Best video so far on this topic. I am Not even a biology or biochem major or any clinical sciences for that matter. Yet, I understood perfectly. Thumbs up and thank you
Your videos are of great help! I have been using them since my first year of university, and now I am in my final 3rd year. They are clear and logically structured to communicate information in an easily understandable way - Thank you for your videos!
Great video! Helps me a lot to understand (Co)Immunoprecipitation. I would like to know more how to analyze the Protein afterwards or how to make the Protein-Protein-Interaktion visible, preferably without the use of fluorescence. Maybe you do have a video on that to?
can you explain what those tables that have the dark bands mean. Every video is about explaining how to do the process, what about the results?? how do we know what's going on in the results??
Hi Rishan. I know a few technique needs to be followed after immunoprecipitation to obtain the results. They are direct and indirect techniques. First, is an indirect technique called SDS-Gel Electroporesis (SDS-PAGE). Namely, the technique describes to have protein solutions to compete inside a gel which have micro diameter pores. The manner of the competition is relied on the length of amino acid sequences of proteins. The dissimilarities occurs when the gel is under a electric current, after submerging in a solution which has conductive ions and salts (and pH). The pore diameter is optimized for proteins to move inside the gel neither freely nor difficultly. Finally, you conduct and compare A and AB and ACD solutions under SDS-PAGE and make proteins visible with various dyes or protein-binding metal ions. The disadvantage of the technique is that you cause both all bounds to unbound and proteins to denature to linear forms. Second, is a direct technique called immuno-fluorescence, is a rather very expensive technique to consider using extra antibodies(AB). That is to say, you mark A and B proteins with a series of another fluorescence bounded antibodies. You can see the difference with directing different fluorescence markers to your preferred ABs. Unsurprisingly, to illustrate with a scenario, sole A will marked with RED, sole B will marked with BLUE, you will see AB together in GREEN which is the visual interference of red and blue. All other techniques that I know are developed from these two basic techniques. if you interest in more details you can find a lot more details by keywords. And beware, there are a lot of interpretations using antibodies. For example, affinity chromotography is my hero by means of its power to scan a huge amount of binding candidates.
Thanks man, really appreciate you trying to help but I guess you didn't really get what I am asking for (maybe it's because I don't know how to present the question) but I am still in the dark about what I needed to know. :(
Rishan Rangslang Hey it was pleasure :) Don't you ever get frustrated when you don't understand something. I believe you have good questions, you will really know it after you learn it. I hate to say "others", but others will memorize it, you will know it. Try to materialize your question again.
Do you want to know what those boxes stand for? They represent any experiment tube, and the upper lines represent the volume consists of aqueous solutions. They differ in ionic content and in pH. If we need proteins to protect their tertiary forms, we use physiological pH 7.4 but if we need primary, linear forms we rather use acidic pH ~3.
btw this is the article I am talking about: www.nature.com/nature/journal/v520/n7548/full/nature14147.html I just want to know if anyone can like tell me what i need to do to understand and be able to interpret the results of the experiments carried out in the research paper mentioned above. is there a specific book or is there a link on the internet or maybe a video would be very helpful.
Best video so far on this topic. I am Not even a biology or biochem major or any clinical sciences for that matter. Yet, I understood perfectly. Thumbs up and thank you
Your videos are of great help! I have been using them since my first year of university, and now I am in my final 3rd year. They are clear and logically structured to communicate information in an easily understandable way - Thank you for your videos!
Wow I just discovered your channel, man you deserve to have millions of followers, thank you so much for your work!
so now how do I analyze the information in a research paper. Any videos available?
Great video! Helps me a lot to understand (Co)Immunoprecipitation. I would like to know more how to analyze the Protein afterwards or how to make the Protein-Protein-Interaktion visible, preferably without the use of fluorescence. Maybe you do have a video on that to?
Thank you so much for this video. Really very helpful. Can you do a video on Chromatin Immunoprecipitation and RNA Immunoprecipitation please.
you saved my life
very educating lecture.
can you explain what those tables that have the dark bands mean. Every video is about explaining how to do the process, what about the results?? how do we know what's going on in the results??
Hi Rishan. I know a few technique needs to be followed after immunoprecipitation to obtain the results. They are direct and indirect techniques.
First, is an indirect technique called SDS-Gel Electroporesis (SDS-PAGE). Namely, the technique describes to have protein solutions to compete inside a gel which have micro diameter pores. The manner of the competition is relied on the length of amino acid sequences of proteins. The dissimilarities occurs when the gel is under a electric current, after submerging in a solution which has conductive ions and salts (and pH). The pore diameter is optimized for proteins to move inside the gel neither freely nor difficultly. Finally, you conduct and compare A and AB and ACD solutions under SDS-PAGE and make proteins visible with various dyes or protein-binding metal ions. The disadvantage of the technique is that you cause both all bounds to unbound and proteins to denature to linear forms.
Second, is a direct technique called immuno-fluorescence, is a rather very expensive technique to consider using extra antibodies(AB). That is to say, you mark A and B proteins with a series of another fluorescence bounded antibodies. You can see the difference with directing different fluorescence markers to your preferred ABs. Unsurprisingly, to illustrate with a scenario, sole A will marked with RED, sole B will marked with BLUE, you will see AB together in GREEN which is the visual interference of red and blue.
All other techniques that I know are developed from these two basic techniques. if you interest in more details you can find a lot more details by keywords. And beware, there are a lot of interpretations using antibodies. For example, affinity chromotography is my hero by means of its power to scan a huge amount of binding candidates.
Thanks man, really appreciate you trying to help but I guess you didn't really get what I am asking for (maybe it's because I don't know how to present the question) but I am still in the dark about what I needed to know. :(
Rishan Rangslang Hey it was pleasure :) Don't you ever get frustrated when you don't understand something. I believe you have good questions, you will really know it after you learn it. I hate to say "others", but others will memorize it, you will know it.
Try to materialize your question again.
Do you want to know what those boxes stand for? They represent any experiment tube, and the upper lines represent the volume consists of aqueous solutions. They differ in ionic content and in pH. If we need proteins to protect their tertiary forms, we use physiological pH 7.4 but if we need primary, linear forms we rather use acidic pH ~3.
btw this is the article I am talking about:
www.nature.com/nature/journal/v520/n7548/full/nature14147.html
I just want to know if anyone can like tell me what i need to do to understand and be able to interpret the results of the experiments carried out in the research paper mentioned above. is there a specific book or is there a link on the internet or maybe a video would be very helpful.
WLH MVP !
Get to the point more quickly, please