Anti-TNF alpha Affibody® Molecule

ab31908 is a recombinant protein produced in E. coli.

This Anti-TNF alpha Affibody^® Molecule is modified with a unique C-terminal cysteine for directed single-point chemical modification, facilitating labelling with fluorescent dyes, biotin or coupling to matrices. However, tail-to-tail dimers are spontaneously generated via a disulphide bridge between the C-terminal cysteines. Prior to coupling via the C-terminal the Affibody^® Molecule needs to be reduced to expose the reactive cysteine residue.

THIS AFFIBODY^® MOLECULE REQUIRES CONJUGATION TO A SUITABLE LABEL BEFORE USE. PLEASE REFER TO THE "PROTOCOLS" LINK

What are Affibody Molecules?
Affibody® affinity ligands are small, simple proteins composed of a three-helix bundle based on the scaffold of one of the IgG-binding domains of Protein A. Protein A is a surface protein from the bacterium Staphylococcus aureus. This scaffold has excellent features as an affinity ligand and can be designed to bind with high affinity to any given target protein. The domain consists of 58 amino acids, 13 of which are randomized to generate Affibody® libraries with a large number of ligand variants. Thus, the libraries consist of a multitude of protein ligands with an identical backbone and variable surface- binding properties. The current Affibody® libraries contains billions of variants. In function, Affibody® molecules mimic antibodies, nature's own binders to an infinite number of antigens. Compared to antibodies, the most striking dissimilarity of Affibody® molecules is the small size. Affibody® molecules have a molecular weight of 14 kDa, compared to the molecular weight of antibodies, which is 150 kDa. In spite of its small size, the binding site of Affibody® molecules is similar to that of an antibody. The advantages of Affibody® molecules over antibodies are · their small size · the simple structure of the molecules · its robust physical properties · its ability to fold correctly intracellularly · the fast and cost-efficient production in bacteria · the possibility to produce Affibody® molecules through chemical synthesis · the possibility to couple Affibody® molecules in multimeric constructs