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- Tel: 858.663.9055
- Email: info@nsjbio.com
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Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. In humans, it is encoded by the TF gene. Transferrin consists of a polypeptide chain containing 679 amino acids in humans. The protein is composed of alpha helices and beta sheets to form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. Transferrin is a glycoprotein that binds iron very tightly but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). And Transferrin has a molecular weight of around 80 kDa and contains 2 specific high-affinity Fe(III) binding sites. The affinity of transferrin for Fe(III) is extremely high (1023 M?1 at pH 7.4) but decreases progressively with decreasing pH below neutrality.
Optimal dilution of the Transferrin antibody should be determined by the researcher.
Amino acids 20-49 (VPDKTVRWCAVSEHEATKCQSFRDHMKSVI) from the human protein were used as the immunogen for the Transferrin antibody.
After reconstitution, the Transferrin antibody can be stored for up to one month at 4oC. For long-term, aliquot and store at -20oC. Avoid repeated freezing and thawing.
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