Recombinant Human Transferrin Protein

Human transferrin is a single-chain glycoprotein. It has two potential N-linked glycosylation sites and one potential O-linked glycosylation site. Transferrin binds two Fe3+ ions, with high affinity (Kd = 10-20 M), together with two synergistically bound CO32- ions. The protein is mainly synthesized in the liver and secreted into the plasma. Lower amounts are also produced in other organs, such as the testis and brain. Transferrin is also capable of acting as a cytokine and has additional functions that may not be related to its iron-carrying capacity. For example, transferrin has been identified as one of the factors that promote the clonal growth of the precursors of murine granulocytes and macrophages cultured in vitro under serum-free conditions. Furthermore the presence of transferrin is vital for most cells grown in culture, such as in vitro fertilisation culturing, and in the maintenance and expansion of stem cell populations. Transferrin is frequently referred to as a growth factor due to the its growth factor-like properties, the high expression of transferrin receptors (TfRs) in proliferating cells, and the requirement for transferrin - TfR binding to initiate and maintain DNA synthesis in cells. Other roles for transferrin include acting as a neurotrophic factor in myotubule formation and as an angiogenic factor in promoting the migration and invasion of endothelial cells. This is a HCX protein. HCX Expression System Details HCX proteins mimic the proteins in the human body because they are expressed from human, rather than animal, insect or bacterial cells. This process gives them human post-translational modifications. Recombinant DNA techniques allow a human protein with the correct amino acid sequence to be expressed in a non-human cell line. However, non-human cells lack the appropriate cellular machinery, such as specific glycosyltransferases, necessary to produce the correct human post-translational modifications of a protein. An extreme example is seen in E. coli cells, which produce recombinant proteins with no glycosylation, as the above figure illustrates. Rodent and yeast cells are able to glycosylate proteins, but they are still different from glycosylation in human cells. Expression System Resultant Proteins Human (e.g. K562, HEK293) Correct amino acid sequence Human post-translational modifications Rodent (e.g. CHO, NSO) Correct amino acid sequence Some natural glycosylation - not human-like Yeast (e.g. Pichia) Correct amino acid sequence Some natural glycosylation - not human-like E.Coli Correct amino acid sequence No PTMs Although there have been significant attempts to make non-human cell derived cytokines more human-like, there is a growing awareness that in many instances, particularly in therapeutics, cytokines should mimic those found in the body as closely as possible. Purified Transferrin HCX consists of 5-20% carbohydrate by weight.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Peptides and proteins are guaranteed for 2 years from date of receipt.

Array NBP1-46259

• Transferrin Antibodies
• Transferrin Antibody Pair
• Transferrin ELISA Kits
• Transferrin Proteins