Technical Data

T8199-12
CAS Number
11096-37-0
Grade
Highly Purified
Applications
E
Molecular Weight
77
EU Commodity Code
38220090
Shipping Temp
Blue Ice
Storage Temp
4°C
Transferrin, Human, HOLO, 99+% (Iron-saturated Siderophilin, TRF)
Transferin, TF, Apotransferrin, Beta-1 Metal-binding Globulin, DKFZp781D0156, PRO1400, PRO1557, PRO2086, Serotransferrin Precursor, Siderophilin

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.
Iron
As Reported
Endotoxin: ≤1EU/mg
Applications
Suitable for use in ELISA. Other applications not tested.
Recommended Dilutions
Optimal dilutions to be determined by the researcher.
Storage and Stability
Lyophilized powder may be stored at 4°C. Stable for 12 months after receipt at 4°C. Reconstitute with sterile ddH2O. Aliquot and store at 4°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
Source
Normal hman serum
Purity
≥98% by SDS-PAGE
Form
Supplied as a dark red, lyophilized powder from Ammonium bicarbonate. Reconstitute in ddH2O.
Important Note
This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications without the expressed written authorization of United States Biological.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

References
1. Human Holo transferrin, holotransferrin study: Intact human holo-transferrin interaction with oxaliplatin. Human holo Transferrin REF: Rapid Communications in Mass Spectrometry Volume 19,Issue 14,Pages 1956-1962/holo/human/Transferrin. 2. Human Holo transferrin, holo transferrin article: The Cytoplasmic Domain of Transferrin Receptor 2 Dictates Its Stability and Response to human Holo-transferrin in Hep3B Cells. Human holo Transferrin REF: J. Biol. Chem., Vol. 282, Issue 9, 6201-6209, March 2, 2007/holo/human/Transferrin. 3. Human transferrin research: Serum Transferrin Receptor Concentrations during Normal Pregnancy. Human Transferrin REF: Clinical Chemistry 46: 725-727, 2000. 4. Human Holo transferrin, holotransferrin study: Circulating Soluble Transferrin Receptor According to Glucose Tolerance Status and Insulin Sensitivity. Human Transferrin REF: Diabetes Care 30:604-608, 2007/holo/human/Transferrin. 5. Human Holo transferrin and apo transferrin study: A structural comparison of human serum transferrin and human lactoferrin. Human holo Transferrin REF:Biometals. 2007 Jan 11|Human holo transferrin and apo transferrin study: Quercetin-induced Conformational Change of Human Serum Transferrin. Human Transferrin REF: Chemistry Letters Vol. 36 (2007) , No. 1 p.84 /holo/human//Transferrin. 6. Human Holo transferrin, holotransferrin study: Decreased transferrin receptor expression by neuromelanin cells in restless legs syndrome. Human holo Transferrin REf: NEUROLOGY 2004;62:1563-1567 7. Human Holo transferrin, research: Effects of artemisinin-tagged holotransferrin on cancer cells. Human holo transferrin REF:Life Sciences, Volume 76, Issue 11, 28 January 2005, Pages 1267-1279 8. Human holo transferrin article: The growth inhibition exhibited by the feoB mutant in Fe-deficient media was relieved by human holo-transferrin, human holo-lactoferrin and Fe3+-dicitrate, but not by FeSO4. Human holo Transferrin REF:Molecular Microbiology Volume 37 Issue 2 Page 274,July 2000. 9. Human holo transferrin research: Iron absorption and cellular transport. This study postulates that the basolateral membranes of absorptive cells possess both human holo-transferrin and human apotransferrin receptors that regulate the ingress and egress of cellular iron. Human holo Transferrin REF: Semin Hematol. 1998 Jan;35(1):13-2610. Human Holo Transferrin research: Human Apo transferrin and Human holotransferrin(holo transferrin) undergo different endocytic cycles in intestinal epithelia (Caco-2) cells. Human holo Transferrin REF:J Biol Chem. 1997 Aug 1;272(31):19425 11. Human transferrin Research: The C2 variant of human serum transferrin retains the iron binding properties of the native protein. Human transferrin REF: Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, Volume 1741, Issue 3, 25 September 2005, Pages 264-270 12. Human holo transferrin research: Relationship Between Transferrin-Iron Saturation, Alcohol Consumption, and the Incidence of Cirrhosis and Liver Cancer. Human holo transferrin REF: Clinical Gastroenterology and Hepatology, Volume 5, Issue 5, May 2007, Pages 624-629. 13. Human holo tranferrin research: Aluminum stimulates uptake of non-transferrin bound iron and transferrin bound iron in human glial cells. Human holo transferrin REF: Toxicology and Applied Pharmacology, Volume 220, Issue 3, 1 May 2007, Pages 349-356
USBio References
No references available
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