Transferrin, HOLO, 98+% Protein

Transferrin, Human, HOLO, 98+% (Iron-saturated Siderophilin, TRF)

Cat. Num. AAA634995

• Applications: ELISA
• Purity: Highly Purified; 98% by SDS. Purification procedures include selective size exclusion, ion exchange chromatography and gel fitration. SDS-Polyacrylamide gel electrophoresis shows one major band only corresponding to the molecular weight of human Transfe
• Synonyms: Transferrin; HOLO; 98+%; Human; 98+% (Iron-saturated Siderophilin; TRF); 98+% protein

• Host: Human serum
• Purity/Purification: Highly Purified; 98% by SDS. Purification procedures include selective size exclusion, ion exchange chromatography and gel fitration. SDS-Polyacrylamide gel electrophoresis shows one major band only corresponding to the molecular weight of human Transfe
• Form/Format: Supplied as a dark red, lyophilized powder. Reconstitute in phosphate buffer with 0.15M sodium chloride, pH 7.0.

• Applicable Applications for Transferrin, HOLO, 98+% protein: ELISA (EL/EIA)
• Application Notes: Suitable for use in ELISA.
• Preparation and Storage: Lyophilized powder may be stored at 4 degree C for short-term only. Reconstitute to nominal volume by adding sterile physiological buffer and store at -20 degree C. Reconstituted product is stable for 12 months at -20 degree C. For maximum recovery of product, centrifuge the original vial prior to removing the cap. Further dilutions can be made in assay buffer.

Testing Data

(Transferin, TF, Apotransferrin, Beta-1 Metal-binding Globulin, DKFZp781D0156, PRO1400, PRO1557, PRO2086, Serotransferrin Precursor, Siderophilin)

Related Product Information for Transferrin, HOLO, 98+% protein

Transferrin is a single polypeptide chain glycoprotein and is a member of the iron binding family of proteins. It has a molecular weight of ~79.5kD and a serum concentration range of 1800-2700mg/L. It is synthesized in the liver and consists of two domains each having a high affinity reversible binding site for Fe3+. The iron is transported in blood and interstitial fluids to sites of use and disposal. Iron/transferrin is essential in hemoglobin synthesis and for certain types of cell division. Serum concentration rises in iron deficiency and pregnancy and falls in iron overload, infection and inflammatory conditions.

Human Transferrin is a glycoprotein with homologous N-terminal and C-terminal iron binding domains. Transferrin(TF) is related to other iron binding proteins including lactoferrin. When human transferrin loaded with iron encounters a transferrin receptor on the surface of a cell, it binds to it and is consequently transported into the cell in a vesicle. The cell will acidify the vesicle, causing human transferrin(TF) to release its iron ions. Each human transferrin molecule has the ability to carry two iron ions in the ferric form (Fe3+).
Human Transferrin levels may be checked in iron deficiency, hemochromatosis and other iron overload disorders. Transferrin is also associated with the innate immune system. Human Transferrin is found in the mucosa and binds iron, thus creating an environment low in free iron, where few bacteria are able to survive.

Product Categories/Family for Transferrin, HOLO, 98+% protein

Molecular Biology; MB-Transferrin