Transferrin is a bilobed glycoprotein. The polypeptide chain of transferrin is composed of two homologous lobes i.e N- and C- lobes. Each lobe is made of two domains N1, N2 and C1, C2 which are linked by a hinge. It has two specific sites for binding of Fe3+.
Application
Anti-Transferrin antibody has been used:
in quantitative precipitin assay
in enzyme linked immunosorbent assay (ELISA)
in western blotting
in immunoblotting
Anti-Transferrin antibody produced in goat was used in western blotting analysis of HEK293 cell extracts.
Biochem/physiol Actions
Transferrin is the major iron transporter protein that binds Fe(+3). The transferring-iron import system consists of a TonB dependent transporter (TbpA), and a lipoprotein co-receptor (TbpB) and both proteins work together in the transport of iron across the membrane.
Transferrin plays a major role in providing iron as a source for haemoglobin synthesis. It binds to the transferrin receptor 1(TfR1).
Preparation Note
treated to remove lipoproteins
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Biochimica et biophysica acta, 1823(9), 1468-1483 (2012-05-23)
Cellular iron homeostasis is maintained by iron regulatory proteins 1 and 2 (IRP1 and IRP2). IRPs bind to iron-responsive elements (IREs) located in the untranslated regions of mRNAs encoding protein involved in iron uptake, storage, utilization and export. Over the
Journal of controlled release : official journal of the Controlled Release Society, 155(3), 386-392 (2011-07-16)
A proinsulin-transferrin (ProINS-Tf) recombinant fusion protein was designed and characterized for the sustained release of an active form of insulin (INS) by hepatoma cells. During incubation with H4IIE hepatoma cells, a gradual decline of ProINS-Tf concentration, with a concomitant generation
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