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Key Documents

T2036

Sigma-Aldrich

apo-Transferrine human

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

Synonyme(s) :

Sidérophiline, Transferrine humaine

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About This Item

Numéro CAS:
Numéro CE :
Numéro MDL:
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.75

Gamme de produits

BioReagent

Niveau de qualité

Pureté

≥98% (agarose gel electrophoresis)

Forme

powder

Poids mol.

76-81 kDa

Concentration

~25 mM

Technique(s)

cell culture | mammalian: suitable

Impuretés

HIV and HBsAg, source material tested negative
endotoxin, tested

Solubilité

H2O: 50 mg/mL

Traces de cations

Fe: ≤0.005%

Numéro d'accès UniProt

Conditions d'expédition

ambient

Température de stockage

−20°C

Informations sur le gène

human ... TF(7018)

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Description générale

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

Actions biochimiques/physiologiques

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.

Autres remarques

Protéine de transport du fer du type non-hème.

Clause de non-responsabilité

Ce produit, destiné à la recherche scientifique, est soumis à une réglementation spécifique en France, y compris pour les activités d′importation et d′exportation (Article L 1211-1 alinéa 2 du Code de la Santé Publique). L′acheteur (c′est-à-dire l′utilisateur FINAL) est tenu d′obtenir une autorisation d′importation auprès du ministère français de la recherche, mentionné à l′article L1245-5-1 II du Code de la Santé Publique. En commandant ce produit, vous confirmez détenir l′autorisation d′importation requise.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3


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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.
Hanseul Park et al.
Nature communications, 14(1), 802-802 (2023-02-14)
Alzheimer's disease (AD) is associated with progressive neuronal degeneration as amyloid-beta (Aβ) and tau proteins accumulate in the brain. Glial cells were recently reported to play an important role in the development of AD. However, little is known about the
Kasumi Murai et al.
Nature communications, 13(1), 6206-6206 (2022-10-21)
Aging normal human oesophagus accumulates TP53 mutant clones. These are the origin of most oesophageal squamous carcinomas, in which biallelic TP53 disruption is almost universal. However, how p53 mutant clones expand and contribute to cancer development is unclear. Here we
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
Daniel Sommer et al.
Frontiers in molecular neuroscience, 15, 894230-894230 (2022-07-02)
Amyotrophic Lateral Sclerosis (ALS) is an incurable neurodegenerative disease characterized by dysfunction and loss of upper and lower motor neurons (MN). Despite several studies identifying drastic alterations affecting synaptic composition and functionality in different experimental models, the specific contribution of

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