Recombinant Human ARG1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0254

Recombinant Human ARG1 Protein (His Tag)

Beta LifeScience SKU/CAT #: BLPSN-0254
Our products are highly customizable to meet your specific needs. You can choose options such as endotoxin removal, liquid or lyophilized forms, preferred tags, and the desired functional sequence range for proteins. Submitting a written inquiry expedites the quoting process.

Submit an inquiry today to inquire about all available size options and prices! Connect with us via the live chat in the bottom corner to receive immediate assistance.

Product Overview

Tag His
Host Species Human
Accession P05089
Synonym ARG1
Background Arginase is the focal enzyme of the urea cycle hydrolysing L-arginine to urea and L-ornithine. Emerging studies have identified arginase in the vasculature and have implicated this enzyme in the regulation of nitric oxide (NO) synthesis and the development of vascular disease. Arginase also redirects the metabolism of L-arginine to L-ornithine and the formation of polyamines and L-proline, which are essential for smooth muscle cell growth and collagen synthesis. Arginase is encoded by two recently discovered genes (Arginase I and Arginase II). In most mammals, Arginase 1 (ARG1) also known as Arginase, liver, which functions in the urea cycle, and is located primarily in the cytoplasm of the liver. The second isozyme, Arginase II, has been implicated in the regulation of the arginine/ornithine concentrations in the cell. It is located in mitochondria of several tissues in the body, with most abundance in the kidney and prostate. It may be found at lower levels in macrophages, lactating mammary glands, and brain.
Description A DNA sequence encoding the human ARG1 isoform 1 (P05089-1) (Met 1-Lys 322) was fused with a His tag at the C-terminus.
Source HEK293
Predicted N Terminal Met 1
AA Sequence Met 1-Lys 322
Molecular Weight The secreted recombinant human ARG1 consists of 333 a.a. and has a calculated molecular mass of 36.2 kDa. The apparent molecular mass of the protein is approximately 40 kDa in SDS-PAGE under reducing conditions.
Purity >90% as determined by SDS-PAGE
Endotoxin < 1.0 EU per μg of the protein as determined by the LAL method
Bioactivity Measured by the production of urea during the hydrolysis of arginine.The specific activity is >35,000 pmoles/min/ug.
Formulation Lyophilized from sterile 20mM Tris, 150mM NaCl, 20% Glycerol, 1mM DTT, pH 7.4.
Stability The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage For Research Use Only
Storage Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

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. In humans, the immunological role in the monocytic/macrophage/dendritic cell (DC) lineage is unsure.
Subcellular Location Cytoplasm. Cytoplasmic granule.
Protein Families Arginase family
Database References
Associated Diseases Argininemia (ARGIN)
Tissue Specificity Within the immune system initially reported to be selectively expressed in granulocytes (polymorphonuclear leukocytes [PMNs]). Also detected in macrophages mycobacterial granulomas. Expressed in group2 innate lymphoid cells (ILC2s) during lung disease.

Gene Functions References

  1. study of the significance of heat activation and the role of metal ions in human arginase PMID: 30282613
  2. TGF-beta1 and arginase-1 may play important roles in determining long-term graft survival. PMID: 30074212
  3. These results showed that arginase controlled sFlt-1 elevation to some extent. PMID: 29548823
  4. ARG1 gene polymorphisms and their association in individuals with essential hypertension in Pakistan has been presented. PMID: 29756997
  5. A subset of well-differentiated hepatocellular carcinomas are arginase-1 negative. PMID: 28970136
  6. The data in this study suggest that arginase I inhibition potentially represents a novel therapeutic target for the prevention and/or treatment of bronchopulmonary dysplasia-associated pulmonary hypertension. PMID: 27895230
  7. this study shows that infiltrating macrophages expressing Arg1 are present in active allergic contact dermatitis lesions PMID: 28747341
  8. High arginase expression is associated with glioblastoma. PMID: 27006175
  9. Report the value of Arg-1 in distinguishing HepPar-1-positive prostatic carcinoma from hepatocellular carcinoma at metastatic sites or cases of liver metastasis from prostate carcinoma. PMID: 27184483
  10. AEG-1 is positively activated in the tumorigenesis and deterioration of NSCLC. PMID: 28152520
  11. Arginase-1 expression is common (62.5%) in hepatoid adenocarcinoma and hence it is not useful in distinguishing hepatocellular carcinoma from hepatoid adenocarcinoma. PMID: 27137985
  12. Arginase 1 was highly expressed by tumor-associated Gr1+ microglia and macrophages. PMID: 27936099
  13. The authors report here that Candida albicans blocks nitric oxide production in human-monocyte-derived macrophages by induction of host arginase activity. PMID: 28119468
  14. Evidence for a negative association of arginase I with job strain and positive association with job control and social support in females. PMID: 28403218
  15. 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. PMID: 28089752
  16. 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. PMID: 26515089
  17. 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. PMID: 27009269
  18. 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 PMID: 26537638
  19. These results showed that alterations in the expression levels of Arg I and iNOS in the peripheral T cells and peripheral nodes of HIV infected patients are associated with disease progression in these patients. PMID: 26647762
  20. Increased ARG1 expression in macrophages after a single radiotherapy dose is an independent prognostic factor of skin toxicities. PMID: 26061397
  21. Arginase inhibition arrests human pulmonary artery smooth muscle cells in the G1/G0-phase under hypoxic conditions. PMID: 26126810
  22. Arginase from neutrophils can modulate nitric oxide production from activated macrophages which may affect the course of infection by intracellular bacteria. PMID: 26119192
  23. Overexpression and elevated activity of arginase I are involved in tobacco-induced pulmonary endothelial dysfunction. PMID: 25889611
  24. This method not only solved the problem of obtaining a large amount of arginase, but also provided a promising alternative for the future industrial production of L-Orn. PMID: 26227111
  25. the combination of high levels of CD14, FOXP3, and ARG1 mRNAs identified a small group of patients with excellent event-free and overall survival. PMID: 26161395
  26. Overexpression of Arg1 in the CNS of transgenic mice significantly reduced tau pathology. PMID: 26538654
  27. data indicate that helminth coinfection induces arginase-1-expressing type 2 granulomas, thereby increasing inflammation and TB disease severity. PMID: 26571397
  28. The data exclude a prognostic role of IL-10 and ARG-1 in metastatic neuroblastoma. PMID: 25961062
  29. Arginase activity increases in peripheral blood of patients with intestinal schistosomiasis. PMID: 25786588
  30. Data indicate that arginase-1 showed positivity in 2 ampullary region carcinomas and diffuse positivity in 1 duodenal adenocarcinoma. PMID: 26030248
  31. Arg1 induced accumulation of autophagosomes in MDA-MB-231 cells. PMID: 25501824
  32. Arg1 and PD-L1 are dynamically modulated upon neutrophil migration into human airways, and, Arg1, but not PD-L1, contributes to early neutrophil-driven T cell suppression in cystic fibrosis, likely hampering resolution of infection and inflammation. PMID: 25926674
  33. These results suggest that ARG1 and GABA influence both neural development and neuroblastoma and that benzodiazepines in clinical use may have potential applications for neuroblastoma therapy. PMID: 25437558
  34. Arg1 expression is decreased, and Arg2 expression is increased in the newborn congenital obstructive nephropathy and in the mouse model. PMID: 25205225
  35. rs2781666 may be associated with protection against pulmonary hypertension in preterm neonates with bronchopulmonary dysplasia PMID: 24919409
  36. The plasma levels of arginase I was higher in patients with DCL. PMID: 25124926
  37. Novel variants in the ARG1 locus associated with CRP levels in cardiovascular disease in a Korean population. [Meta-analysis] PMID: 24763700
  38. Arginase I levels are decreased in the plasma of pediatric patients with atopic dermatitis. PMID: 25027824
  39. Arginase activity was higher in cord blood of gestational diabetes mellitus mothers as opposed to the control group. PMID: 24376824
  40. Our results suggest that serum ARG and CRP together can efficiently diagnose Head and neck squamous cell carcinoma. PMID: 24715304
  41. Serum arginase I might regulate serum L-arginine and 3-nitrotyrosine via L-arginine. PMID: 24060156
  42. The independent associations of arginase I with urinary 8-OHdG and serum insulin may reflect its involvement in oxidative stress and diabetes mellitus. PMID: 24005081
  43. Arginase-1 mRNA expression correlates with myeloid-derived suppressor cell levels in peripheral blood of NSCLC patients. PMID: 23850196
  44. Both arginase-1 and HepPar-1 are effective markers of hepatocellular differentiation PMID: 24281232
  45. This study demonistrated that Five novel mutations in ARG1 gene in Chinese patients of argininemia. PMID: 23859858
  46. Glypican 3 and arginase-1 are the most reliable markers for identifying scirrhous hepatocellular carcinoma. PMID: 23348905
  47. Enzymes that are directly involved in the formation of urea are expressed in ocular tissues. PMID: 23740519
  48. Results show that the positively charged state of arginine is stable in the active site of arginase I, with that stabilization facilitated by the presence of hydroxide. PMID: 23327293
  49. The tumor suppressive function of arginase-I in both infiltrating and circulating myeloid-derived suppressor cells is a downstream target of activated STAT3. PMID: 23454751
  50. results suggest that Arg-1 may play a tumor suppressive role in HCC and could be a new, promising prognostic biomarker for HCC patients PMID: 23505904

FAQs

Please fill out the Online Inquiry form located on the product page. Key product information has been pre-populated. You may also email your questions and inquiry requests to sales1@betalifesci.com. We will do our best to get back to you within 4 business hours.

Feel free to use the Chat function to initiate a live chat. Our customer representative can provide you with a quote immediately.

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.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

Recently viewed