Glycinin

Allergen Ara h 3.0101 Recombinant
Cat. No.
BT17553
Source

Escherichia Coli.

Synonyms

Glycinin, Arah3.

Appearance
Sterile Filtered clear solution.
Purity

Greater than 95% 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 Glycinin produced in E. coli is a non- glycosylated, polypeptide chain having a calculated molecular mass of 63 kDa.

Glycinin is expressed with a 10xHis tag at N-terminus and purified by proprietary chromatographic techniques.

Product Specs

Introduction
Glycinin Ara h 3, a seed storage protein found in peanuts, is classified as an 11S globulin and trypsin inhibitor. Its hexameric structure consists of subunits, each comprised of an acidic and a basic chain linked by a disulfide bond, originating from a single precursor. Notably, Ara h 3 and Ara h 4 are isoforms. Glycinin serves as a primary source of sulfur-containing amino acids in seed meals and is present in the seeds of various leguminous and non-leguminous plants.
Description
Recombinant Glycinin, produced in E. coli, is a non-glycosylated polypeptide chain with a calculated molecular mass of 63 kDa. It is expressed with a 10xHis tag at the N-terminus and purified using proprietary chromatographic techniques.
Physical Appearance
Clear, sterile-filtered solution.
Formulation
Glycinin is provided in a solution of 20mM HEPES buffer at pH 8, containing 6M Urea and 0.25M NaCl.
Stability
For short-term storage (2-4 weeks), maintain the product at 4°C. For extended storage, freeze at -20°C. Minimize freeze-thaw cycles to preserve product integrity.
Purity
Purity exceeds 95% as determined by SDS-PAGE analysis.
Immunological Functions
1. Exhibits binding affinity to human IgE antibodies. 2. Suitable for use in immunodot assays with positive and negative serum panels.
Synonyms

Glycinin, Arah3.

Source

Escherichia Coli.

Product Science Overview

Introduction

Allergen Ara h 3.0101, also known as Glycinin, is a major peanut allergen belonging to the legumin family of proteins. It is a storage protein found in peanuts and is known for its ability to withstand heat treatment and enzymatic activity. This allergen is significant due to its role in peanut allergies, which affect a substantial portion of the population, particularly in Western countries.

Biological Function and Structure

Ara h 3 is a cupin allergen, specifically an 11S globulin, which is a hexameric protein present in the seeds of many plants . The protein provides a significant portion of the total protein content in peanuts, along with other major allergens such as Ara h 1 and Ara h 2 . The recombinant form of Ara h 3 is produced using molecular cloning techniques, which allow for the generation of well-characterized, non-contaminated allergen components .

Allergenicity and Clinical Relevance

Ara h 3 is a major allergen for individuals with peanut allergies. Studies have shown that a significant percentage of peanut-allergic patients are sensitized to Ara h 3, and this sensitization is associated with more severe allergic reactions, including anaphylaxis . The use of specific IgE to Ara h 3, in combination with Ara h 1 and Ara h 2, can be helpful in diagnosing peanut allergies .

Epidemiology

Peanut allergies are prevalent in Western nations, with estimated rates between 1-2% . The prevalence appears to be lower in Asia and other global regions, although comprehensive epidemiological studies are limited . Sensitization to Ara h 3 is particularly significant in children, with the highest frequency of positive test results observed in the three to nine-year-old age group .

Recombinant Allergens in Research and Therapy

The development of recombinant allergens, including Ara h 3, has opened new avenues for allergy diagnosis and research. Recombinant allergens are widely used in molecule-based allergy diagnosis, such as protein microarrays or suspension arrays . These technologies have enabled the production of well-characterized vaccine components with known biological activities, including hypoallergenic derivatives with reduced IgE reactivity . Recombinant allergens have been successfully used in immunotherapy trials to treat various allergies, including birch and grass pollen allergies .

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