Bet v 1.0101, Sf9

Major pollen allergen Bet v 1-A Recombinant, Sf9
Cat. No.
BT16236
Source
Sf9 insect cells.
Synonyms
Major pollen allergen Bet v 1-A, Allergen Bet v I-A, Bet v 1-A, BETVIA, BETVI.
Appearance
Sterile Filtered clear solution.
Purity

Greater than 95.0% 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 Major pollen allergen Bet v 1-A produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 18,942 Dalton.
Bet v 1.0101 is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Bet v 1.0101, a primary allergen found in birch pollen, is a major trigger for allergic reactions in humans. This allergen is widespread in Europe, North America, and the former Soviet Union states, causing symptoms predominantly in early spring.
Description
Recombinant Major pollen allergen Bet v 1-A, produced in Sf9 insect cells, is a glycosylated polypeptide chain with a molecular weight of 18,942 Daltons. It features a 10xHis tag at the N-terminus for purification purposes and is purified using proprietary chromatographic methods.
Physical Appearance
The product is a clear solution that has undergone sterile filtration.
Formulation

The Bet v 1.0101 protein is provided in a solution containing 20mM HEPES buffer at pH 8.0, 200mM NaCl, and 20% glycerol.

Stability
For short-term storage (2-4 weeks), the product can be kept at 4°C. For longer storage, it is recommended to freeze the product at -20°C. Repeated freezing and thawing should be avoided.
Purity

The purity of the product exceeds 95.0%, as determined by SDS-PAGE analysis.

Immunological Functions
1. This protein exhibits binding affinity to human IgE antibodies.
2. It demonstrates reactivity in immunodot assays utilizing panels of positive and negative sera.
Synonyms
Major pollen allergen Bet v 1-A, Allergen Bet v I-A, Bet v 1-A, BETVIA, BETVI.
Source
Sf9 insect cells.

Product Science Overview

Introduction

The Major Pollen Allergen Bet v 1-A is a significant allergen derived from birch pollen (Betula verrucosa). It is known to cause type I allergic reactions, particularly in Europe, North America, and the former Soviet Union states, typically observed in early spring . The recombinant form of this allergen, produced in Sf9 insect cells, is utilized for various research and diagnostic purposes.

Expression System

The recombinant Major Pollen Allergen Bet v 1-A is produced using the Sf9 insect cell expression system. Sf9 cells, derived from the fall armyworm (Spodoptera frugiperda), are commonly used for the production of recombinant proteins due to their ability to perform post-translational modifications, such as glycosylation, which are essential for the proper folding and functionality of many proteins .

Molecular Characteristics

The recombinant Bet v 1-A allergen is a glycosylated polypeptide chain with a calculated molecular mass of approximately 18.5 to 18.9 kDa . It consists of 167 amino acids and is often expressed with a His-tag at the N-terminus to facilitate purification . The protein is typically supplied in a sterile filtered clear solution and formulated in buffers such as HEPES or PBS to maintain stability .

Applications

Recombinant Bet v 1-A is primarily used in allergy research and diagnostics. It binds to IgE antibodies in human sera, making it valuable for immunodot tests and other diagnostic assays . The recombinant form allows for consistent and controlled studies, which are crucial for understanding the allergenic properties and developing potential treatments or preventive measures.

Stability and Storage

The stability of the recombinant Bet v 1-A allergen is maintained by storing it at 4°C for short-term use (2-4 weeks) or at -20°C for long-term storage. It is important to avoid multiple freeze-thaw cycles to preserve the protein’s integrity and functionality .

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