Human Transferrin Protein, His Tag (MALS verified)
Synonym
Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086
Source
Human Transferrin Protein, His Tag (TRN-H52H3) 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 77.1 kDa. The protein migrates as 80-90 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE) due to glycosylation.
Endotoxin
Less than 1.0 EU per μg by the LAL method / rFC method.
Purity
>95% as determined by SDS-PAGE.
>95% as determined by SEC-MALS.
Formulation
Supplied as 0.2 μm filtered solution in PBS, pH7.4 with trehalose as protectant.
Contact us for customized product form or formulation.
Shipping
This product is supplied and shipped with dry ice, please inquire the shipping cost.
Storage
Please avoid repeated freeze-thaw cycles.
This product is stable after storage at:
The product MUST be stored at -70°C or lower upon receipt;
-70°C for 3 months under sterile conditions.
Background
Transferrin is 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 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.
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