Avidin Recombinant
Corn (Zea Mays).
Sterile Filtered white lyophilized powder.
Greater than 90% as visualized by SDS-PAGE.
Description
Recombinant Avidin produced in Plants is a polypeptide chain having a molecular mass of 66kDa and 16kda per subunit.
The Recombinant Avidin is purified by affinity chromatographic techniques.
Product Specs
Avidin is a protein composed of four identical subunits, known as a homotetramer. Each subunit strongly binds to a molecule called biotin. The total molecular weight of the tetrameric Avidin is estimated to be between 66,000 and 69,000 Daltons. Avidin is found in the egg whites of birds, reptiles, and amphibians, originating from their reproductive systems. Chicken egg whites contain approximately 0.05% Avidin by weight, equating to about 1.8 milligrams per egg. Carbohydrates contribute to about 10% of Avidin's molecular weight. These carbohydrates consist of 4-5 mannose units and 3 N-acetylglucosamine units. Avidin possesses at least three distinct types of oligosaccharide structures, which are very similar in their composition and arrangement. Its strong binding affinity for biotin is represented by a dissociation constant (KD) of approximately 10-15M, making it one of the strongest non-covalent bonds known.
Recombinant Avidin, produced in plants, is a polypeptide with a molecular mass of 66 kDa, with each of its four subunits having a mass of 16 kDa. The purification of this Recombinant Avidin is achieved through affinity chromatography techniques.
Sterile Filtered white lyophilized powder.
To reconstitute the lyophilized Recombinant Avidin, it is recommended to dissolve it in sterile 18MΩ-cm H₂O. The final concentration of the solution should be between 100 µg/ml and 10 mg/ml.
Lyophilized Recombinant Avidin remains stable for 3 weeks at room temperature. However, for long-term storage, it should be stored in a dry environment below -18°C. After reconstitution, the Recombinant Avidin solution should be stored at 4°C for a maximum of 2-7 days. For storage beyond this period, it is recommended to store the solution below -18°C. Adding a carrier protein (0.1% HSA or BSA) is suggested for long-term storage. Avoid repeated freezing and thawing of the Recombinant Avidin.
The purity of the Recombinant Avidin is determined to be greater than 90% based on SDS-PAGE analysis.
The biological activity of Recombinant Avidin is measured as 13.5 units per mg of protein. One unit of activity is defined as the amount of Avidin that can bind to 1 µg of biotin.
Corn (Zea Mays).
Product Science Overview
Avidin is a tetrameric protein, meaning it consists of four subunits, each capable of binding one biotin molecule. The structure of avidin is highly stable, both in its free form and when complexed with biotin . This stability is due to the compact nature of the protein and the strong interactions between the subunits and biotin.
Recombinant avidin refers to avidin that is produced using recombinant DNA technology. This involves inserting the gene encoding avidin into a host organism, such as bacteria or yeast, which then produces the protein. Recombinant avidin has several advantages over naturally sourced avidin, including higher purity, consistency, and the ability to introduce specific mutations to alter its properties .
The avidin-biotin interaction is widely exploited in various fields:
- Biotechnology: Avidin is used in affinity chromatography to purify biotinylated proteins and other molecules. The strong binding between avidin and biotin ensures that biotinylated molecules can be selectively captured and purified from complex mixtures .
- Diagnostics: Avidin-biotin systems are used in various diagnostic assays, including enzyme-linked immunosorbent assays (ELISAs) and immunohistochemistry. The high affinity and specificity of the avidin-biotin interaction enhance the sensitivity and accuracy of these assays .
- Drug Delivery: Avidin can be used to target biotinylated drugs to specific cells or tissues. This targeted delivery system can improve the efficacy and reduce the side effects of therapeutic agents .
Avidin is not unique to birds; similar proteins have been found in other organisms, including bacteria. Streptavidin, a protein from the bacterium Streptomyces avidinii, shares similar biotin-binding properties with avidin but has different structural and functional characteristics . The discovery of various avidin-like proteins across different species highlights the evolutionary diversity and significance of biotin-binding proteins .
