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T1408

Sigma-Aldrich

holo-Transferrin bovine

Sinónimos:

Siderophilin, Siderophilin, iron-saturated

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About This Item

Número de CAS:
11096-37-0
EC Number:
234-318-8
MDL number:
MFCD00131337
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine

assay

97-100% (agarose gel electrophoresis)

form

powder

technique(s)

cell culture | mammalian: suitable

UniProt accession no.

Q29443

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

11 - Combustible Solids

wgk_germany

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Certificados de análisis (COA)

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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)
Jillian R Gunther et al.
ACS chemical biology, 4(6), 435-440 (2009-05-16)
Compounds that directly disrupt the androgen receptor/steroid receptor coactivator interaction could function as novel inhibitors of androgen signaling that would remain effective in the treatment of prostate cancer that is resistant to conventional endocrine therapies. A structure-based peptidomimetic approach was
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
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)
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