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Human CellExp Transferrin, human recombinant protein
Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086.
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P02787 |
|---|---|
| Calculated MW | 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. |
| Gene ID | 7018 |
|---|---|
| Gene Symbol | TF |
| Other Names | Transferrin, TF, DKFZp781D0156, PRO1557, PRO2086. |
| Gene Source | Human |
| Source | HEK293 cells |
| Assay&Purity | SDS-PAGE; ≥95% |
| Assay2&Purity2 | N/A; |
| Recombinant | Yes |
| Target/Specificity | Transferrin |
| Application Notes | 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. |
| Format | Lyophilized |
| Storage | -20°C; 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. |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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Provided below are standard protocols that you may find useful for product applications.
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. 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.
References
Yang F.,et al.Proc. Natl. Acad. Sci. U.S.A. 81:2752-2756(1984).
Schaeffer E.,et al.Gene 56:109-116(1987).
Hershberger C.L.,et al.Ann. N. Y. Acad. Sci. 646:140-154(1991).
Beutler E.,et al.Blood 96:4071-4074(2000).
Muzny D.M.,et al.Nature 440:1194-1198(2006).
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