EXACTLY the video I was searching for 😍 You used the same procedure my lab professor used, but explained it 100x better. I didn't even undarstand it was a BCA test until I saw this video...
Thank you for an excellent and very detailed video. I have a question about when you mentioned extrapolating the data to work out the unknown protein concentration. Shouldn't you say interpolate instead of extrapolate as the concentration is being determined within the range of known protein concentrations from the standards based on their absorbance values and the absorbance value of the unknown protein sample? I really enjoy watching your videos.
Thank you so much for the video. Your explanation was excellent. Please, does the linear curve indicate any meaning to the experiment? How do we calculate the protein concentration using the equation of the standard curve?
Hey, thanks for that! The linear curve is of meaning to the experiment. You plot the absorbance value for each of your standard concentrations (use microsoft excel for that). If you have plotted the curve, you can see the formula of that plotted curve (you need that to calculate your sample concentration). Now, you replace "y" with the absorbance value of your sample and calculate "x". This is your sample concentration. Best, Henrik
Thanks for this informing video. I have a question. After getting the concentrations (I am getting them in ug/mL unit) should I have to divide to 20? Because I am taking 200uL from the working buffer and putting 10uL of the sample. In the end, should I divide to 20 or multiply it by 20?
If the device/program is not calculating the concentration itself, you would have to multiply by 20. But read into your device/program since many programs are calculating this already :)
Maybe a weird question but what number at the end is needed to be multiplied by 20 and why? Trying to myself understand how to get results to mg of protein.
I am doing CSF prot.conc. and it is said to be 350µg/ml (micrograms per milliliter). This standard curve do not work so I am thinking to create 800/400/200/100/50µg/mL which is 10x more sensitive. Any thoughts if this will work at all?
You just saved me from failing my lab report! thank you! I didn't grasp anything my prof was saying and this just made everything make sense
EXACTLY the video I was searching for 😍
You used the same procedure my lab professor used, but explained it 100x better. I didn't even undarstand it was a BCA test until I saw this video...
Thank you so much! I have no idea what was going on in BCA assay until I saw your video
Exactly what I was looking for, thank you so much 🙏
Amazing video 👍👍
this video literally save me ,thank u!
Amazing video 🤩 😢Very detailed clear exhaustive you have taken away all my doubts . Spectacular step by step. Thanks a lot
An excellent video, concise with relevant detail too
Thank you for an excellent and very detailed video. I have a question about when you mentioned extrapolating the data to work out the unknown protein concentration. Shouldn't you say interpolate instead of extrapolate as the concentration is being determined within the range of known protein concentrations from the standards based on their absorbance values and the absorbance value of the unknown protein sample? I really enjoy watching your videos.
Gut gemacht mann!
Very good explanation!! By the way, did you do all the animation by yourself?!!
Yes, I did
Thank you so much for the video. Your explanation was excellent.
Please, does the linear curve indicate any meaning to the experiment?
How do we calculate the protein concentration using the equation of the standard curve?
Hey, thanks for that! The linear curve is of meaning to the experiment. You plot the absorbance value for each of your standard concentrations (use microsoft excel for that). If you have plotted the curve, you can see the formula of that plotted curve (you need that to calculate your sample concentration). Now, you replace "y" with the absorbance value of your sample and calculate "x". This is your sample concentration.
Best, Henrik
Awesome man
Thanks for this informing video. I have a question. After getting the concentrations (I am getting them in ug/mL unit) should I have to divide to 20? Because I am taking 200uL from the working buffer and putting 10uL of the sample. In the end, should I divide to 20 or multiply it by 20?
If the device/program is not calculating the concentration itself, you would have to multiply by 20. But read into your device/program since many programs are calculating this already :)
Maybe a weird question but what number at the end is needed to be multiplied by 20 and why? Trying to myself understand how to get results to mg of protein.
I am doing CSF prot.conc. and it is said to be 350µg/ml (micrograms per milliliter). This standard curve do not work so I am thinking to create 800/400/200/100/50µg/mL which is 10x more sensitive. Any thoughts if this will work at all?
Can´t tell, I would suggest to try it out and look at the standard curve!
What part of Germany are you from?
The area where I am from is called Ruhr area (german: Ruhrgebiet)
Why 37 °C for 30 min ??? I believe that is not sufficient ...