Can an immunoblot (western blot) help you determine whether your protein is pure? Why or why...
Can an immunoblot (western blot) help you determine whether your protein is pure? Why or why not?
My guess is no because then additional steps would be required but unsure.
Homework Answers
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Can an immunoblot (western blot) help you determine whether your
protein is pure? Why or why...
this is western blotting experiment and I need your help with questions. I will send the...
this is western blotting experiment and I need your help with
questions. I will send the summary for this exiperiment
PRE-LAB PROTOCOL: Answer the following pre-lab questions: 1. 2. 4. How is mouse anti-goat lgG antibody generated? Why must sodium azide not be included in the secondary antibody incubation steps? Assuming that the overall yield of LDH enzyme in your prep was exactly 100%, how should the intensity of the LDH band in the NADH pool sample compare to that...
Which of the following techniques would allow you to determine whether a gene is alternatively spliced?...
Which of the following techniques would allow you to determine whether a gene is alternatively spliced? a) In situ hybridization b) Northern blot c) Southern blot d) genomic DNA sequencing I honestly need help with this; I first thought it was Northern blot, but I'm starting to second guess myself on that and genomic DNA sequencing. Any help would be appreciated.
You are working on the protein α-catenin in C. elegans and have produced a monoclonal antibody...
You are working on the protein α-catenin in C. elegans and have produced a monoclonal antibody that recognizes this protein. The normal protein identified by this antibody on a Western blot is 104kDa. You go on to identify a mutant that you think produces no protein at all (geneticist call such mutants “protein null” mutants) because Western blots performed using your antibody with protein from this mutant yield no signal. Later, however, another member of your research group sequences your...
Can you please explain what the right answer and why? 43. You are using an anti-mouse...
Can you please explain what the right answer and why?
43. You are using an anti-mouse monoclonal antibody to a nonlinear conformational epitope in an ELISA. Which of the following is TRUE? This antibody should work well in a western blot from an SDS-PAGE gel This antibody can't be used in a western blot because it will be denatured by the residual SDS This antibody be useful in targeting a protein blotted from a native gel. This antibody should have...
You find yourself setting up another Western blot, however. today you are preparing the samples t...
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
Can you help with this question That is all the information I was given This is...
Can you help with this question
That is all the information I was given
This is the entire questions
This is all the information I was given
6. You perform a western blot of CPY* to confirm the results you observed in the growth assay presented in the previous question. Draw bands on the western blot below, assuming it validates (confirms) the results from the growth assay. Wild- Type Th 10% doaON? hra 1AE CPY"Σ Pgkiz 37E 5. You wish...
Can you please help me with this problem: 3. A dominant wild-type allele D produces full...
Can you please help me with this problem:
3. A dominant wild-type allele D produces full enzyme function, but a recessive alleled, produces no functional enzymatic action, and a recessive allele da produces reduced enzyme function. Western blot analysis of the proteins produced by organisms with different genotypes for this gene gives the results shown. Note, proteins separate out in a gel by size similar to DNA fragments with smaller polypeptides traveling farther. Genotype DD Dd, Dd, dod, dd₂ d₂d₂...
can anyone help me with this cell bio question? In Figure 2 part A (Non-denaturing). Lane 1 NEP( E403C) , 2 = WT...
can anyone help me with this cell bio
question?
In Figure 2 part A (Non-denaturing). Lane 1 NEP( E403C) , 2 = WT ECE, , 4= WT= NEP, 9= ECE(C416E). Figure 2 part B. The same as part A, but under denaturing conditions. (note; for simplicity, many lanes are ignored) 1 2 3 5 67 89 10 a -213 -123 -85 -50 b kDa -213 -123 85 -50 Figure 2 Immunoblot analyses of wild-type and cysteine mulants of NEP and...
can you help with part b why isn't the product pure based on the melting point???...
can you help
with part b
why isn't the product pure based on the melting point???
for part c the experiment was
Separation of acid/base/neutral compounds using liquid- liquid
extraction of benzocaine-trans-cinnamic acid and biphenyl
what was the purpose of using Na2SO4
estion 6: 100mg of each Acid, Base and Neutral compounds were used. Assuming 70mg mzocaine, 66mg trans-cinnamic acid and 50mg of biphenyl were isolated. a. Calculate % recovery of benzocaine, trans-cinnamic acid and biphenyl respectively. (show your calculation,...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify a novel protein from mammalian cells. You do not know this protein's size or charge, and are thus unsure of which steps to take. Fortunately, an antibody for this protein is available. You have two cell lines: one that expresses the protein, and one • that does not. . ) 4 5 III111 You run both cell lines on an SDS-PAGE (A) followed by...
this is western blotting experiment and I need your help with
questions. I will send the summary for this exiperiment
PRE-LAB PROTOCOL: Answer the following pre-lab questions: 1. 2. 4. How is mouse anti-goat lgG antibody generated? Why must sodium azide not be included in the secondary antibody incubation steps? Assuming that the overall yield of LDH enzyme in your prep was exactly 100%, how should the intensity of the LDH band in the NADH pool sample compare to that...
Can you please explain what the right answer and why?
43. You are using an anti-mouse monoclonal antibody to a nonlinear conformational epitope in an ELISA. Which of the following is TRUE? This antibody should work well in a western blot from an SDS-PAGE gel This antibody can't be used in a western blot because it will be denatured by the residual SDS This antibody be useful in targeting a protein blotted from a native gel. This antibody should have...
You find yourself setting up another Western blot, however. today you are preparing the samples to load onto the SDS-PAGE gel. You are using a 4-20%SDS-PAGE gel that can hold a maximum of 30 μしper 1 You remember from you so decided to prepare each sample with a final volume of 25 uL. However, no one is perfect at pipetting, so make sure each sample is made at 1.5X the total volume needed per well. The protein you are interested...
Can you help with this question
That is all the information I was given
This is the entire questions
This is all the information I was given
6. You perform a western blot of CPY* to confirm the results you observed in the growth assay presented in the previous question. Draw bands on the western blot below, assuming it validates (confirms) the results from the growth assay. Wild- Type Th 10% doaON? hra 1AE CPY"Σ Pgkiz 37E 5. You wish...
Can you please help me with this problem:
3. A dominant wild-type allele D produces full enzyme function, but a recessive alleled, produces no functional enzymatic action, and a recessive allele da produces reduced enzyme function. Western blot analysis of the proteins produced by organisms with different genotypes for this gene gives the results shown. Note, proteins separate out in a gel by size similar to DNA fragments with smaller polypeptides traveling farther. Genotype DD Dd, Dd, dod, dd₂ d₂d₂...
can anyone help me with this cell bio
question?
In Figure 2 part A (Non-denaturing). Lane 1 NEP( E403C) , 2 = WT ECE, , 4= WT= NEP, 9= ECE(C416E). Figure 2 part B. The same as part A, but under denaturing conditions. (note; for simplicity, many lanes are ignored) 1 2 3 5 67 89 10 a -213 -123 -85 -50 b kDa -213 -123 85 -50 Figure 2 Immunoblot analyses of wild-type and cysteine mulants of NEP and...
can you help
with part b
why isn't the product pure based on the melting point???
for part c the experiment was
Separation of acid/base/neutral compounds using liquid- liquid
extraction of benzocaine-trans-cinnamic acid and biphenyl
what was the purpose of using Na2SO4
estion 6: 100mg of each Acid, Base and Neutral compounds were used. Assuming 70mg mzocaine, 66mg trans-cinnamic acid and 50mg of biphenyl were isolated. a. Calculate % recovery of benzocaine, trans-cinnamic acid and biphenyl respectively. (show your calculation,...
Betergents h. What chemical would you add to refold this protein? 16. You wish to purify a novel protein from mammalian cells. You do not know this protein's size or charge, and are thus unsure of which steps to take. Fortunately, an antibody for this protein is available. You have two cell lines: one that expresses the protein, and one • that does not. . ) 4 5 III111 You run both cell lines on an SDS-PAGE (A) followed by...
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