argi
Species | Cat.# | Product name | Source (Host) | Tag | Protein Length | Price |
---|---|---|---|---|---|---|
Bacillus subtilis | ARGI-0530B | Recombinant Bacillus subtilis ARGI protein, His-tagged | E. coli or Yeast | His |
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Q&As (20)
Ask a questionYes, dietary modifications can influence ARGI protein activity or expression to some extent. Arginine, the substrate for ARGI, is obtained from the diet, and changes in dietary arginine intake can affect the production and availability of arginine for ARGI-mediated processes. Additionally, certain compounds present in the diet, such as flavonoids, have been shown to modulate ARGI expression and activity in animal and cell culture studies. However, more research is needed to fully understand the dietary regulation of ARGI protein.
Yes, hormonal signals can influence ARGI expression or activity. For example, growth hormone has been shown to increase ARGI gene expression in the liver, leading to increased urea production. Insulin, on the other hand, can decrease ARGI activity by promoting its phosphorylation and inactivation. Hormones such as glucagon and cortisol have also been reported to affect ARGI expression and activity, indicating the role of hormonal regulation in modulating ARGI function.
ARGI itself is not commonly used as a biomarker for specific conditions or diseases. However, its downstream product, nitric oxide (NO), is often measured as a biomarker for various physiological and pathological processes. In certain disease contexts, measuring ARGI gene expression or activity levels in specific tissues or cells may provide insights into the underlying dysregulation of arginine metabolism, but more research is needed to establish its clinical utility as a biomarker.
Deficiency in ARGI activity or expression can lead to a condition called arginase deficiency or argininemia. This can result in the accumulation of arginine, hyperammonemia, and decreased urea production, leading to symptoms such as developmental delays, intellectual disability, growth retardation, and liver dysfunction. However, the severity and specific symptoms can vary among individuals.
The expression of the ARGI gene has been found to be altered in certain types of cancers. In some cases, increased ARGI expression has been associated with tumor progression and poor prognosis, while in others, decreased expression has been observed. The exact role of ARGI in cancer development and progression is complex and can vary depending on the specific tumor type. Further research is necessary to better understand the implications of ARGI expression in cancer.
Yes, dysregulation of ARGI has been implicated in various diseases and conditions. One such condition is hyperargininemia, which is characterized by a deficiency of ARGI activity, leading to the accumulation of arginine in the blood. This can result in neurological symptoms and developmental delays. In some cases, dysregulation of ARGI has also been associated with cardiovascular diseases, respiratory diseases, and cancer, although further research is needed to fully understand these connections.
Targeting ARGI in cancer has therapeutic implications, particularly in cancers that exhibit arginine auxotrophy. Some cancer cells, particularly certain types of tumors with deficiencies in arginine biosynthesis, rely on extracellular arginine for growth. Targeting ARGI can lead to arginine depletion in the tumor microenvironment, causing growth arrest or apoptosis of these cancer cells. Strategies like arginine deprivation therapy or pegylated arginine deiminase (ADI-PEG20) have been developed to target tumors with arginine auxotrophy.
Yes, arginine, the amino acid that serves as the substrate for ARGI, is naturally present in various foods. High-protein foods, such as meats (beef, chicken, pork), fish, dairy products (milk, cheese, yogurt), and legumes (beans, lentils), are good dietary sources of arginine. Other sources include nuts, seeds, soy products, and whole grains. The exact amount of arginine in these foods can vary, and cooking and processing methods can also affect arginine content. However, most people can meet their arginine requirements through a balanced diet without the need for supplementation.
While the primary function of ARGI is in the urea cycle, emerging research suggests that it may have additional roles in various physiological and pathological processes. Studies have implicated ARGI in immune responses, wound healing, tissue regeneration, and modulation of nitric oxide signaling, indicating its involvement beyond ammonia detoxification. However, more research is needed to fully understand these secondary functions.
Yes, there have been reported genetic mutations or polymorphisms in the ARGI gene associated with diseases or conditions. For example, certain mutations can lead to arginase deficiency, as mentioned earlier. Moreover, variations in the ARGI gene have also been linked to cardiovascular diseases, such as coronary artery disease and hypertension, as well as metabolic disorders like diabetes and obesity. Additional studies are necessary to further explore the impact of ARGI gene variants on disease development.
The downstream effects of ARGI activity mainly involve the production of nitric oxide (NO) and urea. ARGI catalyzes the conversion of arginine to ornithine and urea. Ornithine can further be metabolized into other compounds. The production of NO by ARGI is important for various physiological processes, including vasodilation, neurotransmission, and immune responses. Urea is a waste product that is excreted by the kidneys, helping to regulate nitrogen balance in the body.
Yes, targeting the ARGI protein can be a potential therapeutic approach for the treatment of hyperargininemia. Hyperargininemia is a rare genetic disorder characterized by high levels of arginine in the blood due to ARGI deficiency. Enzyme replacement therapy and gene therapy strategies aimed at correcting or replacing the dysfunctional ARGI gene are being investigated as potential treatment options for this condition.
ARGI supplementation has been explored for its potential benefits in various health conditions. Due to its role in nitric oxide production, ARGI supplementation has been studied for its potential cardiovascular benefits, including improving blood flow, lowering blood pressure, and supporting heart health. It may also have potential benefits for certain respiratory conditions, such as asthma and chronic obstructive pulmonary disease (COPD), as nitric oxide has been shown to have bronchodilatory effects. Additionally, ARGI supplementation has been investigated for its role in supporting immune function and wound healing. However, further research is needed to fully understand the effects and potential benefits of ARGI supplementation in different health conditions.
While the ARGI gene is predominantly expressed in the liver, it can also be found in other tissues, although at lower levels. For instance, the kidney, intestinal mucosa, and immune cells have been shown to express ARGI. However, the precise expression pattern might vary based on developmental stages, physiological conditions, and pathological states.
Yes, the expression of the ARGI gene can be regulated by various factors. One of the main regulators is the transcription factor called hepatocyte nuclear factor 1-alpha (HNF1α). HNF1α binds to specific regions of the ARGI gene promoter and enhances its transcription. Other transcription factors, such as C/EBPβ and FoxO1, have also been implicated in regulating ARGI gene expression.
ARGI supplementation can interact with certain medications and may have some side effects. ARGI can lower blood pressure, so caution is advised when taking ARGI supplements along with medications for hypertension or other medication that lower blood pressure. ARGI can also interact with nitrates used to treat angina, and combining the two can cause a dangerous drop in blood pressure. Common side effects of ARGI supplementation include gastrointestinal symptoms such as bloating, diarrhea, or abdominal discomfort, although these side effects are generally mild and self-limiting. As with any supplement, it is important to consult with a healthcare professional before starting ARGI supplementation to ensure safety and determine any potential interactions with medications.
ARGI has been studied for its potential role in muscle growth and athletic performance. As a precursor to nitric oxide, arginine supplementation has been proposed to enhance blood flow and nutrient delivery to muscles, potentially aiding in muscle growth and exercise performance. Some studies have reported positive effects on exercise performance, recovery, and muscle protein synthesis with arginine supplementation, while others have shown no significant benefits. The effects may depend on various factors, including the type and intensity of exercise, individual differences, and dose and timing of supplementation. Further research is needed to determine the optimal use of ARGI in relation to muscle growth and athletic performance.
Targeting the ARGI protein for therapeutic purposes has been explored in certain conditions, particularly cancer. Some studies have shown that inhibiting ARGI activity can reduce tumor growth and enhance the effectiveness of certain chemotherapeutic drugs. However, more research is needed to fully evaluate the safety and efficacy of targeting ARGI in therapeutic interventions for various diseases.
Yes, various genetic variations and mutations have been identified in the ARGI gene. Some of these mutations can cause hyperargininemia, a rare genetic disorder characterized by ARGI deficiency. These mutations can result in the production of non-functional or truncated ARGI proteins, leading to the accumulation of arginine in the blood. Other genetic variations in the ARGI gene may influence enzyme activity and contribute to individual differences in arginine metabolism, although their specific effects are still being studied.
Yes, several compounds have been identified as inhibitors or activators of ARGI protein activity. For example, NO is known to inhibit ARGI activity by binding to the enzyme's active site. Various chemical inhibitors, such as N-(omega)-hydroxy-nor-L-arginine (nor-NOHA), can also block ARGI activity. On the other hand, certain molecules, like manganese and zinc ions, have been shown to stimulate ARGI activity.
Customer Reviews (8)
Write a reviewthe ARGI protein offers numerous advantages in trials and research experiments.
I am extremely satisfied with the high performance and the exceptional support associated with this protein, as it has greatly contributed to the success of my scientific endeavors.
Their expertise and prompt assistance have been instrumental in overcoming challenges and optimizing the use of the ARGI protein in my studies.
Highly recommended for its exceptional performance in ELISA, the ARGI protein is a top contender for researchers involved in protein electron microscopy structure analysis.
Coupled with the manufacturer's exceptional technical support and commitment to customer satisfaction, researchers can confidently utilize the ARGI protein in their studies, knowing that they have the necessary resources and assistance to succeed.
Not only does it provide reliable and consistent results due to its high quality and purity, but it also holds significant value in understanding cellular processes and disease mechanisms.
The ARGI protein is of exceptional quality, making it an ideal candidate to fulfill my experimental requirements.
the manufacturer's commitment to delivering excellent technical support has proven to be invaluable in troubleshooting any issues that arose during my experiments.
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