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T4132

Sigma-Aldrich

holo-Transferrin human

≥98%

Synonym(s):

Siderophilin, iron-saturated

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About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

human

Quality Level

assay

≥98%

form

powder

Iron content

1100-1600 μg/g

technique(s)

cell culture | mammalian: suitable

impurities

HIV, hepatitis B and hepatitis C, none detected

UniProt accession no.

storage temp.

2-8°C

Gene Information

human ... TF(7018)

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General description

Transferrin (TF) belongs to the family of bilobal glycoproteins, which bind ferric iron. The homologous N- and C-lobes of the protein have a single iron-binding site present in a deep cleft. The gene encoding TF is localized on human chromosome 3q22.1.

Application

Human holo-transferrin has been used:
  • in colony-forming assays
  • for transferrin uptake and recycling in transfected HEK-293 (human embryonic kidney) cells or bone marrow cells
  • for the preparation of luteinizing and non- luteinizing granulose cells

Biochem/physiol Actions

Studies have shown that co-treatment of breast cancer cells with holo-transferrin, which increases iron levels within cells and derivatives of artemisinin results in increased cell death.
Transferrin (TF) is the iron transport protein in the blood. Iron is transported in the serum by binding to circulating transferrin, which in turn binds to receptors on the cell surface. At the alkaline extracellular pH of 7.4, TF binds one or two ferric ions. The iron-bound TF molecules can bind the dimeric transferrin receptor (TfR). At this pH, iron-free transferrin is not recognized by TfR. This is followed by an endocytotic pathway involving the TfR, where the entire complex is internalized by endocytosis. As the pH reduces in the cell, iron is released from TF. The complex then returns to the cell surface and the apo-TF molecules dissociate from the receptor.

Analysis Note

Purity by agarose gel electrophoresis.

Disclaimer

RESEARCH USE ONLY. This product is regulated in France when intended to be used for scientific purposes, including for import and export activities (Article L 1211-1 paragraph 2 of the Public Health Code). The purchaser (i.e. enduser) is required to obtain an import authorization from the France Ministry of Research referred in the Article L1245-5-1 II. of Public Health Code. By ordering this product, you are confirming that you have obtained the proper import authorization.

Storage Class

11 - Combustible Solids

wgk_germany

WGK 3


Certificates of Analysis (COA)

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Selective toxicity of dihydroartemisinin and holotransferrin toward human breast cancer cells.
Singh NP
Life Sciences, 21, 49-56 (2001)
Atypical serum transferrin isoform distribution in liver cirrhosis studied by HPLC, capillary electrophoresis and transferrin genotyping.
Arndt T, et al.
Clinica Chimica Acta; International Journal of Clinical Chemistry, 394(1-2), 42-46 (2008)
Loss of Dynamin 2 GTP ase function results in microcytic anaemia.
Brown F, et al.
British Journal of Haematology, 178(4), 616-628 (2017)
Hypoxia-inducible factor 1 mediates hypoxia-enhanced synthesis of progesterone during luteinization of granulosa cells.
Yoshioka S, et al.
Journal of Reproduction and Development, 63(1), 75-85 (2017)
Nattawut Sinsuebphon et al.
Journal of biophotonics, 11(10), e201800037-e201800037 (2018-05-29)
Macroscopic fluorescence lifetime imaging (MFLI) has been proved to be an accurate tool to quantify Förster resonance energy transfer (FRET) lifetime-based assessment of receptor-ligand engagement in vitro and in vivo. Herein, we report on the quantitative comparison of MFLI for

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