Chinese Hamster Ovary cells.
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Sterile Filtered clear solution.
Protein is >95% pure as determined by 10% PAGE (coomassie staining).
Recombinant Human Transferrin produced in CHO cells is a glycosylated, polypeptide chain containing having a molecular mass of 76 kDa. Human Transferrin has homologous C and N-terminal domains, each of which binds one ion of ferric iron.
Recombinant Human Transferrin, produced in CHO cells, is a glycosylated polypeptide chain with a molecular mass of 76 kDa. It features homologous C and N-terminal domains, each capable of binding a single ferric iron ion.
A clear, sterile-filtered solution.
The Transferrin solution is formulated with 0.05% NaN3 and PBS.
For use within 2-4 weeks, store at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein (0.1% HSA or BSA) is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
The protein exhibits a purity greater than 95% as determined by 10% PAGE (coomassie staining).
Suitable applications include immunoassays and cell culture.
Serotransferrin, Transferrin, Siderophilin, Beta-1-metal-binding globulin, TF, PRO1557, PRO2086, DKFZp781D0156, HTF.
Chinese Hamster Ovary cells.
Transferrin is composed of two homologous domains, each capable of binding one ferric iron ion (Fe³⁺). This binding is essential for the transport of iron to various tissues and cells, where it is utilized for processes such as DNA synthesis and oxygen transport . The molecular weight of transferrin is approximately 76.5 kDa .
The recombinant form of human transferrin is produced using CHO cells, which are widely used in biotechnology for the production of therapeutic proteins. CHO cells are preferred due to their ability to perform post-translational modifications, such as glycosylation, which are crucial for the stability and functionality of the protein .