Haha thank you ... maybe you can recommend it to your colleagues ;)

throw that ish on Rap Chat yo, that would be FIRE!

your professor probs done thousands of 'gels' while doing his first research work. I m assuming he's just not interested any more:-))

this is why professors should do research and teachers should teach. not always the case; some professors are excellent, lively, dynamic and patient teachers also ...but most just want to get back to overseeing their projects, publishing papers and finishing grant applications before the dreaded deadlines.

Hehe

yup, stay tuned for more videos :)

Hello, thank you for your comment ... happy you got what you need from the video :)

Biomedical and Biological Sciences yes i actually have an exam about all those technics soon and you saved my life haha !

Wow, this is good ... I have a playlist on my channel containing videos about all the electrophoresis techniques, have a look at it, it will help you for your exam: kzfaq.info/get/bejne/hdSPjdKlycDJqH0.html

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Thank you for your comment ... I will ... Stay tuned :)

True

the same to you

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You are welcome :D

HAHAHA this is normal ... Sometimes we do things without going into the details ... stay tuned in the channel so you can see all the new videos :)

I had the same question as you, and in case you haven't found your answer yet, I found some helpful information in my lab class's Theory Manual. After the chloride anions form the leading boundary in the stacking gel, the area immediately behind is rich in Tris cations and depleted of anionic species. This attracts anionic protein molecules and causes them to migrate at a rate similar to that of the chloride anions, at least initially, and protein molecules of identical size will be concentrated into a narrow band by the time they reach the separating gel.

@@andrewfoster9823 thx sir, that really helped. however i've two questions remaining: 1) what's the purpose of the glycin when the proteins simply get draged by the Cl- front? 2) how does the glycine behind the sample manage to get past it since it's supposed to stack it before? i know that it speeds up, but that stacking-process sounds as if the glycine fraction wasn`t able to get past it because otherwise there would be no sandwitching. to me, it seems to be more logical if the faster moving thing actually has to be behind the sample in order to stack it.

@x4rrr had the same problem, now I was looking through my script again and came across the answer: Due to the fact, that the chloride-anions migrate at a very high speed through the stacking gel, behind this "layer" forms a zone with a high electrical tension (as @Andrew foster mentioned above, it's effected due to the positive cations of the buffer) The second quickest substance are the proteins, which are migrating through the stacking gel. Little proteins are migrating very fast, into the "positive zone" right behind the chloride anions but can't get much further at this speed, because the negative chloride is restraining them a little bit to do so (negatively charged). On the other side, very big proteins are migrating slowly. To avoid, that they don't get stuck too much, glycin pushes them through the stacking gel, so that's the positive effect of glycin. In Austria we call chloride because of that "leitionen" = leading ions, the glycine "folgeionen" = following ions. In the separation gel then glycin is overtaking the proteins, so they aren't pushed anymore and can separate slowly

@@samuelgantner4609 maybe it helped a little

Because agarose is mostly used for purification of DNA/RNA

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