Human ApoTransferrin
Native whole molecule Transferrin but lacking bound iron. Iron Content: <30 µg per gram
Produktdetails
Synonyms
Apo indicates the Transferrin is free of Iron. Siderophilin, Serotransferrin, Beta-1 metal-binding globulin, ApoTRF, ApoTF, PRO1400, PRO1557
Description of Human ApoTransferrin
Human ApoTransferrin is a 80 kDa protein. Apotransferrin, the iron-free form of the glycoprotein transferrin, serves as a critical regulator of systemic iron homeostasis by binding and transporting ferric ions (Fe³⁺) through plasma via a pH-dependent mechanism. It exhibits a structure with two iron-binding sites. Beyond its primary role in iron distribution, apotransferrin modulates immune function by sequestering free iron to limit microbial growth and directly suppresses proinflammatory cytokine production in autoimmune conditions like type 1 diabetes. Clinically, congenital atransferrinemia-caused by TF gene mutations-manifests as severe microcytic anemia coupled with tissue iron overload, requiring lifelong apotransferrin replacement therapy. In biotechnology, ultra-purified apotransferrin (<0.01% iron content, 1.25 µg/mg iron-binding capacity) serves as an essential cell culture supplement, facilitating iron uptake through transferrin receptor-mediated endocytosis while preventing oxidative stress. Recent applications exploit its targeting potential in nanoparticle drug delivery systems for cancer therapeutics and as an antimicrobial adjuvant to enhance antibiotic efficacy against Gram-negative pathogens. The protein's solubility (10 mg/ml in aqueous solutions) and stability under physiological conditions enable its use in diagnostic assays and bioreactor media for biopharmaceutical production.
Source
Human plasma non-reactive for HBsAG, anti-HCV, anti-HBc, and negative for anti-HIV 1 & 2 by FDA approved tests
Storage
For long term, store Human ApoTransferrin at -20°C.
Applications
ELISA, Antigen for Antibody production, IVD Antigens, Calibrators & Controls, Protein Chemistry Research, Drug Delivery research.
Citations/Publications
Dziuba, N., et al., (2018) 'Low-molecular-mass iron in healthy blood plasma is not predominately ferric citrate', Metallomics, 10: pp. 802. Available at: https://doi.org/10.1039/C8MT00055G
Lane, D. D., et al., (2020) 'Effects of core titanium crystal dimension and crystal phase on ROS generation and tumour accumulation of transferrin coated titanium dioxide nanoaggregates', RSC Adv., 10: pp. 23759. Available at: DOI https://doi.org/10.1039/D0RA01878C
Profitt, L. A., et al., (2022) 'Superstoichiometric Binding of the Anticancer Agent Titanocene Dichloride by Human Serum Transferrin and the Accompanying Lobe Closure', Biochemistry, 61(9): pp. 795–803. Available at: https://doi.org/10.1021/acs.biochem.1c00813
Sakamoto, K., et al., (2017) 'IL-22 Controls Iron-Dependent Nutritional Immunity Against Systemic Bacterial Infections', Sci Immunol., 2(8): Available at: doi:10.1126/sciimmunol.aai8371.
Malone, C. D., et al., (2022) 'Activation of nano‑photosensitizers by Y‑90 microspheres to enhance oxidative stress and cell death in hepatocellular carcinoma', Sci Rep, 12: pp. 12748. Aviable at: https://doi.org/10.1038/s41598-022-17185-0
NCBI: https://www.ncbi.nlm.nih.gov/protein/P02787
Shipped with ice packs
Gel Scan of Human ApoTransferrin
Fig. 1: SDS-PAGE Gel |
Usage: For research use only. Not for use in diagnostic or therapeutic procedures. Not for human use.
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