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| Product Name | Native Human Transferrin (Partially Saturated) |
| Catalog No. | RESK-0481 |
| Description | Human transferrin (TRF, siderophilin) is a glycoprotein with homologous N-terminal and C-terminal iron-binding domains. It is related to several other iron-binding proteins, including lactoferrin, melanotransferrin, and ovotransferrin, which belong to the transferrin superfamily. Transferrin is the main iron-containing protein in plasma, responsible for transporting iron absorbed by the digestive tract and iron released from the degradation of red blood cells; it enters the bone marrow as a TRF-Fe3+ complex to support the production of mature red blood cells. TRF is a single-chain glycoprotein with a carbohydrate content of approximately 6%. TRF reversibly binds multivalent ions, including iron, copper, zinc, and cobalt, and each TRF molecule can bind two ferric iron atoms. TRF is mainly synthesized by hepatocytes and has a half-life of 7 days. The plasma TRF concentration is regulated by iron supply: it rises in iron-deficiency states and returns to normal after effective iron therapy. Plasma TRF levels can be used for the diagnosis of anemia and for monitoring treatment. In iron-deficiency hypochromic anemia, TRF levels increase (due to increased synthesis), but its iron saturation is very low (normal range 30%-38%). Conversely, if anemia is caused by impaired iron utilization by red blood cells (e.g., aplastic anemia), plasma TRF is normal or low, but iron saturation is increased. In iron overload, TRF levels are normal, but saturation can exceed 50%, even reaching 90%. TRF tends to decrease in acute-phase reactions, so it often declines together with albumin and prealbumin in inflammation and malignant disease. It also decreases in chronic liver disease and malnutrition and can therefore serve as an indicator of nutritional status. |
| Intended Use | Used as an iron-transporting glycoprotein in research applications; plasma transferrin levels can be used in the study of anemia diagnosis, treatment monitoring, and nutritional status assessment. |
| Principle / Technology | Transferrin reversibly binds multivalent ions, including iron, copper, zinc, and cobalt; each transferrin molecule can bind two ferric iron atoms. Naturally extracted from human serum. |
| Performance Range / Specifications | Source: natural extraction English synonym: Siderophilin, partially saturated Molecular weight: 76-81 kDa Purity: >=98% (lyophilized powder) Solubility: soluble in water Iron content: 300-600 ppm CAS Number: 11096-37-0 Endotoxin level: <1.0 endotoxin units/mg Lambda max: 280 nm (water) |
| Storage Conditions | 2-8 °C. Do not freeze. |
| Shelf Life | 3 years |
| Package Specifications | 100 mg, 500 mg, 1 g |
| Product Form | Lyophilized powder |
| Quality Control | Purity >=98% (lyophilized powder); endotoxin level <1.0 endotoxin units/mg. |
| Purity | >=98% (lyophilized powder) |
| Molecular Weight | 76-81 kDa |
| Source / Origin | Naturally extracted from human serum. |
| Regulatory / Compliance | For research use only. |
| Application Notes / Precautions | Do not freeze the product after preparation into solution, as freezing will affect product activity. This product is partially saturated; the degree of saturation has not been experimentally determined. This product does not contain beta lactam. |
For research use only, not for clinical use.
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