|
|
| Format : |
Purified |
| Amount : |
100 µg |
Transferrin (Tsf) is a multitask secretory glycoprotein involved in a wide range of physiological functions, starting from delicate iron homeostasis, growth, differentiation, to an array of cytoprotective activities including apoptosis. It has high affinity binding sites for iron and thereby maintains a safe level of free iron in body tissues. Iron binding to Tsf creates a physiological ambience for the smooth functioning of cellular processes and at the same time it provides a bacteriostatic environment by limiting the availability of iron, essentially required for the multiplication of pathogens. Tsf has been well characterized in many multicellular animals and some insect families.
REFERENCES:
1. Dutta, A., Dandapat, J. and Mohanty, N. (2019) First report on transferrin in the silkworm, Antheraea mylitta, with a putative role in antioxidant defense: Insights from proteomic analysis and immune detection. Comparative Biochemistry and Physiology Part B. 233: 23-34.
2. Geiser, D. L.,Winzerling, J. J. (2012) Insect transferrins: multifunctional proteins. Biochim Biophys Acta. 1820: 437-51.
Transferrin antibody is highly recommended for the detection of transferrin in silkworm Antheraea mylitta, Spodoptera litura, Leucinodes orbonalis, Drosophilla melanogaster, Apis cerana indica, Drosophilla melanogaster and Rattus norvegicus. Transferrin is detected by western blotting in all the above species. Transferrin is also detected in all tissues and cells of silkworm Antheraea mylitta by western blotting, Immunofluorescence and immunohistochemistry. Molecular weight of transferrin is 75 kDa.
1. Dutta A, Dandapat J, Mohanty N. First report on transferrin in the silkworm, Antheraea mylitta, with a putative role in antioxidant defense: Insights from proteomic analysis and immunodetection. Comp Biochem Physiol B Biochem Mol Biol. 2019;233:23-34. doi:10.1016/j.cbpb.2019.03.010
