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- 详细信息
- 文献和实验
- 技术资料
- 保存条件:
-20℃ to -80℃
- 保质期:
12个月
- 英文名:
Recombinant Human FGFR4 / FGF Receptor 4 Protein (His Tag)
- 库存:
99
- 供应商:
北京义翘神州科技股份有限公司
- 规格:
1.00 mg/50.00 µg/100.00 µg
| 规格: | 1.00 mg | 产品价格: | ¥21030.0 |
|---|---|---|---|
| 规格: | 50.00 µg | 产品价格: | ¥2570.0 |
| 规格: | 100.00 µg | 产品价格: | ¥4520.0 |
蛋白名称:Human FGFR4 / FGF Receptor 4 Protein (His Tag)
蛋白构建:A DNA sequence encoding the extracellular domain (Met 1-Asp 369) of human FGFR4 (NP_002002.3) was fused with a polyhistidine tag at the C-terminus.
表达宿主:HEK293 Cells
蛋白纯度:> 90 % as determined by SDS-PAGE
蛋白活性:Measured by its ability to inhibit FGF acidic (aFGF / FGF1) dependent proliferation of Balb/c3T3 mouse embryonic fibroblasts. The ED50 for this effect is typically 0.2-1μg/mL.
蛋白内毒素:< 1.0 EU per μg of the protein as determined by the LAL method
预测N端:Leu 22
蛋白分子量:The secreted recombinant human FGFR4 consists of 359 amino acids and has a predicted molecular mass of 40 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rh FGFR4 is approximately 60 kDa due to glycosylation.
蛋白NP号:NP_002002.3
蛋白氨基酸序列:Met1-Asp369
蛋白标签:C-His
蛋白保存条件:Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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文献和实验浅析染色质免疫沉淀(ChIP)技术在 DNA 与蛋白质相互作用研究中的重要性
, D.C., et al., Genomic studies with Escherichia coli MelR protein: applications of chromatin immunoprecipitation and microarrays. J Bacteriol, 2004. 186(20): p. 6938-43. [5] Wu, C.H., et al., Combined analysis of murine and human microarrays and ChIP
Identifying Protein Interactions by Hydroxyl‐Radical Protein Footprinting
Basic Protocol 1: Generation of an Active Recombinant Protein That is End‐Labeled Basic Protocol 2: Hydroxyl Radical Cleavage of Protein in Absence and Presence of Ligand Basic Protocol 3: Analyze Gel
Site‐Specific Protein Labeling with SNAP‐Tags
with time‐resolved FRET and snap‐tag technologies: Application to G protein‐coupled receptor oligomerization. Methods Mol. Biol. 756:201–214. Eyster, C.A., Higginson, J.D
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