T1408
holo-Transferrin bovine
Synonym(s):
Siderophilin, Siderophilin, iron-saturated
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About This Item
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biological source
bovine
Quality Level
Assay
97-100% (agarose gel electrophoresis)
form
powder
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
storage temp.
2-8°C
Gene Information
bovine ... TF(280705)
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General description
Holo-Transferrin is an iron transporting glycoprotein and belongs to metalloprotein class. The gene encoding transferrin is mapped to bovine chromosome 1.
Application
Holo-Transferrin bovine has been used:
- as a RPMI-1640 medium supplement for culturing cancer cell lines
- as a component of visceral fat differentiation medium for the pre-adipocytes primary cell culture
- to test the influence of iron-saturation complex on the growth of Malassezia pachydermatis
- as a standard for strong anion exchange (SAX) reactor measurements
Biochem/physiol Actions
Holo-Transferrin (holo-Tf) or the iron bound transferrin functions as an iron sequester and is crucial for defense against microbial infections. Transferrin is used as a model system for understanding the kinetics and dynamics of protein structure based interactions. It is a potential candidate for delivery studies for its ability to cross the blood-brain barrier. The interaction of holo-Tf with thrombin is implicated in the pathogenesis of intracerebral hemorrhage. Polymorphisms in the bovine transferrin gene has led to the generation of 10 variant transferrin protein.
Studies show that treatment of breast cancer cells with holo-transferrin in combination with dihydroartemisinin results in increased tumor cell death due to elevated levels of intracellular ferrous iron.
Analysis Note
Purity by agarose gel electrophoresis.
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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Holo-transferrin and thrombin can interact to cause brain damage
Nakamura T, et al.
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Transferrin as a model system for method development to study structure, dynamics and interactions of metalloproteins using mass spectrometry
Kaltashov IA, et al.
Biochim. Biophys. Acta Gen. Subj., 1820(3), 417-426 (2012)
A single nucleotide polymorphism in the coding region of bovine transferrin is associated with milk fat yield
Sanz A, et al.
Genetics and molecular research : GMR, 9(2), 843-848 (2010)
Bovine and canine transferrin inhibit the growth of Malassezia pachydermatis in vitro
Bond R, et al.
Medical Mycology, 43(5), 447-451 (2005)
N P Singh et al.
Life sciences, 70(1), 49-56 (2002-01-05)
Artemisinin becomes cytotoxic in the presence of ferrous iron. Since iron influx is high in cancer cells, artemisinin and its analogs selectively kill cancer cells under conditions that increase intracellular iron concentrations. We report here that after incubation with holotransferrin
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