

Supplier:
Boster ImmunoleaderCat no: RP1022
Polyclonal Anti-human Transferrin
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SPECIFICATIONS
Price
240.00 USD
Catalog Number
RP1022
Size
100ug/vial
Applications
ELISA, IHC, WB
Reactivities
Hum
Form
Lyophilized
Format
Each vial contains 0.9mg NaCl, 0.2mg Na2HPO4, 0.05mg NaN3.
Gene Id
TF
References
1. Asada-Senju, M., Maeda, T., Sakata, T., Hayashi, A., Suzuki, T.Molecular analysis of the transferrin gene in a patient with hereditary hypotransferrinemia.J. Hum. Genet. 47: 355-359, 2002.\n2. Delanghe, J., Verstraelen, H., Pynaert, I., Debels, L., Taes, Y., Verhasselt, B., De Henauw, S., Temmerman, M.Human transferrin G277S mutation and iron deficiency in pregnancy. (Letter)Brit. J. Haemat. 132: 249-250, 2005.\n3. Pang, H., Koda, Y., Soejima, M., Kimura, H.Identification of a mutation (A1879G) of transferrin from cDNA prepared from peripheral blood cells.Ann. Hum. Genet. 62: 271-274, 1998.
Swiss Prot
P02787
Storage Temp
\"At -20 degree C for one year. After reconstitution, at 4 degree C for one month. It can also be aliquotted and stored frozen at -20 degree C for a longer time.\nAvoid repeated freezing and thawing. \n\"\n
Additional Info
Oryza sativa-derived human Transferrin recombinant protein (Position: V20-P698).
Scientific Background
Transferrins are iron-binding blood plasma glycoproteins that control the level of free iron in biological fluids. In humans, it is encoded by the TF gene. In humans, transferrin consists of a polypeptide chain containing 679 amino acids. The protein is composed of alpha helices and beta sheets to form two domains. The N- and C- terminal sequences are represented by globular lobes and between the two lobes is an iron-binding site. Transferrin is a glycoprotein that binds iron very tightly but reversibly. 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). Transferrin has a molecular weight of around 80 kDa and contains 2 specific high-affinity Fe(III) binding sites. 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.
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