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transferrin fragment
本产品不向个人销售，仅用作科学研究，不用于任何人体实验及非科研性质的动物实验。
transferrin fragment图片
包装与价格：
包装价格(元)
1mg电议
5mg电议
10mg电议
25mg电议

产品介绍

Transferrin fragment

别名H2N-Ala-Asp-Arg-Asp-Gln-Tyr-Glu-Leu-Leu-Cys-Leu-Asp-Asn-Thr-Arg-OH
Canonical SMILESNC(C)C(NC(CC(O)=O)C(NC(CCCNC(N)=N)C(NC(CC(O)=O)C(NC(CCC(N)=O)C(NC(CC1=CC=C(O)C=C1)C(NC(CCC(O)=O)C(NC(CC(C)C)C(NC(CC(C)C)C(NC(CS)C(NC(CC(C)C)C(NC(CC(O)=O)C(NC(CC(N)=O)C(NC(C(C)O)C(NC(CCCNC(N)=N)C(O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O)=O
分子式C75H121N23O28S
分子量1824.97
溶解度≥ 182.4mg/mL in DMSO
储存条件Store at -20℃
General tipsFor obtaining a higher solubility , please warm the tube at 37 ℃ and shake it in the ultrasonic bath for a while.
Shipping ConditionEvaluation sample solution : ship with blue ice
All other available size: ship with RT , or blue ice upon request
产品描述

Transferrin is the principal ironbinding protein in animal serum and is analogous in its iron-binding site and properties to lactoferrin1. Human transferrin is a single-chain glycoprotein of molecular weight near 80,000. The molecule is arranged in two lobes, each bearing a single metal-binding site. Although similar in ligand structure2, 3, the sites are distinguishable in many of their properties4, 5. Sequence homology between the lobes6and internal homology in organization of the transferrin gene7establish that the modern protein arose by duplication and fusion of a primitive gene specifying a single-sited transferrin precursor protein.

Each lobe of the transferrin molecule contains a recognition site for the chick receptor, and that both lobes are required for binding to receptor8. The receptor-binding activity of human transferrin is essentially confined to the C-terminal lobe and is preserved in the C-fragment even in the absence of the N-fragment.

References:
1.M. C. Custer And J. Norman Hansen, Lactoferrin and Transferrin Fragments React with Nitrite To Form an Inhibitor of Bacillus cereus Spore Outgrowth, Applied And Environmental Microbiology, Mar. 942-949, 1983
2.Anderson, B. F., Baker, H. M., Dodson, E. J., N o m s , G. E., Rumball, S. V., Waters, J. M., and Baker, E. N. (1987) Proc. Natl. Acad. Sei. U. S. A. 84, 1769-1773
3.Bailey, S., Evans, R. W., Garratt, R. C . , Gorinsky, B., Hasnain, S., Horsburgh, C., Jhoti, H., Lindley, P. F., Mydin, A., Sarra, R., and Watson, J. L. (1988) Biochemistry 27, 5804-5812
4.Aisen, P. (1989) in Iron Carriers and Iron Proteins (Loehr, T. M., Gray, H. B., and Lever, H. B. P., eds) pp. 353-371, VCH Publishers, Weinheim.
5.Harris, D. C., and Aisen, P. (1989) in Iron Carriers and Iron Proteins (Loehr, T. M., Gray, H. B., and Lever, A. B. P., eds) pp. 239351, VCH Publishers, Weinheim.
6.MacGillivray, R. T. A,, Mendez, E., Shewale, J. G., Sinha, S. K., Lineback-Zins, J., and Brew, K. (1983) J. Biol. Chem. 258,3543-3553
7.Park, I., Schaeffer, E., Sidoli, A,, Baralle, F. E., Cohen, G. N., and Zakin, M. M. (1985) Proc. Natl. Acad. Sci. U. S. A. 82, 3149-3153
8.Olga Zaks, Deborah ’hinder, and Philip AisenSB, Primary Receptor-Recognition Site of Human Transferrin Is in the C-terminal Lobe. The Journal of Biological Chemistry. 269: 7110-7114, 1994