Skip to Content
MilliporeSigma
All Photos(3)

Documents

T2036

Sigma-Aldrich

apo-Transferrin human

powder, BioReagent, suitable for cell culture, ≥98% (agarose gel electrophoresis)

Synonym(s):

Human transferrin, Siderophilin

Sign Into View Organizational & Contract Pricing


About This Item

CAS Number:
EC Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.75

product line

BioReagent

Assay

≥98% (agarose gel electrophoresis)

form

powder

mol wt

76-81 kDa

concentration

~25 mM

technique(s)

cell culture | mammalian: suitable

impurities

HIV and HBsAg, source material tested negative
endotoxin, tested

solubility

H2O: 50 mg/mL

cation traces

Fe: ≤0.005%

UniProt accession no.

shipped in

ambient

storage temp.

−20°C

Gene Information

human ... TF(7018)

Looking for similar products? Visit Product Comparison Guide

General description

Transferrin, majorly synthesized in the liver, is an abundant glycoprotein in the serum. The members of the transferrin superfamily have similar polypeptide folding patterns. Transferrin contains N- and C-terminal iron-binding homologous domains. Each of these domains is split into two subdomains having binding sites for iron and anions within the inter-subdomain cleft. The binding cleft opens and closes with iron releasing and iron binding. apo-Transferrin is an iron-free protein that arises after transferrin dissociates from its receptor. This product can be supplemented with iron or used to bind free iron present in media.

Application

apo-Transferrin human has been used:
  • to culture human primary pancreatic endothelial cells, Het1As (non-tumorous esophagus cells), and immortalized human colonic epithelial cells (HCEC-1CT)
  • to culture α mouse liver 12 (AML-12) (mature hepatocytes) cells
  • as a source for human apo-transferrin for purification before crystallography

Biochem/physiol Actions

Transferrin is responsible for transporting iron from the sites of absorption and storage to the tissue cells. It maintains the levels of iron in biological fluids. The levels of transferrin may indicate the total iron-binding capacity (TIBC). Transferrin supplies the required iron for incorporation into hemoglobin within RBCs in the bone marrow. Iron deficiency causes an increase in the levels of transferrin. Pregnancy and estrogen administration can also raise the levels of transferrin. Chronic liver disease, renal insufficiency, malnutrition, and protein-losing enteropathies reduce the synthesis of transferrin.

Other Notes

Non-heme iron-transport protein.

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 Code

11 - Combustible Solids

WGK

WGK 3


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Justin P Curtin et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 23(3), 471-480 (2018-04-07)
The presence of ionic titanium in the serum of patients with titanium implants is currently unexplained. This is presumed due to corrosion, and yet the serum titanium concentration measured in patients is far greater than that predicted by its solubility.
Huifang Lian et al.
Frontiers in medicine, 9, 845129-845129 (2022-04-26)
Fungal keratitis is a sight-threatening corneal infection caused by fungal pathogens, and the pathogenic mechanisms have not been fully elucidated. The aim of this study was to determine whether NOD-like receptor family pyrin domain containing 3 (NLRP3) inflammasome-mediated pyroptosis contributes
Carmen Mirabelli et al.
Proceedings of the National Academy of Sciences of the United States of America, 118(36) (2021-08-21)
The global spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and the associated disease COVID-19, requires therapeutic interventions that can be rapidly identified and translated to clinical care. Traditional drug discovery methods have a >90% failure rate and
Carmen Mirabelli et al.
bioRxiv : the preprint server for biology (2020-06-25)
The global spread of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), and the associated disease COVID-19, requires therapeutic interventions that can be rapidly identified and translated to clinical care. Traditional drug discovery methods have a >90% failure rate and
Orsolya Dömötör et al.
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 27(3), 315-328 (2022-03-05)
Solution speciation and serum protein binding of selected In(III) complexes bearing O,O and O,N donor sets were studied to provide comparative data for In(III) and analogous Ga(III) complexes. Aqueous stability of the In(III) complexes of maltol, deferiprone, 8-hydroxyquinoline (HQ) and

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service