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Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)
Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)
- 中文名称:
- Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)
- 英文名称:
- Recombinant Human Epidermal Growth Factor Receptor-Sf9 (ErbB1)
- 品牌:
- AAA Biotech
- 品牌介绍:
- AAA Biotech专注于为全球生命科学研究提供高品质的蛋白质研究工具,核心产品包括经严格验证的抗体、重组蛋白及ELISA试剂盒。
- 货号:
- AAA38571
- 规格:
- 0.002 mg|0.01 mg|0.1 mg|2x0.1 mg|3x0.1 mg
- 保存建议:
- Lyophilized EGFR although stable at room temperature for 3 weeks, should be stored desiccated below -18 degree C. Upon reconstitution EGFR should be stored at 4 degree C between 2-7 days and for future use below -18 degree C.For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Please prevent freeze-thaw cycles.
- 货期:
- 6-8周
- 纯度:
- Greater than 90.0% as determined by SDS-PAGE.
- 产品形式:
- ErbB1 was lyophilized from a concentrated (1mg/ml) sterile solution containing 1x PBS pH-7.4.
Sterile Filtered White lyophilized (freeze-dried) powder.
- 免责声明:
- *本产品仅供科研实验使用,不得用于临床诊断。*
- 说明书:
Description: The EGFR contains the extracellular domain of the human EGFR (25-647 a.a.) excluding the signal peptide which is cleaved by the insect cells having an approximate Mw of 85kDa. The EGFR is fused to a C-terminal Strep-tag and purified by proprietary chromatographic techniques.
Introduction: The epidermal growth factor receptor (EGF R) subfamily of receptor tyrosine kinases comprises four members: EGF R (also known as HER1, ErbB1 or ErbB), ErbB2 (Neu, HER-2), ErbB3 (HER-3), and ErbB4 (HER-4). All family members are type I transmembrane glycoprotein that has an extracellular domain which contains two cysteine-rich domains separated by a spacer region that is involved in ligand-binding, and a cytoplasmic domain which has a membrane-proximal tyrosine kinase domain and a C-terminal tail with multiple tyrosine autophosphorylation sites. The human EGF R gene encodes a 1210 amino acid (aa) residue precursor with a 24 aa putative signal peptide, a 621 aa extracellular domain, a 23 aa transmembrane domain, and a 542 aa cytoplasmic domain. EGF R has been shown to bind a subset of the EGF family ligands, including EGF, amphiregulin, TGF-?, betacellulin, epiregulin, heparin-binding EGF and neuregulin-2 in the absence of a co-receptor. Ligand binding induces EGF R homodimerization as well as heterdimerization with ErbB2, resulting in kinase activation, tyrosine phosphorylation and cell signaling. EGF R can also be recruited to form heterodimers with the ligand-activated ErbB3 or ErbB4. EGF R signaling has been shown to regulate multiple biological functions including cell proliferation, differentiation, motility and apoptosis. In addition, EGF R signaling has also been shown to play a role in carcinogenesis.