Treponema Mosaic

Treponema pallidum Mosaic Recombinant
Cat. No.
BT9265
Source
Escherichia Coli.
Synonyms
Appearance

Sterile Filtered solution.

Purity

Treponema Mosaic is >95% pure as determined by 10% PAGE (coomassie staining).

Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. They may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Treponema pallidum Mosaic contains TP15, TP17 & TP47 epitopes containing 382 a.a. produced in E.Coli and fused to a 6xHis tag at C-terminus. The total Mw is 38kDa and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Treponema pallidum, a gram-negative spirochaete bacterium with limited metabolic capabilities, is known to have at least four subspecies: T. pallidum pallidum, T. pallidum pertenue, T. pallidum carateum, and T. pallidum endemicum. Its helical structure enables corkscrew motion through viscous substances like mucus. The subspecies pallidum, with a small genome of 1.14 million base pairs, exhibits reduced metabolic abilities, indicating adaptation to the nutrient-rich environment of mammalian tissue.
Description
Recombinant Treponema pallidum Mosaic is a 38kDa protein comprising TP15, TP17, and TP47 epitopes. Produced in E. coli, it encompasses 382 amino acids and features a C-terminal 6xHis tag. Purification is achieved through proprietary chromatographic techniques.
Physical Appearance
Sterile Filtered solution.
Formulation
Treponema Mosaic protein solution is formulated in 1x PBS and 25mM K2CO3.
Stability
For optimal stability, Treponema Mosaic protein should be stored below -18°C. While it can remain stable at 4°C for a week, freeze-thaw cycles should be avoided.
Applications
Immunoassay.
Purity
Treponema Mosaic exhibits a purity greater than 95%, as determined by 10% PAGE (coomassie staining).
Source
Escherichia Coli.

Product Science Overview

Recombinant Proteins in Syphilis Diagnosis

Recombinant proteins are artificially produced proteins that are used in various diagnostic and therapeutic applications. In the context of Treponema pallidum, several recombinant proteins have been developed to improve the accuracy of syphilis diagnosis. These proteins include TmpA, TpN17, and TpN47, which have shown varying degrees of sensitivity and specificity in serological tests .

  • TmpA: This protein has shown high specificity but lower sensitivity in serological tests.
  • TpN17: Known for its high specificity and moderate sensitivity, making it a reliable marker in syphilis diagnosis.
  • TpN47: Exhibits the highest accuracy among the tested recombinant proteins, with high sensitivity and specificity .
Mosaic Recombinant Proteins

Mosaic recombinant proteins are engineered by combining sequences from different strains or variants of a pathogen. This approach aims to create a more comprehensive antigen that can elicit a stronger immune response or improve diagnostic accuracy. In the case of Treponema pallidum, mosaic recombinant proteins are designed to include epitopes from multiple strains, enhancing their ability to detect diverse variants of the bacterium .

Applications and Implications

The development of mosaic recombinant proteins for Treponema pallidum has significant implications for both diagnostics and vaccine development. By incorporating multiple epitopes, these proteins can improve the sensitivity and specificity of serological tests, leading to more accurate diagnoses. Additionally, they hold promise for the development of a universal syphilis vaccine that can provide broad protection against various strains of the bacterium .

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