Human CellExp™ Transferrin, human recombinant

Biomolecule/Target: Transferrin

Synonyms: Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086.

Alternates names: Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086.

Taglines: An iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids

Taglines: USA

Country of Animal Origin: USA

NCBI Gene ID #.: 7018

NCBI Gene Symbol: TF

Gene Source: Human

Accession #: P02787

Recombinant: Yes

Source: HEK293 cells

Purity by SDS-PAGE #: ≥95%

Assay: SDS-PAGE

Purity: N/A

Assay #2: N/A

Endotoxin Level: <1 EU/μg by LAL method

Activity (Specifications/test method): N/A

Biological activity: N/A

Results: N/A

Binding Capacity: N/A

Unit Definition: N/A

Molecular Weight: This protein is fused with a C-terminal 6-His tag, and has a calculated MW of 76 kDa. DTT-reduced protein migrates as 74 kDa in SDS-PAGE due to glycosylation.

Concentration: N/A

Appearance: Lyophilized

Physical form description: Lyophilized from 0.22 μm filtered solution in 50 mM tris, 100 mM glycine, pH 7.0. Normally Mannitol or Trehalose is added as protectants before lyophilization.

Reconstitution Instructions: Centrifuge the vial prior to opening. Reconstitute in sterile PBS, pH 7.4 to a concentration of 50 µg/ml. Do not vortex. This solution can be stored at 2-8°C for up to 1 month. For extended storage, it is recommended to store at -20°C.

Background Information: Transferrin, also known as Serotransferrin, Beta-1 metal-binding globulin, TF, and is iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. Although iron bound to transferrin is less than 0.1% (4 mg) of the total body iron, it is the most important iron pool, with the highest rate of turnover (25 mg/24 h). The affinity of transferrin for Fe (III) is extremely high (1023 M−1 at pH 7.4) but decreases progressively with decreasing pH below neutrality. When not bound to iron, it is known as "apo-transferrin". In humans, transferrin consists of a polypeptide chain containing 679 amino acids. It is a complex composed of alpha helices and beta sheets to form two domains (the first situated in the N-terminus and the second in the C-terminus). The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. The liver is the main source of manufacturing transferrin, but other sources such as the brain also produce this molecule. Transferrin is also associated with the innate immune system. Transferrin is found in the mucosa and binds iron, thus creating an environment low in free iron that impedes bacteria survival in a process called iron withholding. The level of transferrin decreases in inflammation. The metal binding properties of transferrin have a great influence on the biochemistry of plutonium in humans. Transferrin has a bactericidal effect on bacteria, in that it makes Fe3+ unavailable to the bacteria. Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored via laboratory testing.

Amino acid sequence: N/A

Handling: Centrifuge the vial prior to opening.

Usage: For Research Use Only! Not to be used in humans