Recombinant Full Length Mycobacterium Bovis Peptidoglycan-Binding Protein Arfa(Arfa) Protein, His-Tagged
Cat.No. : | RFL28229MF |
Product Overview : | Recombinant Full Length Mycobacterium bovis Peptidoglycan-binding protein ArfA(arfA) Protein (A1KH31) (1-326aa), fused to N-terminal His tag, was expressed in E. coli. |
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Source : | E.coli expression system |
Species : | Mycobacterium bovis (strain BCG / Pasteur 1173P2) |
Tag : | His |
Form : | Lyophilized powder |
Protein Length : | Full Length (1-326) |
AA Sequence : | MASKAGLGQTPATTDARRTQKFYRG SPGRPWLIGAVVIPLLIAAIGYGAF ERPQSVTGPT GVLPTLTPTSTRGASALSLSLLSIS RSGNTVTLIGDFPDEAAKAALMTAL NGLLAPGVNV IDQIHVDPVVRSLDFSSAEPVFTAS VPIPDFGLKVERDTVTLTGTAPSSE HKDAVKRAAT STWPDMKIVNNIEVTGQAPPGPPAS GPCADLQSAINAVTGGPIAFGNDGA SLIPADYEIL NRVADKLKACPDARVTINGYTDNTG SEGINIPLSAQRAKIVADYLVARGV AGDHIATVGL GSVNPIASNATPEGRAKNRRVEIVV N |
Purity : | Greater than 90% as determined by SDS-PAGE. |
Notes : | Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week. |
Storage : | Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles. |
Storage Buffer : | Tris/PBS-based buffer, 6% Trehalose, pH 8.0 |
Reconstitution : | We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference. |
Gene Name : | arfA |
Synonyms : | arfA; ompA; BCG_0951; Peptidoglycan-binding protein ArfA; Outer membrane protein A; OmpATb; Outer membrane protein ArfA |
UniProt ID : | A1KH31 |
Gene Name : | arfA |
Synonyms : | arfA; ompA; BCG_0951; Peptidoglycan-binding protein ArfA; Outer membrane protein A; OmpATb; Outer membrane protein ArfA |
UniProt ID : | A1KH31 |
Products Types
◆ Recombinant Protein | ||
arfA-5674M | Recombinant Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) arfA protein, His-tagged | +Inquiry |
For Research Use Only. Not intended for any clinical use. No products from Creative BioMart may be resold, modified for resale or used to manufacture commercial products without prior written approval from Creative BioMart.
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Q&As (34)
Ask a questionThe arfA protein is generally conserved across different bacterial species, although there may be variations in its sequence or expression levels.
There is evidence to suggest that arfA expression can be influenced by environmental conditions. Studies have shown that arfA expression can be upregulated under various stress conditions such as nutrient limitation, temperature shifts, or exposure to specific chemicals or antibiotics. These responses likely contribute to bacterial adaptation and survival in changing environments.
The regulation of arfA gene expression is not fully understood. However, studies suggest that certain stress conditions, such as nutrient starvation or antibiotic exposure, may influence arfA gene expression and the levels of arfA protein.
The arfA protein has been implicated in the regulation of ribosome stalling, which is a process that can occur during translation. It may help rescue stalled ribosomes and allow for the proper synthesis of proteins.
Some studies have suggested potential roles for the arfA protein in bacterial virulence and pathogenesis. For example, in certain bacteria, increased expression of arfA has been associated with enhanced virulence in various infection models. However, further research is needed to fully understand the link between the arfA protein and bacterial pathogenesis.
Research efforts are underway to investigate the potential of targeting the arfA protein for therapeutic purposes. As it plays a role in rescuing stalled ribosomes, which can contribute to bacterial antibiotic resistance, inhibiting the arfA protein's activity could potentially enhance the efficacy of antibiotics. However, more research is needed to fully understand the mechanisms and potential therapeutic applications of targeting the arfA protein.
To the best of my knowledge, there are currently no known small molecules that can specifically modulate the activity of the arfA protein. However, screening efforts using chemical libraries or targeted drug discovery approaches may identify potential small molecule modulators in the future.
To the best of my knowledge, no significant functional variations of the arfA protein have been reported. However, as research on arfA continues, it is possible that variations in its sequence or structure may be discovered, which could have implications for its function and properties.
The arfA protein is not universal among all bacterial species but has been identified in various gram-negative bacteria, including E. coli and Salmonella. The presence of arfA homologs or functional analogs in other bacterial species is still being investigated.
Some studies suggest that arfA protein expression is increased in response to antibiotic exposure, indicating a potential role in antibiotic response. However, the exact contribution of arfA protein to antibiotic resistance or sensitivity is not well understood.
As of now, there are no known genetic variations in the arfA gene specifically associated with drug resistance. However, the genetic variability within bacterial populations, including potential arfA gene variations, can contribute to overall drug resistance phenotypes. Further studies are needed to explore the genetic diversity of arfA and its potential links to drug resistance.
Some open research questions about the arfA protein include its exact molecular mechanism, its specific role in ribosome stalling rescue, its implications in bacterial physiology and pathogenesis, and its potential as a target for therapeutics. Understanding these aspects will contribute to our knowledge of the arfA protein and its broader biological significance.
Certain environmental cues, such as stress conditions or changes in nutrient availability, may influence the expression of the arfA protein. However, the specific mechanisms or signaling pathways involved in regulating arfA expression in response to environmental cues have not been fully elucidated.
At present, there is no evidence to suggest that the arfA protein can be used as a specific biomarker for bacterial infections or conditions. However, as research on arfA progresses, new insights regarding its potential as a biomarker may emerge.
Yes, the arfA gene has been studied in various bacterial strains and clinical isolates. Research has been conducted to investigate its presence, expression levels, and potential role in different bacterial species. These studies provide insight into the conservation and functional significance of arfA across different strains and isolates.
Yes, the arfA protein has been found to interact with other proteins involved in translation, such as ribosomal proteins and elongation factors. These interactions may play a role in its function.
The implications of arfA protein dysregulation in bacteria are not yet fully understood. It is possible that dysregulation could affect protein synthesis, gene expression, and bacterial physiology, but further research is needed to clarify its specific role.
Currently, there is limited information on arfA protein dysfunction and its association with specific diseases or conditions. Further research is needed to determine its potential involvement in disease processes.
The primary known role of the arfA protein is in rescuing stalled ribosomes during translation. However, it is possible that the arfA protein may have additional roles in bacterial physiology or adaptation to specific conditions, which require further investigation.
The arfA protein is primarily found in bacteria and does not have direct homologs or orthologs in eukaryotes. However, there may be functional analogs or proteins with similar roles in other organisms.
To the best of my knowledge, there are no known diseases or conditions directly associated with mutations or dysregulation of the arfA gene. However, further studies may reveal potential links between arfA gene alterations and specific phenotypes.
The structure of the arfA protein has not been determined to date. Structural information is crucial for understanding the molecular mechanisms and interactions of proteins, so efforts are being made to determine the three-dimensional structure of arfA using techniques like X-ray crystallography or cryo-electron microscopy.
It is unclear whether the arfA protein can be directly targeted for the development of antibacterial drugs with a broad spectrum of activity. However, understanding the role of arfA in bacterial translation and stress response could potentially lead to the identification of novel targets or pathways for developing broad-spectrum antibacterial agents.
The arfA protein primarily influences the cellular process of protein synthesis by rescuing stalled ribosomes. This rescue mechanism helps to maintain efficient translation and prevent translation arrest. Additionally, the arfA protein may have broader effects on bacterial physiology and adaptation to stress conditions, although these are still being investigated.
The arfA protein is synthesized through the cellular process of translation. The gene that encodes the arfA protein is transcribed into mRNA, which is then translated by ribosomes in the cytoplasm to produce the arfA protein.
The arfA protein has been found to interact with certain ribosomal proteins, elongation factors, and other translation-related proteins. These interactions suggest that the arfA protein may play a role in modulating protein synthesis.
The arfA protein is a small protein, typically consisting of around 60-80 amino acids. It does not contain well-defined structural domains, but it may adopt a specific conformation upon interaction with other proteins or molecules.
As the function of the arfA protein is not well understood, and its role in disease processes is unclear, there are currently no specific therapeutic interventions targeting this protein.
The exact mechanism of how the arfA protein rescues stalled ribosomes is still under investigation. It is proposed that the arfA protein binds to the stalled ribosome, interacting with other components of the translation machinery to promote ribosome recycling and translation restart.
As the arfA protein is not well characterized, there are currently no known drugs or compounds that specifically interact with it.
The specific interactions between the arfA protein and other cellular components are not well-defined. However, arfA is thought to interact with ribosomes or associated factors to mediate its role in ribosome rescue. Additionally, research is ongoing to explore potential interactions with other proteins or cellular factors involved in bacterial translation and stress response.
It is currently unclear whether the arfA protein itself can be directly targeted for developing new antibiotics. However, understanding the mechanisms and regulatory pathways involving the arfA protein's function in ribosome rescue may provide insights for identifying novel targets for antibiotic development.
Yes, there is evidence to suggest that arfA plays a role in antibiotic resistance. When bacteria are exposed to certain antibiotics, translation can be stalled, leading to the activation of arfA to rescue the stalled ribosomes and maintain protein synthesis. This rescue mechanism can potentially contribute to bacterial survival and antibiotic resistance.
Currently, there are no known specific inhibitors or activators of the arfA protein. Identifying molecules that can modulate the activity or expression of the arfA protein could potentially be of interest for future therapeutic developments.
Customer Reviews (8)
Write a reviewThe arfA Protein not only delivers exceptional results in my experiments but also provides peace of mind due to its reliability.
the arfA Protein comes highly recommended for its exceptional performance in WB experiments and its utility in protein electron microscopy structure analysis.
Its high specificity and functional integrity ensure accurate and reproducible data, allowing researchers to draw meaningful conclusions from their experiments.
the arfA protein has been extensively studied and validated in various experimental applications.
Their team of technical experts possess deep knowledge and expertise regarding the protein, ensuring that researchers receive accurate and timely assistance.
the arfA Protein's quality and versatility make it an invaluable resource in my laboratory.
Its unparalleled quality ensures accurate and reproducible data, giving me confidence in the conclusions drawn from my analyses.
In addition to its advantages in trials, the manufacturer of the arfA protein offers exceptional support to researchers.
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