| 货号 (SKU) | 包装规格 | 是否现货 | 价格 | 数量 |
|---|---|---|---|---|
| rp170191-10μg |
10μg |
期货  |
| |
| rp170191-20μg |
20μg |
现货 |
|
| 产品名称 | Recombinant Human EGF Protein (Biotin) |
|---|---|
| 别名 | 重组人表皮生长因子蛋白(EGF) | 重组人 EGF 蛋白(生物素) |
| 英文别名 | beta-urogastrone | EGF | epidermal growth factor (beta-urogastrone) | epidermal growth factor | hEGF | HOMG4 | pro-epidermal growth factor | URG | Urogastrone | EGF |
| 规格或纯度 | ActiBioPure™, 无叠氮钠, 生物活性 |
| 产品介绍 |
Introduction: |
| 生物活性 | Binding EGFR |
| 表达系统 | 毕赤酵母 |
| 种属 | 人(Human) |
| 氨基酸 | 971 - 1021 aa |
| 序列 | NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGERCQYRDLKWWE |
| 蛋白标签 | No tag |
| 蛋白长度 | Full length protein |
| 无载体 | No |
| 偶联 | Biotin |
| Accession # | P01133 |
| 来源 | 重组表达 |
| 应用 | Flow,IF |
|---|---|
| 物理形态 | 冻干(Lyophilized) |
| 储存缓冲液 | Lyophilized from PBS (pH 7.4) buffer containing 1% BSA |
| 防腐剂 | No |
| 复溶 | This product should be reconstituted in 100μL of deionized water to make a 0.2mg/mL stock solution. Prepare working dilution on day of use. Stock solution is stable for about 8 weeks at 2-8°C as an undiluted liquid. Avoid freeze-thaw cycles. Protect from light. |
| 储存温度 | 2-8°C储存,避光 |
| 运输条件 | 冰袋运输 |
| 稳定性与储存 | 冻干产品在使用前应保存在 -20°C 温度下。打开前，应使产品温热至室温。避免光照。如储存得当，产品至少可稳定保存 12 个月。 |
| 分子类型 | 蛋白质 |
Recombinant Human EGF Protein (Biotin) (rp170191) - Flow Cytometry
Flow analysis of EGF receptors (red line) in A431 Cells. Cells were labeled with Recombinant Human EGF Protein (Biotin) (rp170191) at 1/2500 dilution for 1 hour at 4°C, and then incubated with Streptavidin protein (APC) (np169048) at a dilution of 1/400 for 30 minutes at 4°C in the dark. Unlabeled Cells (black line) were used as a negative control.
通过匹配包装上的批号来查找并下载产品的 COA，每批产品都进行了严格的验证，您可放心使用！
| 批号(Lot Number) | 证书类型 | 货号 |
|---|---|---|
 ZJ23F0700645 |
分析证书 | rp170191 |
¥499.90
¥339.90
¥3,999.90
¥339.90
| 1. Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M et al.. (2002) Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.. Cell, 110 (6): (775-87). [PMID:12297050] |
| 2. Lesuisse D, Mauger J, Nemecek C, Maignan S, Boiziau J, Harlow G, Hittinger A, Ruf S, Strobel H, Nair A, Ritter K, Malleron JL, Dagallier A, El-Ahmad Y, Guilloteau JP, Guizani H, Bouchard H, Venot C.. (2011) Discovery of the first non-ATP competitive IGF-1R kinase inhibitors: advantages in comparison with competitive inhibitors.. Bioorg Med Chem Lett, 21 (8): (2224-2228). [PMID:21441024] [10.1016/j.bmcl.2011.03.003] |
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| 4. Hommel, U U, Harvey, T S TS, Driscoll, P C PC and Campbell, I D ID.. (1992) Human epidermal growth factor. High resolution solution structure and comparison with human transforming growth factor alpha.. Journal of molecular biology, (5): [PMID:1522591] |
| 5. Furuya, M M, Akashi, S S and Hirayama, K K.. (1989) The primary structure of human EGF produced by genetic engineering, studied by high-performance tandem mass spectrometry.. Biochemical and biophysical research communications, (15): [PMID:2789514] |
| 6. Bell, G I GI and 8 more authors.. (1986) Human epidermal growth factor precursor: cDNA sequence, expression in vitro and gene organization.. Nucleic acids research, (11): [PMID:3491360] |
| 7. Lu, H S HS and 5 more authors.. (2001) Crystal structure of human epidermal growth factor and its dimerization.. The Journal of biological chemistry, (14): [PMID:11438527] |
| 8. Ferguson, Kathryn M KM and 5 more authors.. (2003) EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.. Molecular cell, [PMID:12620237] |
| 9. Groenestege, Wouter M Tiel WM and 10 more authors.. (2007) Impaired basolateral sorting of pro-EGF causes isolated recessive renal hypomagnesemia.. The Journal of clinical investigation, [PMID:17671655] |
| 10. Lu, Chafen C and 6 more authors.. (2010) Structural evidence for loose linkage between ligand binding and kinase activation in the epidermal growth factor receptor.. Molecular and cellular biology, [PMID:20837704] |
| 11. Huang, Hsiao-Wen HW, Mohan, Sepuru K SK and Yu, C C.. (2010) The NMR solution structure of human epidermal growth factor (hEGF) at physiological pH and its interactions with suramin.. Biochemical and biophysical research communications, (26): [PMID:21029725] |
| 12. Zettl, Markus M, Adrain, Colin C, Strisovsky, Kvido K, Lastun, Viorica V and Freeman, Matthew M.. (2011) Rhomboid family pseudoproteases use the ER quality control machinery to regulate intercellular signaling.. Cell, (1): [PMID:21439629] |
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