Anti-Transferrin/TF Antibody Picoband® (Dylight488 Conjugate)

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.

A synthetic peptide corresponding to a sequence at the N-terminus of human Transferrin, different from the related mouse and rat sequences by five amino acids.

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.

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br> Immunohistochemistry (Paraffin-embedded Section), 2-5μg/ml, Human, By Heat<br> Flow Cytometry(Fixed), 1-3 μg/1x10⁶ cells, Human<br>