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The Anti-Transferrin Protein A Scaffold molecule was selected against human transferrin. Cross reactivity with other species has not been tested. The Anti-Transferrin Protein A Scaffold molecule is an ideal capture molecule for ELISA assays and works very well for purification and depletion of transferrin from plasma. The Anti- Transferrin Protein A Scaffold molecule is modified with a unique C-terminal cysteine for directed singlepoint chemical modification, facilitating coupling to matrices.
Suitable as capture reagent in ELISA and in Affinity Chromatography.
Anti-Transferrin Protein A scaffold molecule binds to human transferrin. Cross reactivity with other species has not been tested.
At +4°C is recommended for lyophilized protein. For reconstituted protein in physiological buffer, short-term storage at +4°C is recommended. For long-term storage, the protein solution should be aliquoted and then stored at -20°C. There is no decrease in
Transferrin is a single polypeptide chain glycoprotein with a molecular weight of 79.5 kDa. Transferrin (serotransferrin) circulates in the plasma, binds iron from donor cells and delivers it via the plasma to specific receptors on donor cells. The number of transferrin receptors varies according to the cells need for iron. The requirements for iron in the erythroid marrow and placenta are hundredfold greater than in other organs and transferrin is the only system available to meet this need. Transferrin is synthesized in the liver and consists of two domains each having a high affinity binding site for Fe3+. Transferrin is present in lymph and cerebrospinal fluid as well as in plasma. The plasma concentration range between 1.8-2.7 mg/ml but the concentration falls during iron overload and rises in iron deficiency states such as protein malnutrition, hemolysis and inflammation of various causes.
Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate. It is responsible for the transport of iron from sites of absorption and heme degradation to those of storage and utilization. Serum transferrin may also have a further role in stimulating cell proliferation.