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Datasheet
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蛋白及NCBI編號(hào)： |
NM_001963.6 |
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宿主： |
E.coli | ||
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表達(dá)區(qū)域： |
Asn971-Arg1023 |
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蛋白長(zhǎng)度： |
174aa（含標(biāo)簽） |
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蛋白序列： |
NSDSECPLSHDGYCLHDGVCMYIEALDKYACNCVVGYIGER CQYRDLKWWELR |
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分子量： |
蛋白由174個(gè)氨基酸組成（含融合標(biāo)簽），預(yù)測(cè)分子量為19.9kDa，實(shí)際分子量約為21kDa。 |
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融合標(biāo)簽： |
6xHis-SUMO（N端） |
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純度： |
≥95% 蛋白電泳 | ||
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物理性狀： |
液態(tài)或凍干粉 | ||
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組分： |
0.01M PBS+20%甘油，溶液無(wú)菌 | ||
| 穩(wěn)定性： 分裝后樣品在-20℃至-80℃下的穩(wěn)定性可達(dá)6個(gè)月，避免反復(fù)凍融 | |||
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應(yīng)用： 抗體制備，免疫實(shí)驗(yàn)（ELISA，WB），亞細(xì)胞定位和互作蛋白鑒定等。 |
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內(nèi)毒素： < 0.1 EU per ug of the protein as determined by the LAL method |
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別名
Pro-epidermal growth factor; EGF.
背景
人表皮生長(zhǎng)因子（EGF）是6-kDa的蛋白質(zhì)，具有53個(gè)氨基酸殘基和三個(gè)分子內(nèi)二硫鍵，通過(guò)與細(xì)胞表面的同源受體EGFR結(jié)合，可以刺激細(xì)胞生長(zhǎng)、分化和存活。EGF在體內(nèi)和體外刺激各種表皮和上皮組織的生長(zhǎng)，在細(xì)胞培養(yǎng)中刺激一些成纖維細(xì)胞的生長(zhǎng)。這刺激配體誘導(dǎo)的二聚化，激活受體的固有蛋白酪氨酸激酶活性。
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2. Harris RC, et al. EGF receptor ligands, Experimental Cell Research. 284 (1): 2–13.
3. Custo, S, et al. A comparative profile of total protein and six angiogenically-active growth factors in three platelet products. GMS Interdisciplinary Plastic and Reconstructive Surgery DGPW. 11 (Doc06): Doc06.
4. Venturi S, Venturi M (2009). Iodine in evolution of salivary glands and in oral health. Nutrition and Health. 20 (2): 119–34.
5. Hollenberg MD, Gregory H (May 1980). Epidermal growth factor-urogastrone: biological activity and receptor binding of derivatives. Molecular Pharmacology. 17 (3): 314–20.
6. Herbst RS (2004). Review of epidermal growth factor receptor biology. International Journal of Radiation Oncology, Biology, Physics. 59 (2 Suppl): 21–6.
7. Kumar V, et al. Robbins and Cotran pathologic basis of disease (7th ed.). St. Louis, Mo: Elsevier Saunders. ISBN 978-0-7216-0187-8.
8. Chao J (2013-01-01), Rawlings ND, Salvesen G (eds.), Chapter 624 - Mouse Kallikrein 9, Epidermal Growth Factor-binding Protein, Handbook of Proteolytic Enzymes (Third ed.), Academic Press, pp. 2830–2831
9. Dawson JP, et al. Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface. Molecular and Cellular Biology. 25 (17): 7734–42.
10. Fallon JH, et al. Epidermal growth factor immunoreactive material in the central nervous system: location and development. Science. 224 (4653): 1107–9
11. Carpenter G, et al. Epidermal growth factor. The Journal of Biological Chemistry. 265 (14): 7709–12
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