Photoreceptors and Image ProcESsing Part 1B - Jeremy Nathans
本视频由科普中国和生物医学大讲堂出品
Jeremy Nathans (Johns Hopkins) Part 1B: Photoreceptors and Image ProcESsing
In this set of lecturES, Jeremy Nathans explorES the molecular mechanisms within the retina that mediate the first steps in vision. The first lecture focusES on the structure of the light sensing receptors, the intracellular signals that are triggered by light absorption, and the ways in which the retina extracts information from a complex scene. See more at http://www.ibioseminars.org
GE：WEStern blot 整体解决方案—— Amersham WB与您携手实现完美WB
重复性差、实验周期长、过程繁琐——作为一种最常见蛋白质分析技术，wEStern blot 在您心中的印象是否依旧如此？wEStern blot技术于1981年被发明，时至今日，您是否想要了解一下这项技术的最新进展呢？GE公司倾情推出AWB一体化免疫印迹系统，最快4小时完成实验，采用双通道荧光标记技术，并引入总蛋白归一化功能，标准化、自动化流程专注决重复性难题，为您的蛋白质研究保驾护航。
GE：创新解决方案4小时完成wEStern-blot
WEStern blot蛋白免疫印迹技术是分子生物学研究的经典研究手段之一，约60％的科学期刊出版物包含WB实验结果。但WB实验步骤多，耗时长，要获得一个完美的结果十分不易，WB实验结果的不稳定，重复不出来？定量不准确？凝胶又漏了？
GE公司最新推出的Amersham WB系统，4小时内可完成电泳、转印、杂交、孵育、成像、定量分析，一气呵成，为WEStern blot提供了整体解决方案。每个样品、每一次实验都能获得一致的定量数据。再也无需担心结果难以重复再现，无需反复摸索实验条件！
Stability of Morphogen Gradients & Movement of MoleculES
In my second lecture I dEScribe experiments using EGFP tagged Bicoid to follow Bcd gradient EStablishment in living embryos, and to tESt various aspects of the simple model. DESpite continuous synthESis of new Bcd protein at the anterior end of the egg, we find that the concentration of Bcd in nuclei at any given point along the anterior posterior axis is constant over time and is reproducible from embryo to the next. This reproducibility means that the gradient is sufficiently robust to provide positional information and thus can accurately direct gene activitiES. One the other hand, quantitative imaging experiments point to several featurES of the gradient that are hard to explain - how target genES activated by Bcd distinguish relatively subtle differencES in low concentrations, and how Bcd moleculES move from the anterior site of their synthESis to the site of their transcriptional activity. See more at http://www.ibioseminars.org
Protein synthESis: a high fidelity molecular event
Rachel Green (Johns Hopkins U., HHMI) 1: Protein synthESis: a high fidelity molecular event
Talk Overview:
In her first talk, Green providES a detailed look at protein synthESis, or translation. Translation is the procESs by which nucleotidES, the “language” of DNA and RNA, are translated into amino acids, the “language” of proteins. Green begins by dEScribing the components needed for translation; mRNA, tRNA, ribosomES, and the initiation, elongation, and termination factors. She then explains the rolES of thESe players in ensuring accuracy during the initiation, elongation, termination and recycling steps of the translation procESs. By comparing translation in bacteria and eukaryotES, Green explains that it is possible to determine which components and steps are highly conserved and predate the divergence of different kingdoms on the tree of life, and which are more recent adaptations.
Green’s second talk focusES on work from her lab invEStigating how ribosomES detect defective mRNAs and trigger events leading to the degradation of the bad RNA and the incompletely translated protein product and to the recycling of the ribosome components. Working in yeast and using a number of biochemical and genetic techniquES, Green’s lab showed that the protein Dom34 is critical for facilitating ribosome release from the short mRNAs that rESult from mRNA cleavage. Experiments showed that Dom34-mediated rEScue of ribosomES from short mRNAs is an ESsential procESs for cell survival in higher eukaryotES.
Speaker Biography:
Rachel Green received her BS in chemistry from the University of Michigan. She then moved to Harvard to pursue her PhD in the lab of Jack Szostak where she worked on dESigning catalytic RNA moleculES and invEStigating their implications for the evolution of life. As a post-doctoral fellow at the University of California, Santa Cruz, Green began to study how the ribosome translatES mRNA to protein with such accuracy.
Currently, Green is a ProfESsor of Molecular Biology and Genetics at the Johns Hopkins School of Medicine and an InvEStigator of the Howard HughES Medical Institute. RESearch in her lab continuES to focus on the ribosome and factors involved in the fidelity of eukaryotic and prokaryotic translation.
Green is the recipient of a Johns Hopkins University School of Medicine Graduate Teaching Award as well as the recipient for numerous awards for her rESearch. She was elected to the National Academy of SciencES in 2012.
Protein synthESis: mRNA surveillance by the ribosome
Rachel Green (Johns Hopkins U., HHMI) 2: Protein synthESis: mRNA surveillance by the ribosome
Talk Overview:
In her first talk, Green providES a detailed look at protein synthESis, or translation. Translation is the procESs by which nucleotidES, the “language” of DNA and RNA, are translated into amino acids, the “language” of proteins. Green begins by dEScribing the components needed for translation; mRNA, tRNA, ribosomES, and the initiation, elongation, and termination factors. She then explains the rolES of thESe players in ensuring accuracy during the initiation, elongation, termination and recycling steps of the translation procESs. By comparing translation in bacteria and eukaryotES, Green explains that it is possible to determine which components and steps are highly conserved and predate the divergence of different kingdoms on the tree of life, and which are more recent adaptations.
Green’s second talk focusES on work from her lab invEStigating how ribosomES detect defective mRNAs and trigger events leading to the degradation of the bad RNA and the incompletely translated protein product and to the recycling of the ribosome components. Working in yeast and using a number of biochemical and genetic techniquES, Green’s lab showed that the protein Dom34 is critical for facilitating ribosome release from the short mRNAs that rESult from mRNA cleavage. Experiments showed that Dom34-mediated rEScue of ribosomES from short mRNAs is an ESsential procESs for cell survival in higher eukaryotES.
Speaker Biography:
Rachel Green received her BS in chemistry from the University of Michigan. She then moved to Harvard to pursue her PhD in the lab of Jack Szostak where she worked on dESigning catalytic RNA moleculES and invEStigating their implications for the evolution of life. As a post-doctoral fellow at the University of California, Santa Cruz, Green began to study how the ribosome translatES mRNA to protein with such accuracy.
Currently, Green is a ProfESsor of Molecular Biology and Genetics at the Johns Hopkins School of Medicine and an InvEStigator of the Howard HughES Medical Institute. RESearch in her lab continuES to focus on the ribosome and factors involved in the fidelity of eukaryotic and prokaryotic translation.
Green is the recipient of a Johns Hopkins University School of Medicine Graduate Teaching Award as well as the recipient for numerous awards for her rESearch. She was elected to the National Academy of SciencES in 2012.
如何做一个完美的WEStern Blot检测
In the wEStern blot visual protocol video, you will learn how to prepare your samplES before loading them into a gel, load a gel and separate the proteins through electrophorESis, transfer your proteins from the SDS-PAGE gel onto a PVDF or nitrocellulose membrane, block the membrane, stain in Ponceau red, add the primary and secondary antibodiES, and visualize your protein of interESt. Additional help can be found in the support section of http://www.novusbio.com, through our live chat service, or by calling us directly to talk with our elite customer and technical service scientists.
WEStern Blot 第1阶段：样品制备
Novus Biologicals Visual Protocols: In phase 1 of the wEStern blot procedure, you will learn how to prepare your samplES before loading them into a gel. Here we isolate protein from cultured cells, quantify total protein concentrations with a BCA assay, add loading buffer to the sample, and heat the sample. Additional help can be found in the support section of http://www.novusbio.com, through our live chat service, or by calling us directly to talk with our elite customer and technical service scientists.
WEStern Blot 第2阶段：蛋白电泳(SDS-PAGE)
Novus Biologicals Visual Protocols: In phase 2 of the wEStern blot procedure, you will learn how to load a gel and separate the proteins through electrophorESis, based upon protein weight. Additional help can be found in the support section of http://www.novusbio.com, through our live chat service, or by calling us directly to talk with our elite customer and technical service scientists.
WEStern Blot 第3阶段：膜转移
Novus Biologicals Visual Protocols: In phase 3 of the wEStern blot procedure, you will learn how to transfer your proteins from the SDS-PAGE gel onto a PVDF or nitrocellulose membrane. Here we remove the gel from the cassette, and stack it in a sandwich comprised of a sponge, filter paper, the gel, membrane, filter paper, and sponge. The negatively charged proteins will then transfer onto the membrane toward the positive current. Additional help can be found in the support section of http://www.novusbio.com, through our live chat service, or by calling us directly to talk with our elite customer and technical service scientists.