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TF (Transferrin), Human
Catalog Number: EZC-TRN-H1
Synonym: Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086
Source: Recombinant human Transferrin / TF (rhTF) Val20- Pro698 (Accession # AAH59367 ) fused with a C-terminal 6-His tag was produced in human HEK 293 cells.
Molecular Characterization: rhTF 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.
Purity: >95% as determined by SDS-PAGE. All lots are greater than 95% pure.
Endotoxin: Less than 1.0 EU per 1 g of the rhFollistatin by the LAL method.
Formulation: Bulk protein in a 0.22 m 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.
Storage: Store at -20? in lyophilized state after receipt. For long term storage, upon reconstitution rhFollistatin should be aliquot and store at -20? or -80?. Avoid repeated freeze-thaw cycles.
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]
      Research Use Only. Not for use in diagnostic or therapeutic procedures.
Purchase This Product
  Size Price Number
  200 g $434.00
  1 mg $1,680.00
(1) Crichton RR, Charloteaux-Wauters M. 1987, Eur. J. Biochem. 164 (3): 485506. (2) Aisen, Phillip, et al.,1978, Journal of Biological Chemistry 253 (6): 19301937 (3) Zhou A, et al., 2003, Nat. Struct. Biol. 10 (7): 5414 (4) Sharpe PC, 2001, Ann. Clin. Biochem. 38 (Pt 6): 65264
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