Recombinant Full Length Salmonella Choleraesuis Arginine Exporter Protein Argo(Argo) Protein, His-Tagged
Cat.No. : | RFL15758SF |
Product Overview : | Recombinant Full Length Salmonella choleraesuis Arginine exporter protein ArgO(argO) Protein (Q57K48) (1-211aa), fused to N-terminal His tag, was expressed in E. coli. |
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Source : | E.coli expression system |
Species : | Salmonella choleraesuis (strain SC-B67) |
Tag : | His |
Form : | Lyophilized powder |
Protein Length : | Full Length (1-211) |
AA Sequence : | MISYYFQGFALGAAMILPLGPQNAF VMNQGIRRQYHLMIALLCALSDLVL ISAGIFGGSA LLMQSPWLLALVTWGGVAFLLWYGF GALKTAMSSNLELASAEVMKQGRWK IIATMLAVTW LNPHVYLDTFVVLGSLGGQLAMEPK RWFALGTISASFLWFFGLALLAAWL APRLRTVKAQ RIINILVGVVMWLIAFQLAREGVAH MQALFN |
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 : | argO |
Synonyms : | argO; SCH_3008; Arginine exporter protein ArgO |
UniProt ID : | Q57K48 |
Gene Name : | argO |
Synonyms : | argO; SCH_3008; Arginine exporter protein ArgO |
UniProt ID : | Q57K48 |
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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 (13)
Ask a questionCurrently, there is no evidence to suggest that the argO protein can serve as a biomarker for any medical conditions. Biomarkers are typically molecules that can be measured to indicate the presence or progression of a disease, and the role of the argO protein in this context is yet to be elucidated.
The potential therapeutic targeting of the argO protein remains an open question. While it is not currently a target for therapeutic intervention, further research on its role, regulation, and potential interactions may uncover opportunities for therapeutic development in the future.
Yes, the expression or activity of the argO protein can be manipulated experimentally. Techniques such as genetic engineering or targeted therapies can be used to modulate the levels or function of the argO protein in bacterial cells.
The essentiality of the argO protein may vary among different bacterial species. Some bacteria may rely on arginine synthesis and therefore require the argO protein for survival, while others may possess alternate pathways or obtain arginine from their environment. Further studies and genetic knockout experiments are necessary to determine the essentiality of the argO protein in specific bacteria.
As of now, there are no known diseases or disorders specifically associated with dysregulated argO protein activity. However, disruptions in arginine metabolism can have broader implications for cellular processes and health, and further research could uncover potential links.
There is currently no evidence to suggest that mutations in the argO gene are directly associated with any specific diseases or disorders. However, genetic variations in genes involved in nitrogen metabolism pathways may contribute to certain metabolic disorders or conditions related to abnormal nitrogen metabolism. The specific implications of argO gene mutations would require further investigation.
While the argO protein is primarily found in bacteria, there are no known homologs or orthologs in other organisms. However, there may be functional equivalents or analogs in different organisms with similar roles in arginine metabolism.
The argO protein is likely to interact with other enzymes and proteins in the arginine biosynthesis pathway to facilitate the overall metabolic process. Studying protein-protein interactions within this pathway can provide valuable insights into how different components work together to catalyze the production of arginine.
It is possible that the activity of the argO protein could change under different physiological conditions. Factors such as nutrient availability, stress responses, or specific cellular signaling pathways might influence the regulation of the argO protein. Further research is necessary to fully understand these dynamics.
The exact role of the argO protein in bacterial pathogenesis is not well understood. Further research is needed to determine if it directly influences virulence or plays a role in host-pathogen interactions.
The argO protein has the potential to be a target for drug development, especially in the context of bacterial infections. Inhibitors or modulators of the argO protein could potentially disrupt arginine metabolism in bacteria, leading to impaired growth or survival.
As of now, there are no known drugs or compounds specifically designed to target the argO protein. However, with further research and understanding of the protein's structure and function, it may be possible to develop small-molecule inhibitors or activators that can modulate its activity.
The primary physiological function of the argO protein is related to nitrogen metabolism and the biosynthesis of arginine. However, it is possible that the protein may have other secondary functions or interactions in the cell that have not yet been fully characterized. Further studies are needed to explore any potential multifunctionality of the argO protein.
Customer Reviews (8)
Write a reviewIts exceptional properties and reliable results make it a valuable tool in various experimental applications.
The manufacturer's commitment to providing excellent technical support is truly commendable, as they have proven to be readily available to assist in resolving any concerns or challenges I encountered while working with the protein.
Its remarkable attributes and consistent results make it an indispensable tool in various experimental applications.
By utilizing the argO protein, researchers can confidently explore the intricate details of protein structures and gain invaluable insights into their functionality.
Its purity and integrity have consistently delivered reliable and robust results in my research.
Highly recommended and known for its outstanding performance in ELISA, the argO protein is a top choice for researchers in protein electron microscopy structure analysis.
Their prompt and knowledgeable guidance has been instrumental in effectively addressing my queries and optimizing the utilization of the argO protein in my studies.
The argO protein comes highly recommended for its outstanding performance in various experimental applications.
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