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一步法完成IP | Co-IP | ChIP
lebo / 2019-06-28
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One step一步法完成IP | Co-IP | ChIP,让您的免疫沉淀更简捷,更可靠,更专业

?????????? 德国Chromotek?产品??? ? ??????????????????????????????????????????????????? —— 北京皇冠黑网不给提款|免费注册生物中国区授权代理
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GFP-Trap_A (产品货号:gta-20)
??? 产品描述: 与agarose?beads结合
??????????????????????? particle?size?~?80?μm
??? 存储缓冲液:20%?EtOH
????储存方法:室温运输,收到后4℃储存一年。请勿冰冻。

? Nano-Traps?值得信赖的科研工具???
???
?? Chromotek的Nano-Trap?基于alpaca的单域抗体片段(VHHS)
????√?小型
??? √?极端稳定
????√?70℃仍保持稳定,functional?in?2M?NaCl?or?0.5%?SDS
????√?高亲和力
????√?解离常数范围在sub-nM内
??? √?高特异性
GFP-Trap???产品特点(高稳定性、高亲和力)
????特异性结合绿色荧光蛋白的衍生物,如GFPS65T,YPF或EYFP,不与DsRed衍生蛋白结合。(见FAQs
??? √?多功能且功能强大的GFP融合蛋白生化实验
????√?缩短孵化时间(只需5-30min)
??? √?从细胞提取物或细胞器中定量分离融合蛋白及结合(暂时性)因子
??? √?超低的非特异性结合影响
??? √?无污染的普通抗体的轻链与重链
??? √?适用于染色质免疫沉淀(ChIP)
GFP-Trap???产品应用:
????√?免疫沉淀?IP?/?Co-IP
??? √?质谱分析
??? √?酶活测定
??? √?生物大分子相互作用/亲和力实验
??? √?染色质免疫沉淀(ChIP,Chromatin?Immunoprecipitation)

Nano-Traps?reliable?research?reagents
NanoTraps?are?based?on?recombinant?single?domain?antibody?fragments?(VHHS)?derived?from?
alpaca?coupled?to?monovalent?matrices?(agarose?beads,?magnetic?particles?or?multiwell?plates).
Our?GFPTrap??/?RFPTrap??are?novel?high?quality?tools?for?the?fast,?reliable?and?efficient?onestep
isolation?of?fluorescent?fusion?proteins?and?their?interacting?factors.
Features
·?Robust?and?versatile?tools?for?biochemical?analyses?of?fluorescent?fusion?proteins
·?Short?incubation?times?(5?–?30?min)
·?Quantitative?isolation?of?fusion?proteins?and?transiently?bound?factors?from?various?cell?extracts
??and?organelles?(from?all?organisms)
·?Low?unspecific?binding
·?No?unspecific?binding?or?contamination?by?heavy?and?light?chains?of?conventional?antibodies
GFP-Trap?
Our?GFP-Trap??is?a?high?quality?GFP-binding?protein?coupled?to?a?monovalent?matrix?(agarose?beads,?
magnetic?particles?or?in?96-multiwell?plates)?for?biochemical?analysis?of?GFP?fusion?proteins?and?
their?interacting?partners.?
The?GFP-Trap??specifically?binds?to?most?common?GFP?derivates?(see?FAQs?for?a?complete?list).?
No?binding?to?red?fluorescent?proteins?derived?from?DsRed?can?be?detected.
GFP-Trap??features?at?a?glance:
·?Robust?and?versatile?tool?for?biochemical?analyses?of?GFP-fusion?proteins
·?Short?incubation?times?(5?–?30?min)
·?Quantitative?isolation?of?fusion?proteins?and?transiently?bound?factors?from?cell?extracts?or?organelles
·?Low?unspecifi?c?binding
·?No?contaminating?heavy?and?light?chains?of?conventional?antibodies
·?Applicable?in?Chromatin?Immunoprecipitation?(ChIP)
Use?GFP-Trap??for:
·?Pulldowns/?Immunoprecipitations
·?Co-IP
·?Mass?spectroscopy
·?Enzyme?activity?measurements
·?ChIP?analysis
GFP-Trap_A
???? Description?
???????????GFP-Trap??coupled?to?agarose?beads
???????????particle?size?~?80?μm
???? Storage?buffer
???????????20%?EtOH
????? Storage?instructions
???????????Shipped?at?ambient?temperature.?Upon?receipt?store?at?4°C;?stable?for?one?
???????????year.?Do?not?freeze.

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Latest references

  • Castello, A. Fischer, B. Eichelbaum, K. Horos, R. Beckmann, B. Strein, C. Davey, N. Humphreys, D. Preiss, T. Steinmetz, L. Krijgsveld, J Hentze, M. (2012). Insights into RNA Biology from an Atlas of Mammalian mRNA-Binding Proteins. Cell (PubMed)
  • Ries, J. Kaplan, C. Platonova, E. Eghidi, H. Ewers, H. (2012). A simple, versatile method for GFP-base super-resolution microscopy via nanobodies. Nat. Methods. 10.1038. (PubMed)
  • Pichler, G. Jack, A. Wolf, P. Hake, S. B. (2012). Versatile Toolbox for High Throughput Biochemical and Functional Studies with Fluorescent Fusion Proteins. PLoS One. 7: e36967. (PubMed)
  • Gudesblat, G. E. Schneider-Pizon, J. Betti, C. Mayerhofer, J. Vanhoutte, I. van Dongen, W. Boeren, S. Zhiponova, M. de Vries, S. Jonak, C. Russinova, E. (2012). SPEECHLESS integrates brassinosteroid and stomata signalling pathways. Nat Cell Biol. (PubMed)
  • Majumdar, A. Cesario, W. C. White-Grindley, E. Jiang, H. Ren, F. Khan, M. R. Li, L. Choi, E. M. Kannan, K. Guo, F. Unruh, J. Slaughter, B. Si, K. (2012). Critical role of amyloid-like oligomers of Drosophila Orb2 in the persistence of memory. Cell. 148: 515-29. (PubMed)
  • Metzger, T. Gache, V. Xu, M. Cadot, B. Folker, E. S. Richardson, B. E. Gomes, E. R. Baylies, M. K. (2012). MAP and kinesin-dependent nuclear positioning is required for skeletal muscle function. Nature. (PubMed)
  • Wild, P. Farhan, H. McEwan, D. G. Wagner, S. Rogov, V. V. Brady, N. R. Richter, B. Korac, J. Waidmann, O. Choudhary, C. Dotsch, V. Bumann, D. Dikic, I. (2011). Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth. Science. 333: 228-33. (PubMed)

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