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| Size | 100ug |
|---|---|
| Brand | ProteoGenix |
| Product type | Recombinant Proteins |
| Product name | Recombinant Neisseria gonorrhoeae cppB, N-GST |
|---|---|
| Origin species | Neisseria gonorrhoeae |
| Expression system | Prokaryotic expression |
| Molecular weight | 50.75 kDa |
| Buffer | Lyophilized from a solution in PBS pH 7.4, 0.02% NLS, 1mM EDTA, 4% Trehalose, 1% Mannitol. |
| Form | Liquid |
| 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-Arg213 |
| Aliases /Synonyms | Cryptic plasmid protein B, cppB |
| Reference | ARO-P12838 |
| Note | For research use only. |
Recombinant Neisseria gonorrhoeae cppB is a protein that has been genetically engineered and produced in a laboratory setting. It is a highly versatile protein with a wide range of applications in the field of biotechnology and medicine. In this article, we will explore the structure, activity, and various applications of this recombinant protein.
The cppB gene, which encodes for the Recombinant Neisseria gonorrhoeae cppB protein, is found in the genome of the bacterium Neisseria gonorrhoeae. The protein is composed of 226 amino acids and has a molecular weight of approximately 26kDa. It has a highly conserved structure, with 98% sequence identity among different strains of Neisseria gonorrhoeae.
The crystal structure of Recombinant Neisseria gonorrhoeae cppB has been determined through X-ray crystallography, revealing a compact globular protein with three distinct domains. The first domain is a beta-barrel structure, which is involved in binding to the bacterial cell surface. The second domain is a helical bundle, which is responsible for the protein’s stability. The third domain is a flexible loop that is important for the protein’s function.
The primary function of Recombinant Neisseria gonorrhoeae cppB is to act as an antigen, stimulating an immune response in the host. The protein is highly immunogenic and has been shown to induce a strong antibody response in animal studies. It is also involved in the attachment and invasion of Neisseria gonorrhoeae into host cells, making it a potential target for vaccine development.
Furthermore, Recombinant Neisseria gonorrhoeae cppB has been found to have antimicrobial activity. It can bind to and neutralize the activity of certain antimicrobial peptides, making it a potential therapeutic target for the treatment of infections caused by Neisseria gonorrhoeae.
One of the most promising applications of Recombinant Neisseria gonorrhoeae cppB is in the development of a vaccine against Neisseria gonorrhoeae. As mentioned earlier, the protein is highly immunogenic and has been shown to induce a strong antibody response. This makes it a potential candidate for inclusion in a vaccine formulation to protect against gonorrhea.
Several studies have been conducted to evaluate the efficacy of Recombinant Neisseria gonorrhoeae cppB as a vaccine antigen. In a mouse model, immunization with the protein was found to confer protection against a challenge with Neisseria gonorrhoeae. This promising result warrants further research into the development of a vaccine containing Recombinant Neisseria gonorrhoeae cppB.
Recombinant Neisseria gonorrhoeae cppB has also been used as a diagnostic tool for the detection of Neisseria gonorrhoeae infections. Antibodies against the protein have been used in various immunoassays, such as ELISA and Western blot, to detect the presence of the bacterium in clinical samples. This has proven to be a sensitive and specific method for the diagnosis of gonorrhea, especially in cases where traditional culture methods have failed.
The antimicrobial activity of Recombinant Neisseria gonorrhoeae cppB has also sparked interest in its potential use as a therapeutic agent. It has been shown to inhibit the growth of Neisseria gonorrhoeae in vitro and in animal models. This suggests that the protein could be developed into a novel treatment for gonorrhea, particularly in cases where antibiotic
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