Treponema TP0453
Escherichia Coli.
Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453
Sterile Filtered clear solution.
Protein is >95% pure as determined by SDS-PAGE (coomassie staining).
Description
Recombinant Treponema pallidum Outer Membrane Protein TP0453 has a Mw of 26kDa, and was purified from E. coli.
The Recombinant Treponema pallidum Outer Membrane Protein TP0453 is fused to 6 amino acid His tag at its C terminal and purified by proprietary chromatographic technique.
Product Specs
Tp0453, a protein responsible for transporting lipids and glycolipids within the outer membrane, is believed to be a novel bacterial outer membrane protein. This protein is thought to limit the permeability of T. pallidum's outer membrane to nutrients while remaining undetected by antibodies. Notably, Tp0453 demonstrated 100% specificity and sensitivity in tests with sera from syphilis patients, showing no reactivity with sera from patients with Lyme disease, relapsing fever, or leptospirosis.
Recombinant Treponema pallidum Outer Membrane Protein TP0453, with a molecular weight of 26kDa, is produced in E. coli and purified using a proprietary chromatographic method. The protein is fused with a 6 amino acid His tag at its C-terminus.
A clear, sterile-filtered solution.
Treponema TP0453 is supplied in a solution of 25mM K2CO3 and PBS.
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze at -20°C. The addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Repeated freezing and thawing should be avoided.
The purity of the protein is determined to be greater than 95% by SDS-PAGE analysis with Coomassie blue staining.
This product is suitable for use in rapid tests and immunoassays.
Outer membrane protein TP0453, 30kLP, TP_0453, TPANIC_0453
Escherichia Coli.
Product Science Overview
Treponema pallidum is the bacterium responsible for syphilis, a sexually transmitted infection. The outer membrane proteins (OMPs) of Treponema pallidum play a crucial role in the bacterium’s pathogenicity and immune evasion. These proteins are integral to the bacterium’s ability to infect and persist within the host. The recombinant forms of these proteins are used in research to understand their structure, function, and potential as vaccine candidates.
The outer membrane of Treponema pallidum is unique compared to other Gram-negative bacteria. It has a low protein content and lacks many of the common proteins found in other bacterial outer membranes . The OMPs of Treponema pallidum include several key proteins such as BamA, LptD, and members of the Tpr family . These proteins are involved in various functions, including nutrient uptake, immune evasion, and maintaining the integrity of the outer membrane.
Recombinant DNA technology has enabled the production of these OMPs in a laboratory setting. This allows researchers to study the proteins in detail without the need for live bacteria. Recombinant OMPs are produced by inserting the gene encoding the protein into a suitable expression system, such as Escherichia coli. The protein is then expressed, purified, and used in various assays to study its properties .
Research on recombinant OMPs of Treponema pallidum has provided valuable insights into the bacterium’s biology and pathogenesis. For example, structural modeling of these proteins has revealed their potential roles in the bacterium’s ability to infect and persist within the host . Additionally, recombinant OMPs are being investigated as potential vaccine candidates. By understanding how these proteins interact with the host immune system, researchers hope to develop vaccines that can prevent syphilis infection .
