T1408
holo-Transferrin bovine
Synonym(s):
Siderophilin, Siderophilin, iron-saturated
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About This Item
Form:
powder
Assay:
97-100% (agarose gel electrophoresis)
Biological source:
bovine
biological source
bovine
assay
97-100% (agarose gel electrophoresis)
form
powder
technique(s)
cell culture | mammalian: suitable
UniProt accession no.
storage temp.
2-8°C
Quality Level
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
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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Dynamics of iron release from transferrin N-lobe studied by electrospray ionization mass spectrometry
Gumerov DR and Kaltashov IA
Analytical Chemistry, 73(11), 2565-2570 (2001)
New ammunition for the proteomic reactor: strong anion exchange beads and multiple enzymes enhance protein identification and sequence coverage
Zhou H, et al.
Analytical and Bioanalytical Chemistry, 397(8), 3421-3430 (2010)
Holo-transferrin and thrombin can interact to cause brain damage
Nakamura T, et al.
Stroke, 36(2), 348-352 (2005)
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)
Tomoji Ono et al.
The British journal of nutrition, 105(2), 200-211 (2010-09-22)
Lactoferrin (LF) is a multifunctional glycoprotein in mammalian milk. In a previous report, we showed that enteric-coated bovine LF tablets can decrease visceral fat accumulation, hypothesising that the enteric coating is critical to the functional peptides reaching the visceral fat
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