Recombinant Staphylococcus epidermidis ATCC 12228 ARGS protein, His-tagged

• Cat.No.: ARGS-3102S
• Product Overview: Recombinant Staphylococcus epidermidis ATCC 12228 ARGS full length or partial length protein was expressed.

Specification

• Source: E. coli or Yeast
• Species: Staphylococcus
• Tag: His
• Form: Liquid or lyophilized powder
• Endotoxin: < 1.0 EU per μg of the protein as determined by the LAL method.
• Purity: > 80% by SDS-PAGE
• Notes: This item requires custom production and lead time is between 5-9 weeks. We can custom produce according to your specifications.
• Storage: Store it at +4 ºC for short term. For long term storage, store it at -20 ºC~-80 ºC.
• Storage buffer: PBS buffer

Gene Information

• Gene Name: argS arginyl-tRNA synthetase [ Staphylococcus epidermidis ATCC 12228 ]
• Official Symbol: ARGS
• Synonyms: ARGS; arginyl-tRNA synthetase
• Gene ID: 1056748
• UniProt ID: Q8CTN9

Reviews

02/13/2023

Its versatility and reliability make it a great asset in the pursuit of scientific discoveries.

06/14/2022

Its consistent performance and remarkable stability make it a reliable tool in studying various cellular processes and signaling pathways.

05/04/2022

In ELISA assays, it has consistently exhibited exceptional reliability and accuracy, providing precise and reproducible results.

03/18/2022

I have successfully implemented the ARGS protein in protein electron microscopy structure analysis, where its attributes have greatly aided in elucidating complex molecular structures.

12/11/2020

With the ARGS protein, researchers can confidently delve into the complexity of protein structures and gain deeper insights into their functions.

11/18/2020

the ARGS protein's exceptional quality and purity guarantee its suitability for a wide range of experimental applications.

04/24/2017

Considering its remarkable performance across multiple assays, I wholeheartedly endorse the usage of the ARGS protein in various research studies.

05/01/2016

when utilized in Western Blotting experiments, the ARGS protein has consistently produced distinct and well-defined protein bands, facilitating clear and accurate interpretation of results.

Q&As

Are there any known regulatory factors that modulate the activity of the ARGS protein?

Various regulatory factors can modulate the activity of the ARGS protein. For example, certain transcription factors or co-factors may interact with the ARGS protein and enhance or inhibit its DNA-binding ability. Additionally, post-translational modifications, such as phosphorylation, can influence the protein's activity.

Are there any known diseases or disorders associated with dysfunction of the ARGS protein?

Currently, there are no known diseases or disorders directly linked to dysfunction of the ARGS protein. However, further research is necessary to fully understand its potential roles and implications in various biological processes.

Are there any known inhibitors or activators of the ARGS protein?

Currently, there are no known specific inhibitors or activators of the ARGS protein. Understanding its regulation and potential interactions with other proteins or factors may eventually lead to the development of targeted inhibitors or activators in the future.

Is the ARGS protein conserved across different species?

Yes, the ARGS protein is evolutionarily conserved, meaning that it is found in various species and shows a degree of similarity in its amino acid sequence and function across different organisms. This conservation implies that the ARGS protein plays important roles in biological processes that have been preserved throughout evolution.

Is the ARGS gene expressed in all tissues or is its expression restricted to specific cell types?

The expression of the ARGS gene is not well-studied in terms of tissue specificity. However, based on available data, it appears that the ARGS gene is expressed in a wide range of tissues and cell types, suggesting that it may have broad physiological functions.

Are there any ongoing clinical trials or research studies related to the ARGS protein?

At this time, there is limited information available regarding clinical trials or research studies specifically focused on the ARGS protein. However, the field of arginine metabolism and its associated proteins continues to be an active area of research, and new studies may emerge in the future.

Are there any diseases associated with abnormalities in arginine metabolism?

Yes, abnormalities in arginine metabolism have been linked to several diseases. For example, deficiencies in enzymes involved in the urea cycle can lead to urea cycle disorders characterized by the accumulation of ammonia in the body. Additionally, dysregulation of arginine metabolism and nitric oxide synthesis have been implicated in cardiovascular diseases, neurodegenerative disorders, and certain types of cancer.

Can the ARGS protein be used in biotechnological applications?

While the exact utility of the ARGS protein in biotechnological applications is not well-established, its involvement in arginine metabolism and regulation of gene expression suggests potential applications in industries such as agriculture (modification of arginine metabolism in crops) or biopharmaceutical production (modulating arginine-related pathways in cell culture systems). However, further research is necessary to explore these possibilities.

Can the ARGS protein be targeted for therapeutic purposes?

While there is no direct therapeutic targeting of the ARGS protein at present, understanding its function and regulation could have implications in developing treatments for arginine-related disorders, such as arginine metabolism disorders or certain types of cancer where arginine metabolism plays a role.

Are there any drug targets or therapeutic implications associated with the ARGS protein?

Currently, there are no known drug targets or therapeutic implications specifically associated with the ARGS protein. However, considering its involvement in arginine metabolism and potential roles in diseases, understanding its regulation and interactions may lead to the identification of therapeutic targets or strategies in the future.

Is the ARGS protein conserved across different bacterial species?

The ARGS protein is not universally conserved across all bacterial species. It is found in certain bacteria, particularly those that have an arginine biosynthesis pathway and require a mechanism to monitor and regulate arginine levels. The presence and characteristics of the ARGS protein can vary among different bacterial species.

How does the ARGS protein function in arginine sensing?

The ARGS protein has a binding site specifically designed to interact with arginine molecules. When arginine levels are low, the ARGS protein undergoes a conformational change that allows it to bind to DNA and activate the expression of genes involved in arginine biosynthesis. This helps the cell increase arginine levels in response to a deficiency.

Can the ARGS protein be used as a biomarker for arginine-related conditions?

As of now, there is no evidence to support the use of the ARGS protein as a specific biomarker for arginine-related conditions. However, future studies may reveal its potential utility as a biomarker in certain contexts.

Are there any known variations or isoforms of the ARGS protein?

Yes, variations or isoforms of the ARGS protein have been identified. Different bacterial species may have slightly different versions of the protein, with variations in the amino acid sequence or structural domains. These variations can influence the protein's affinity for arginine or its ability to activate gene expression.

Can the ARGS protein detect arginine levels in other organisms or environments outside of bacterial cells?

The ARGS protein is highly specific to bacterial cells and is primarily involved in sensing arginine levels within those cells. It is not known to have the ability to detect arginine levels in other organisms or external environments.

Does the ARGS protein interact with other proteins or molecules?

Yes, the ARGS protein can interact with other proteins or molecules to carry out its functions. For example, it has been reported to interact with other transcription factors to regulate gene expression. Additionally, it may have protein-protein interactions involved in arginine metabolism, though the specific interactions are not well-characterized.

Are there any known interactions between the ARGS protein and other proteins?

Yes, the ARGS protein is known to interact with other proteins within the cellular environment. These interactions can influence its activity and regulate its function. For instance, certain transcription factors, co-factors, or chaperones may interact with the ARGS protein, modulating its ability to bind DNA or regulate gene expression.

Has the ARGS protein been implicated in any specific biological processes or pathways?

The ARGS protein is primarily implicated in regulating arginine metabolism and biosynthesis-related pathways. It is known to activate the expression of genes involved in arginine biosynthesis when arginine levels are low. However, further investigations are required to understand its potential involvement in other biological processes or signaling pathways.

Are there any genetic variations or mutations in the ARGS gene associated with disease?

Currently, there is limited information available about genetic variations or mutations in the ARGS gene associated with disease. Further research is needed to explore potential associations between genetic variations in the ARGS gene and disease susceptibility or phenotypic traits.