Transferrin

Transferrin (TRF) is an important glycoprotein in human plasma, mainly synthesized in the liver. It is composed of 679 amino acid residues, with glycose accounting for about 6%. It has two highly homologous domains, the N - terminal and C - terminal. Each domain has a Fe³⁺ binding site and can reversibly bind two Fe³⁺. Transferrin can be divided into common transferrin, iron - saturated transferrin, etc. according to the iron - containing number, and can be divided into common - type transferrin and iso - type transferrin according to the configuration. Its main function is to act as a carrier for iron transport, transporting iron ions from absorption and storage sites to red blood cells and other iron - requiring cells, participating in the regulation of iron metabolism and balance, and also playing a role in respiration, cell proliferation, immune system regulation, and antibacterial and bactericidal aspects.



Product List

TargetCatalog#Product NameReactivityPredicted MW

Transferrin(HOLO)

PCH90044

GMP Recombinant Human

Transferrin

Human

75.2 kDa

Transferrin(APO)

PCH90046

GMP Recombinant Human

Transferrin(APO)

Human

75.2 kDa

Transferrin

PCB90045

GMP Recombinant Bovine Transferrin

Bovine

75.8 kDa

Transferrin

PCM90059

GMP Recombinant Mouse Transferrin

Mouse

74.5 kDa

Validation Data

GMP Recombinant Human Transferrin (HOLO) (Catalog: PCH90044)

undefined

             Transferrin (HOLO) SDS-PAGE image

undefined                        Bioactivity image: The ED50 for this effect is 0.5-2 μg/mL.

GMP Recombinant Human Transferrin(APO) (Catalog: PCH90046)

undefined                        Bioactivity image: The ED50 for this effect is ≤5 μg/mL.

References

1. Lobe specificity of iron binding to transferrin modulates murine erythropoiesis and iron homeostasis. Parrow NL, et al. Blood. 2019. [PMID: 31434707]