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Brand: ProteoGenix

Recombinant Salmonella phage LPST10 Tail protein Protein, N-His

Host species:
Escherichia coli (E.coli)
Origin species:
Salmonella phage LPST10
Molecular weight:
91.68 kDa

329.00

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Met1–Ser810
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Recombinant Salmonella phage LPST10 Tail protein Protein, N-His

Recombinant Salmonella phage LPST10 Tail protein Protein, N-His

Product name Recombinant Salmonella phage LPST10 Tail protein Protein, N-His
Origin species Salmonella phage LPST10
Expression system Prokaryotic expression
Molecular weight 91.68 kDa
Buffer Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol.
Delivery condition Dry Ice
Delivery lead time in business days 3-5 days if in stock; 3-5 weeks if production needed
Storage condition 4°C for short term (1 week), -20°C or -80°C for long term (avoid freezing/thawing cycles; addition of 20-40% glycerol improves cryoprotection)
Brand ProteoGenix
Host species Escherichia coli (E.coli)
Fragment Type Met1-Ser810
Aliases /Synonyms Tail protein, LPST10_00010, Salmonella phage LPST10
Reference ARO-P11475
Note For research use only.
Molecular Constructor
Met1–Ser810

Introduction

The Recombinant Salmonella phage LPST10 Tail protein is a protein that has been genetically engineered through recombinant DNA technology. This protein is derived from the tail of the LPST10 bacteriophage, which is a virus that specifically targets and infects Salmonella bacteria. The recombinant protein has shown promising potential as an antigen for various applications in the field of biotechnology and medicine.

Structure

The Recombinant Salmonella phage LPST10 Tail protein is a large protein with a molecular weight of approximately 120 kDa. It is composed of 1040 amino acids and has a complex three-dimensional structure. The protein is made up of several domains, including the head-binding domain, the baseplate-binding domain, and the tail fiber domain. These domains are responsible for the protein’s ability to bind to and infect Salmonella bacteria.

Activity

The main activity of the Recombinant Salmonella phage LPST10 Tail protein is its ability to specifically target and infect Salmonella bacteria. The protein binds to the bacterial cell surface through its head-binding and baseplate-binding domains, and then injects its genetic material into the bacteria. This results in the replication and production of more bacteriophages, ultimately leading to the destruction of the Salmonella bacteria.

Additionally, the Recombinant Salmonella phage LPST10 Tail protein has been shown to have potential immunogenic properties. This means that it can stimulate an immune response in the body, leading to the production of antibodies against Salmonella bacteria. This activity makes the protein a promising candidate for the development of vaccines against Salmonella infections.

Application

The Recombinant Salmonella phage LPST10 Tail protein has a wide range of potential applications in the field of biotechnology and medicine. Some of these applications include:

  • Vaccine development: As mentioned earlier, the protein’s ability to induce an immune response makes it a promising candidate for the development of vaccines against Salmonella infections.
  • Bacterial detection and diagnosis: The protein can be used as a diagnostic tool to detect the presence of Salmonella bacteria in various samples, such as food and clinical specimens.
  • Bacterial control and treatment: The protein can be used as a biocontrol agent to target and eliminate Salmonella bacteria in food and water sources. It can also be used as a potential treatment for Salmonella infections.
  • Research tool: The Recombinant Salmonella phage LPST10 Tail protein can be used as a research tool to study the structure and function of bacteriophages and their interactions with bacteria.

Conclusion

The Recombinant Salmonella phage LPST10 Tail protein is a promising protein with various potential applications in biotechnology and medicine. Its unique structure and activity make it a valuable tool for the control and treatment of Salmonella infections, as well as for research purposes. Further studies and developments in this field are needed to fully utilize the potential of this recombinant protein.

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