleotidase CD39 but Not Arginase-1. PMID: 26491691 The production of arginase-1 by tumor cells leads to an ineffective anti-tumor immune response. PMID: 24614600 Arg1+ microglia are involved in Abeta plaque reduction during sustained, IL-1beta-dependent neuroinflammation PMID: 26538310 findings suggest that increased IL-17A expression by macrophages in E7-expressing skin exposed to DNCB promotes arginase-1 induction and contributes directly to the observed hyperinflammation. PMID: 25720383 Arginase 1 is crucially involved in Ang II-induced smooth muscle cell proliferation and arterial fibrosis and stiffness and represents a promising therapeutic target. PMID: 25807386 FoxO4 activates Arg1 transcription in endothelial cells in response to MI, leading to downregulation of nitric oxide and upregulation of neutrophil infiltration to the infarct area. PMID: 26438688 TAT fused to WW2/WW3 of Smurf2 could interfere with TGF-beta signaling and reduce ArgI gene expression. PMID: 25612247 ARG1 activity may participate in the pathogenesis of lymphoproliferative and myeloproliferative disorders. PMID: 26363032 data indicate that helminth coinfection induces arginase-1-expressing type 2 granulomas, thereby increasing inflammation and TB disease severity. PMID: 26571397 Flow cytometric analysis of intrasplenic leukocytes exposed the presence of a transient population of activated neutrophils that correlated quantitatively with elevated ArgI levels in culture media PMID: 25966956 Arginase 1 activity worsens lung-protective immunity against Streptococcus pneumoniae infection. PMID: 25789453 Arg1 expression is decreased, and Arg2 expression is increased in the newborn congenital obstructive nephropathy and in the mouse model. PMID: 25205225 Promoter region methylation was decreased at Arg1 in THC-induced myeloid-derived suppressor cells, which then expressed higher Arg1 levels. PMID: 25713087 Arg1 plays a central role in the control of TB when NOS2 is rendered ineffective by hypoxia. PMID: 25201986 arginase I activity is required for M2 macrophages mediated protection during DSS-induced colitis in PI3Kp110delta-deficient mice. PMID: 25124254 the cross talk between HDAC4 and STAT6 is an important regulatory mechanism of Arg1 transcription in dendritic cells PMID: 25332236 Diabetic mice exhibit elevated vascular Arg1 and impaired vascular endothelial and nitrergic function. PMID: 23977269 A myeloid cell uptake of damaged retinal pigment epithelium or its derivatives as a mechanism generating VEGF (+) Arg-1(+) phenotype in vivo, is demonstrated. PMID: 23977372 Our results demonstrate that HPV16.E7 protein enhances drug associated production of arginase-1 by myeloid cells and consequent inflammatory cellular infiltration of skin. PMID: 24732401 Reduced arginase-1 activity in Arg1(fl/fl)/Tie2-Cre(tg/-) mice resulted in increased inflammatory response and nitric oxide production by NOS2. PMID: 24465919 these data support the notion that PTEN contributes to cell fate decisions of macrophages exemplified by increased Arginase I expression. PMID: 25015834 tumor myeloid cells inhibit the adaptive immune response after radiation therapy through expression of the enzyme arginase I PMID: 24992164 neither induction of alternative activation nor expression of arginase1 are critical features of disease mediated by attenuated or virulent Francisella species. PMID: 24324751 A kinesin heavy chain released by T. brucei induces IL-10 and arginase-1 through SIGN-R1 signaling in myeloid cells, which promotes early trypanosome growth and favors parasite settlement in the host. PMID: 24204274 ATRA enhances both Arg-1 and iNOS expression in IFN-gamma-treated DCs, resulting in a tolerogenic phenotype. PMID: 24790153 Murine primary macrophages treated with HDL showed increased gene expression for the M2 markers Arginase-1 (Arg-1) and Fizz-1 PMID: 23991225 ILC2s are a novel source of Arg1 in resting tissue and during allergic inflammation. PMID: 23924659 In preclinical murine models reduced Arg expression directly correlates with delayed healing of skin wounds. PMID: 23552798 Our objective was to elucidate mechanisms involved in modulating arginase I induction by IL-4 in murine M2 macrophages PMID: 23913966 wall shear stress is a key biomechanical regulator of arginase during atherosclerotic plaque formation and stability PMID: 23390893

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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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