Cor a 14.0101
Sf9 insect cells.
Greater than 80.0% as determined by SDS-PAGE.
Description
Recombinant 2S albumin produced in SF9 is a glycosylated, polypeptide chain having a calculated molecular mass of 14kDa.
Cor a 14.0101 is expressed with a 6xHis tag and purified by proprietary chromatographic techniques.
Product Specs
Sf9 insect cells.
Product Science Overview
2S albumins are generally heterodimers composed of two different polypeptide chains linked by disulfide bonds. These chains are formed from the post-translational proteolysis of a precursor protein. For example, the well-characterized 2S albumin from oilseed rape, known as napin, consists of large and small subunits with molecular masses of 9 and 4 kilodaltons, respectively . The three-dimensional structure of 2S albumins is compact and globular, enriched in alpha-helices .
The exact physiological function of 2S albumins is not entirely understood. However, it is believed that these proteins act as nitrogen and sulfur donors based on their amino acid composition and their high content in seeds. They are mobilized during seed germination to provide essential nutrients for the developing plant . Additionally, 2S albumins have been proposed to have antifungal activity, serine protease inhibition, and calmodulin antagonism .
2S albumins have attracted considerable attention in allergen science due to their allergenic potential. Several notable food allergens, such as Sin a 1 from mustard and Bra j 1 from broccoli, belong to this protein family . The allergenic properties of 2S albumins are often linked to specific regions within their structure that interact with the immune system .
Recombinant 2S albumin refers to the production of 2S albumin proteins using recombinant DNA technology. This involves inserting the gene encoding the 2S albumin protein into a suitable expression system, such as bacteria or yeast, to produce the protein in large quantities. Recombinant 2S albumins are valuable for research purposes, particularly in studying their structure, function, and allergenic properties .
An example of a recombinant 2S albumin is Ber e 1, the major allergen from Brazil nuts. The solution structure of recombinant Ber e 1 has been solved using nuclear magnetic resonance spectroscopy. This protein has a hydrophobic cavity that can interact with divalent copper ions, which may influence its allergenic properties . The overall fold of Ber e 1 is similar to other 2S albumins, but its unique structural features contribute to its specific interactions and allergenic potential .
In conclusion, 2S albumins are a fascinating group of proteins with significant implications in both plant physiology and allergen science. The use of recombinant DNA technology to produce these proteins has opened up new avenues for research and potential applications in biotechnology.
