The indirect immunofluorescence ("fluorescent Ab") test shown below is performed to test for: $5.4 ㅅ T. pallidum from Specific antibodies laboratory stock in serum of patient Antibodies bind to T. pallidum + Fluorescent dye-labeled anti-human immune serum globulin (This will react with any immunoglobulin) Fluorescent spirochetes (see Figure 3.6b) None of the other four answers are correct The presence of T. pallidum bacteria in the patient's blood Whether the patient has made antibodies against other human antibodies Immunologic evidence of current or past infection with T. pallidum (i.e., Ab against T. pallidum) Growth of T. pallidum in culture from a syphilis patient

Because they sometimes cross-react with antigens other than those being tested for, polyclonal antibodies lack   1. reactivity 2. sensitivity 3. specificity 4. antigenicity

1) SDS PAGE gels can be probed with NBT/BCIP to perform an immunoblot true/ false 2) the direction of migration of protiens through a matrix is due to most proteins in natur having a net negative charge  true/false 3)  PBST  is a buffer that is used for blocking the membrane during immunoblotting. true/false 4) the buffer used during for transferring proteins to nitrocellulose methanol. true/false 7) The size of the pores of a polyacrylamide gel dcreases as concentrations of polyacrylamide increases. True or false 10) The secondary antibody used in laboratory for western blotting is conjugated to which enzyme  A) Alkaline decarboxylase B) GAPDH C) Alkaline Phosphatase D) Horseeradish peroxide 13) In protien electrophroresis, what reagent present in the sample buffer is used to eliminate difference in the charge densities of protein A) SDS B) 2- mercaptoethanol C) Tris-HCL pH6.8 D) Tris- HCL PH 8.8

What is "defined as the structural differences (diversity) observed in the variable domains of antibodies?   This is for immunology.

The substrate for the secondary antibody used in the lab for western blotting is:  triton X-100 BCIP/NBT Tween    TMB

Addition of immunoglobulin G (IgG) specific for hemoglobin to a solution of hemoglobin results in the formation of a red precipitate. In contrast, addition of the Fab fragments from this antibody to hemoglobin results in no such precipitate. What could explain this difference in results? Treatment with papain produces Fab fragments with different antigen specificity than the original IgG molecule. IgG can simultaneously bind two different antigens, whereas an Fab fragment can only bind one antigen at a time. The Fab fragments preferentially bind to other Fab fragments rather than to hemoglobin. The hemoglobin molecule antibody-binding sites can bind IgG molecules, but cannot bind Fab fragments.

eds Antibodies (Immunoglobulins) Objective 14 Antibodies (immunoglobulins) are glycoproteins secreted by plasma cells. They are located in interstitial fluid, plasma (gamma globulin fraction) and in body secretions. onse A. Antibody Structure Heavy chain Antigen-binding site Light chain Insmakamos Hinge region Complement- binding site Stem region Macrophage binding site OHO (a) Antibody molecule OHO X = Disulfide bond Carbohydrate four polypeptide chains (two heavy, two light) chains are held together by covalent disulfide bonds (S=S) each heavy chain and each light chain has two functional areas: consists of highly variable amino acid sequences which forms the basis of antibody specificity; antigen binds here ????? to more conserved amino acid sequences; there are five basic sequences of amino acids, which define the 5 antibody classes (IgG, IgA, IgM, IgE and IgD); ????? each class has its own characteristic set of effector functions (see next page) Your notes: 4 40 4. 39