Iron (Fe) is a tightly metabolically controlled mineral and growth factor present in all living cells. Iron not bound in erythrocyte hemoglobin is transported by transferrin (Tf), the iron transport protein of vertebrate serum. The transferrin protein contains two homologous domains, each of which contain an Fe-binding site. The majority of transferrin is synthesized in the liver and secreted into the blood, but it is also produced in lower amounts in testis and brain as well as in oligodendrocytes, where transferrin is an early marker of oligodendrocyte differentiation. From the blood, transferrin is internalized by erythroblasts and reticulocytes upon binding the transferrin receptor (TfR), also designated CD71, through a system of coated pits and vesicles. After Fe release, transferrin is returned to the extracellular medium, where it can be reused. Defects in the transferrin gene results in atransferrinemia, a rare autosomal recessive disorder characterized by microcytic anemia and iron loading.
200ug/ml of Ab purified from Bioreactor Concentrate by Protein A/G. Prepared in 10mM PBS with 0.05% BSA & 0.05% azide. Also available WITHOUT BSA & azide at 1.0mg/ml.
Formalin-fixed, paraffin-embedded human kidney stained with Transferrin Mouse Monoclonal Antibody (TF/4798). Inset: PBS instead of primary antibody, secondary only negative control.
SDS-PAGE Analysis of Purified Transferrin Mouse Monoclonal Antibody (TF/4798). Confirmation of Purity and Integrity of Antibody.
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