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Recombinant Human Transferrin Protein / TF, 1mg  

Recombinant Human Transferrin Protein / TF, 1mg

Recombinant human Transferrin / TF (rhTF), Val20- Pro698, produced in human HEK 293 cells, fused with a C-terminal 6-His tag

Synonym: recombinant, human, protein, Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086

More details

TRN-H4229-1K

Availability: within 7 days

1 200,00 €

Background
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.[1] 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)[2] 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.[3] The metal binding properties of transferrin have a great influence on the biochemistry of plutonium in humans. Transferrin has a bacteriocidal 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.[4]

Source
Recombinant Human Transferrin, His Tag (TRN-H4229) is expressed from human 293 cells (HEK293). It contains AA Val 20 - Pro 698 (Accession # AAH59367). Predicted N-terminus: Val 20

Molecular Characterization
This protein carries a polyhistidine tag at the C-terminus.
The protein has a calculated MW of 76 kDa. The protein migrates as 75-100 kDa under reducing (R) condition (SDS-PAGE).

Endotoxin
Less than 1.0 EU per 1 μg of the rhFollistatin by the LAL method.

Purity
>95% as determined by SDS-PAGE. All lots are greater than 95% pure.

Formulation
Bulk protein in a 0.22 μm filtered solution of PBS, pH 7.4 and delivered as liquid formulation or lyophilized powder.Normally 5-8% trehalose and mannitol are added as protectants before lyophilization.

Reconstitution
See Certificate of Analysis for details of reconstitution instruction and specific concentration.

Bioactivity
Immobilized Human Transferrin, His Tag (Cat. No. TRN-H4229) at 2 μg/mL (100 μL/well) can bind Biotinylated Human TfR, His Tag (Cat. No. TFR-H8243) with a linear range of 5-78 ng/mL (QC tested).

Storage
Avoid repeated freeze-thaw cycles.
No activity loss was observed after storage at:
In lyophilized state for 1 year (4°C-8°C); After reconstitution under sterile conditions for 1 month (4°C-8°C) or 3 months (-20°C to -70°C).

References

(1) Crichton RR, Charloteaux-Wauters M. 1987, Eur. J. Biochem. 164 (3): 485–506.
(2) Aisen, Phillip, et al.,1978, Journal of Biological Chemistry 253 (6): 1930–1937.
(3) Ritchie RF,et al., 1999, J. Clin. Lab. Anal. 13 (6): 273–9.
(4) Sharpe PC, 2001, Ann. Clin. Biochem. 38 (Pt 6): 652–64.