transferrin fragment
(Synonyms: H2N-Ala-Asp-Arg-Asp-Gln-Tyr-Glu-Leu-Leu-Cys-Leu-Asp-Asn-Thr-Arg-OH ) 目录号 : GP10064
转铁蛋白片段
Sample solution is provided at 25 µL, 10mM.
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Quality Control & SDS
- View current batch:
- Purity: >99.00%
- COA (Certificate Of Analysis)
- SDS (Safety Data Sheet)
- Datasheet
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
| Cas No. | SDF | ||
| 别名 | H2N-Ala-Asp-Arg-Asp-Gln-Tyr-Glu-Leu-Leu-Cys-Leu-Asp-Asn-Thr-Arg-OH | ||
| Canonical 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 | ||
| 分子式 | C75H121N23O28S | 分子量 | 1824.97 |
| 溶解度 | ≥ 182.4mg/mL in DMSO | 储存条件 | Store at -20°C |
| General tips | 请根据产品在不同溶剂中的溶解度选择合适的溶剂配制储备液；一旦配成溶液，请分装保存，避免反复冻融造成的产品失效。 储备液的保存方式和期限：-80°C 储存时，请在 6 个月内使用，-20°C 储存时，请在 1 个月内使用。 为了提高溶解度，请将管子加热至37℃，然后在超声波浴中震荡一段时间。 |
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| Shipping Condition | 评估样品解决方案：配备蓝冰进行发货。所有其他可用尺寸：配备RT，或根据请求配备蓝冰。 | ||
| 制备储备液 | |||
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1 mg | 5 mg | 10 mg |
| 1 mM | 0.548 mL | 2.7398 mL | 5.4795 mL |
| 5 mM | 0.1096 mL | 0.548 mL | 1.0959 mL |
| 10 mM | 0.0548 mL | 0.274 mL | 0.548 mL |
| 第一步：请输入基本实验信息（考虑到实验过程中的损耗，建议多配一只动物的药量） | ||||||||||
| 给药剂量 | mg/kg |  |
动物平均体重 | g | |
每只动物给药体积 | ul | |
动物数量 | 只 |
| 第二步：请输入动物体内配方组成（配方适用于不溶于水的药物；不同批次药物配方比例不同，请联系GLPBIO为您提供正确的澄清溶液配方） | ||||||||||
| % DMSO % % Tween 80 % saline | ||||||||||
| 计算重置 | ||||||||||
计算结果:
工作液浓度： mg/ml；
DMSO母液配制方法： mg 药物溶于 μL DMSO溶液（母液浓度 mg/mL，
体内配方配制方法：取 μL DMSO母液，加入 μL PEG300，混匀澄清后加入μL Tween 80，混匀澄清后加入 μL saline，混匀澄清。
1. 首先保证母液是澄清的；
2.
一定要按照顺序依次将溶剂加入，进行下一步操作之前必须保证上一步操作得到的是澄清的溶液，可采用涡旋、超声或水浴加热等物理方法助溶。
3. 以上所有助溶剂都可在 GlpBio 网站选购。