GLPBio

transferrin fragment

Catalog No.: GP10064Purity:>99.00%Synonyms: H2N-Ala-Asp-Arg-Asp-Gln-Tyr-Glu-Leu-Leu-Cys-Leu-Asp-Asn-Thr-Arg-OH

Products are for research use only. Not for human use. We do not sell to patients.


transferrin fragment
1mgIn Stock
$60.00
1
5mgIn Stock
$180.00
1
10mgIn Stock
$300.00
1
25mgIn Stock
$420.00
1

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Description

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 properties 4, 5. Sequence homology between the lobes6 and internal homology in organization of the transferrin gene7 establish 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

Product Documents

Purity:>99.00%Appearance:A solid

Chemical Properties

Synonyms
H2N-Ala-Asp-Arg-Asp-Gln-Tyr-Glu-Leu-Leu-Cys-Leu-Asp-Asn-Thr-Arg-OH
SMILES
NC(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
Molecular Formula
C75H121N23O28S
Molecular Weight
1824.97
Solubility
≥182.4mg/mL in DMSO
Storage
Store at -20°C
General tips
Select a suitable solvent according to the product solubility data. Once prepared, aliquot the stock solution to avoid repeated freeze-thaw cycles.
Use stock solutions within 6 months when stored at -80°C or within 1 month when stored at -20°C.
To improve solubility, warm the tube to 37°C and sonicate it for an appropriate period.
Shipping Condition
Evaluation samples are shipped with blue ice. Other available sizes are shipped at room temperature or with blue ice upon request.

CalculatorsMolarity / Dilution / Molecular Weight / Unit Conversion / In Vivo Formulation / Solubility

g/mol

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