Compare and contrast the following techniques: FISH, immunofluorescence, and GFP fusion proteins. In your answer, be sure to include similarities and differences, as well as the application of each technique (what are they used for – what can they tell us)?
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Compare and contrast the following techniques: FISH, immunofluorescence, and GFP fusion
proteins. In your answer, be sure to include similarities and differences, as well as the application of
each technique (what are they used for – what can they tell us)?
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- With detail, compare and contrast the following 5 real-time assays; Taqman, SYBR Green, Molecular Beacon, FRET, and Scorpion. Please write complete sentences in paragraph form. Identify how the assays are similar but more importantly, what are the distinguishing features of each of the technologies.explain how the following genotypic andphenotypic methods of microbe identification is done. Use diagrams or schematic representations to explain yourwork. (1) Restriction Fragment Length Polymorphism (RFLP)(2) Pulsed-Field Gel Electrophoresis (PFGE)(3) Whole Genome Sequencing (WGS)(4) Gram Staining(5) Biochemical Reactions: Multiple Tube Fermentation Technique(6) Biochemical Reactions: IMViC TestThe table below shows the response of our ESKAPE safe relatives to 4 bacteria isolated from a master grid. We do not know the identity or any characteristics of the unknown bacteria. Each safe relative was spread onto a petri dish using aseptic technique. A grid pattern was taped to each plate and the unknown bacteria were patched into one of the squares. If there was no inhibition visible, including with a magnifying lens, the result was listed as -. If there was an inhibition zone between 1 and 10mm in diameter, the result is listed as +. If the inhibition zone was 10mm or greater, the result is listed as ++. In the lab, the MGC instructors plated all 6 of the ESKAPE pathogen safe relatives on LB agar plates. Then we patched Unknown Bacteria 5 from a Master plate onto the safe relative. The results are shown here: METRIC METRIC METRIC 1 B. subtilis S. epidermidis E. coli Complete the final column (Unknown Bacteria 5) of the table by selecting -, +, or ++ using the criteria in the…
- The table below shows the response of our ESKAPE safe relatives to 4 bacteria isolated from a master grid. We do not know the identity or any characteristics of the unknown bacteria. Each safe relative was spread onto a petri dish using aseptic technique. A grid pattern was taped to each plate and the unknown bacteria were patched into one of the squares. If there was no inhibition visible, including with a magnifying lens, the result was listed as -. If there was an inhibition zone between 1 and 10mm in diameter, the result is listed as +. If the inhibition zone was greater than 10mm, the result is listed as ++. Page 50 in your research guide states: "Some antibiotics are broad spectrum, meaning that they affect a wide range of bacteria. Other antibiotics have a narrow spectrum of activity. One anatomical feature that plays a significant role in the susceptibility of a microbe to a particular antibiotic is its cell wall composition (discussed in Section 8)". Research the cell wall…The table below shows the response of our ESKAPE safe relatives to 4 bacteria isolated from a master grid. We do not know the identity or any characteristics of the unknown bacteria. Each safe relative was spread onto a petri dish using aseptic technique. A grid pattern was taped to each plate and the unknown bacteria were patched into one of the squares. If there was no inhibition visible, including with a magnifying lens, the result was listed as -. If there was an inhibition zone between 1 and 10mm in diameter, the result is listed as +. If the inhibition zone was greater than 10mm, the result is listed as ++, Page 50 in your research guide states: "Some antibiotics are broad spectrum, meaning that they affect a wide range of bacteria. Other antibiotics have a narrow spectrum of activity. One anatomical feature that plays a significant role in the susceptibility of a microbe to a particular antibiotic is its cell wall composition (discussed in Section 8)". Research the cell wall…What are the ordered steps of an ELISA protocol? A. Add primary antibody->wash-> Bind sample to a surface ->Add substrate ->Add secondary antibody-enzyme conjugate ->wash B. Bind sample to support -> Add substrate -> Add primary antibody -> wash -> Add secondary antibody-enzyme conjugate -> wash C. Bind sample to a surface -> Add primary antibody -> wash -> Add secondary antibody-enzyme conjugate -> wash -> Add substrate D. Add secondary antibody-enzyme conjugate -> wash -> Add primary antibody -> wash -> Add substrate -> Bind sample to surface
- Recombinant Protein G from Streptococcus are covalently attached in an oriented fashion to magnetic beads. Bovine Serum is added and the antibodies are captured by the beads. Using the magnetic device, beads are attached and unbound material is washed away. Antibodies are eluted using a lower pH buffer and the solution is neutralized. The equilibration step is adding the serum sample to the buffer-equilibrated (pH 6) magnetic Protein G beads. What was expected to occur if this step was missed? When we mix the samples on the mixer, it was crucial that there was no foam present in the sample - why is this and what part of the mixture would be "foamy" at this step? Lastly, we use an neutralizing buffer after eluting the samples from the column. Why is this step important?What is an advantage of using an ELISA instead of a protein microarray to study a proteome? What is a disadvantage?What technique would you use for each senario(a and b) and why. FISH, immunofluorescence, and GFP fusion. proteins. Each technique is only used once. a.You are studying cells in the lab from four patients with I-cell disease. First, you need to know if the phosphotransferase gene is being expressed in any of these 4 patient’s cells. b.Next, you want to determine if you can replace the defective protein with a normal one. First, you need to determine if the replacement protein (one that you are creating in the lab and inserting it into the patent’s cells), will be targeted to the lysosome.
- You perform a plaque assay with your bacteria and serial dilutions of your bacteriophage, , and then count the plaques. In the 10-5 dilution you have 318 plaques. In the 10-6 dilution, you count 32 plaques, and in the 10-7 dilution, there are 3 plaques. What is the approximate PFU/cell of your sample? 3.2 x 105 318 3.2 x 107 O 3.2 x 106A plaque assay is performed beginning with 1 mL of a solution containing bacteriophages. This solution is serially diluted three times by combining 0.1 mL of each sequential dilution with 9.9 mL of liquid medium. Then 0.1 mL of the final dilution is plated in the plaque assay and yields 17 plaques. What is the initial density of bacteriophages in the original 1 mL?Complete the following tasks. You discovered that a species of bacteria can break down StyrofoamT (polystyrene) products due to an enzyme it produces, polystyrenase. You wish to study the gene that codes for this enzyme. Task 1: DNA Extraction To begin work on the bacterium, you begin by extracting its genomic DNA (GDNA). What is the purpose of the following procedures? Answer briefly but completely. Using sodium dodecyl sulfate, a detergent Answer: а. b. Adding RNase A and Proteinase K during extraction Answer: c. Adding ethanol before recovering the DNA extract С. Answer: Task 2: Polymerase Chain Reaction After purifying the gDNA extract, you want to isolate and amplify the polystyrenase gene. You perform PCR using the appropriate gene-targeted primers. What is the purpose of the following PCR components? Answer briefly but completely. DNA polymerase isolated from Thermus aquaticus Answer: а. b. Deoxynucleotide triphosphates (DNTPS) Answer: С. Forward and reverse primers Answer: Task…