Borrelia Spielmanii DbpA

Borrelia Spielmanii Decorin Binding Protein A Recombinant
Cat. No.
BT30108
Source
Escherichia Coli.
Synonyms
Appearance
Sterile Filtered clear solution.
Purity
Greater than 80.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

Recombinant Borrelia Spielmanii Decorin Binding Protein A produced in E.coli is a non-glycosylated, polypeptide chain having a calculated molecular mass of 17kDa.

Borrelia Spielmanii DbpA is expressed with a -10x His tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction

Borrelia, a bacterial genus within the spirochete phylum, is responsible for causing borreliosis. This zoonotic vector-borne disease is primarily transmitted by ticks, with some species also transmitted by lice. Among the 36 identified Borrelia species, 12 are known to cause Lyme disease or borreliosis and are spread through tick bites. Borreliella spielmanii, a Gram-negative bacterium, is one of the pathogens belonging to the Borreliella burgdorferi sensu lato complex, which causes Lyme disease. DbpA, also referred to as p17 or Osp17, exhibits heterogeneity among the human pathogenic B. burgdorferi sensu lato species.

Description

Recombinant Borrelia Spielmanii Decorin Binding Protein A, produced in E.coli, is a non-glycosylated polypeptide chain with a calculated molecular mass of 17kDa.

A -10x His tag is added to the N-terminus of Borrelia Spielmanii DbpA during expression, and purification is achieved using proprietary chromatographic techniques.

Physical Appearance
A clear, sterile-filtered solution.
Formulation

Borrelia Spielmanii DbpA is supplied in a buffer solution containing 20mM HEPES (pH 7.6), 250mM NaCl, and 20% glycerol.

Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For extended storage, it should be frozen at -20°C. Repeated freezing and thawing should be avoided.
Purity
Purity exceeding 80.0% as assessed by SDS-PAGE.
Applications
Suitable for Western blot analysis using Lyme-positive plasma.
Immunological Functions

1. Exhibits binding affinity for human IgG and IgM antibodies.
2. Applicable for use in immunodot testing with plasma samples from individuals with positive or negative Lyme disease status.

Source
Escherichia Coli.

Product Science Overview

Introduction

Borrelia spielmanii is a species of spirochete bacteria belonging to the Borrelia burgdorferi sensu lato complex, which is known to cause Lyme borreliosis. This species was identified relatively recently and is one of the several Borrelia species that can infect humans. Decorin binding protein A (DbpA) is a surface adhesin found in Borrelia species, including Borrelia spielmanii. DbpA plays a crucial role in the pathogenesis of Lyme disease by facilitating the attachment of the bacteria to host tissues. The recombinant form of this protein, Borrelia spielmanii Decorin Binding Protein A Recombinant, is produced using genetic engineering techniques to study its structure, function, and potential as a target for vaccines and diagnostics.

Preparation Methods

The recombinant Borrelia spielmanii Decorin Binding Protein A is typically produced in a bacterial expression system, such as Escherichia coli (E. coli). The gene encoding DbpA is cloned into an expression vector, which is then introduced into E. coli cells. These cells are cultured under conditions that induce the expression of the recombinant protein. The protein is often tagged with a histidine (His) tag to facilitate purification. After expression, the cells are lysed, and the recombinant protein is purified using affinity chromatography techniques, such as nickel-nitrilotriacetic acid (Ni-NTA) chromatography, which binds to the His tag. The purified protein is then analyzed for purity and functionality .

Chemical Reactions Analysis

Decorin binding protein A (DbpA) interacts with decorin, a collagen-associated proteoglycan found in the extracellular matrix of host tissues. This interaction is critical for the adhesion of Borrelia spielmanii to host cells, which is a key step in the establishment of infection. The binding of DbpA to decorin can be studied using various biochemical and biophysical techniques, such as surface plasmon resonance (SPR) and enzyme-linked immunosorbent assays (ELISA). These methods allow researchers to quantify the binding affinity and kinetics of the interaction between DbpA and decorin.

Additionally, the immunogenicity of DbpA can be analyzed by examining the antibody response in infected individuals or animals. Studies have shown that DbpA is highly immunogenic and elicits a strong antibody response, making it a potential candidate for vaccine development . The recombinant form of DbpA can be used to generate specific antibodies, which can then be employed in diagnostic assays to detect Borrelia spielmanii infections.

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