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Safety Information

T2036

Sigma-Aldrich

apo-Transferrin human

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

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Synonym(s):
Human transferrin, Siderophilin
CAS Number:
11096-37-0
EC Number:
234-318-8
MDL number:
MFCD00130536
NACRES:
NA.75

product line

BioReagent

Quality Level

200

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.

P02787

shipped in

ambient

storage temp.

−20°C

Gene Information

human ... TF(7018)

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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

Regulatory Information

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  5. What is the carbohydrate content of human transferrin?

    We have found the information on transferrin in a reference book:The Plasma Proteins, F.W. Putnam, ed, volume 2, chapter 4, Table II.According to the table, Transferrin is 6 percent carbohydrate, citing G.A. Jamieson, J. Biol. Chem. 240(7), 2914-2920 (1965).The table also gives information on the percentage of each type of monosaccharide that is present.

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