Anti-Transferrin Receptor / TFRC / CD71, clone TFRC/1396

1 mg/ml in 1X PBS, BSA free, sodium azide free. It recognizes a ~90-95kDa protein which is identified as cell surface transferrin receptor (CD71), a disulfide-bonded homodimeric glycoprotein of 180-190kDa. This MAb is highly specific to CD71 and shows no cross-reaction with other related proteins. Ligand for transferrin receptor is the serum iron transport protein, transferrin. This receptor is broadly distributed in carcinomas, sarcomas, leukemias, and lymphomas. CD71/Transferrin receptor has been reported to be associated with cell proliferation in both normal and neoplastic tissues and useful in predicting clinical behavior or response to therapy in a number of malignancies including breast cancer. Protein function: Cellular uptake of iron occurs via receptor-mediated endocytosis of ligand-occupied transferrin receptor into specialized endosomes (PubMed:26214738). Endosomal acidification leads to iron release. The apotransferrin-receptor complex is then recycled to the cell surface with a return to neutral pH and the concomitant loss of affinity of apotransferrin for its receptor. Transferrin receptor is necessary for development of erythrocytes and the nervous system. A second ligand, the hereditary hemochromatosis protein HFE, competes for binding with transferrin for an overlapping C- terminal binding site. Positively regulates T and B cell proliferation through iron uptake (PubMed:26642240). Acts as a lipid sensor that regulates mitochondrial fusion by regulating activation of the JNK pathway (PubMed:26214738). When dietary levels of stearate (C18:0) are low, promotes activation of the JNK pathway, resulting in HUWE1- mediated ubiquitination and subsequent degradation of the mitofusin MFN2 and inhibition of mitochondrial fusion (PubMed:26214738). When dietary levels of stearate (C18:0) are high, TFRC stearoylation inhibits activation of the JNK pathway and thus degradation of the mitofusin MFN2 (PubMed:26214738). Mediates uptake of NICOL1 into fibroblasts where it may regulate extracellular matrix production. [The UniProt Consortium]