what is main problem in creating monoclonal antibodies?
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Honestly, its all up to you and there isn't really any answers that can help you better coz lets face it, you know your problem better than anyone else. If there is any solution, it has to be from you yourself.\n\ngood luck\n\nLove is omnipresence, Love is patient, love is kind. It does not envy, it does not boast, it is not proud. It is not rude, it is not self-seeking, it is not easily angered, it keeps no record of wrongs. Love does not delight in evil but rejoices with the truth. It always protects, always trusts, always hopes, always perseveres. Love never fails.
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Generally polyclonal anitbodies are used to bind non-specifically to antigens. For instance, you might use monoclonal antibodies to specifically bind to your protein of intererst. You might then use polyclonal Ab to bind the rest of the proteins i.e. to block off the other available 'slots'
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Too many to list and explain here, without copying and pasting  --and why should I do all your uni work for you? ;-)\n\nI will recommend a couple of good text books through.  Well worth a purchase or just get them on loan from your library...\n\nAlberts et al, Molecular Biology of the Cell\nStryer, Biochemistry\n\nIt's been since I bought mine.  Think I got editions 2 & 7 back in 1996 and I know both have been updated a couple of times since.  These are still a GREAT basic resourse for this sort of question.
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Yarnlady is correct. This is certainly not something that can be easily br adequately answered in a yahoo answers forum. \n\nBasically the problems boil down to investment in hardware, software and resources trained in implementing such as system. \n\nThe solutions at a very high level are start slowly, plan carefully obtain funding and get buy in from a project sponser down to the end users for the new system
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B cells produce antibodies when triggered by an antigen.  They also produce memory cells (these "remember" a particular antigen and allow large scale production of antibodies if the antigen enters the system again) \n\nAntibodies are also called immunoglobins, and their job is to combine with specific antigens (such as pollen, dust, etc.).  They may coat the antigens in such a way that they can be absorbed by phagocytic cells, combine with an antigen in order to inhibit its function, or may actually lyse and destroy the antigens.  \n\nCytotoxic, or killer, T cells lyse and destroy foreign cells and material and any cells in the organism infected with foreign material.\n\nHope this is helpful :-)
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Antigen is any substance that evokes the production of an antibody when introduced into the body. Antigens can enter the body through the respiratory tract, digestive tract, or skin. The most common antigens are proteins such as those found in/on bacteria and viruses.While an antibody Antibody, any of perhaps a million kinds of normally occurring protein molecules that are produced in the body of cells called lymphocytes and that act primarily as a defence against invasion by foreign substances. An important component of the immune system, antibodies are found in the blood of all vertebrates, in the fraction of the blood called gamma globulin.
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immunoglobulins are the basis of the immune system and that isn't just fighting infection but more importantly self-recognition.\nimmunoglobilins must be able to bind to surface antigens to confirm whether the cell carrying the antigen is foreign or not, human immunoglobulins are most definately different to other animals'. For example if you needed a liver transplant and introduced a sheep's liver into your body your immunoglobulins whould identify it as foreign and reject it.\nAlso diseases that afect livestock do not affect humans so our immune systems are quite different.\nI am in no doudt that the milk contains immunoglobulins since it is the way the young animal builds its immune system. However they would be completely incompatible with the human body and they would just be broken down, also if you think about it immunoglobulins are large protein molecules which cannot be absorbed by the digestive system without being broken down, in which case they would be useless anyway.\nThe fundamental reason for this incompatibility is the fact that human DNA is different to cows DNA ect. so the immunoglobulins coded for by the cow's DNA are useless to humans.
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Have you tried this site\nhttp://www.answers.com/topic/elisa
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In order to perform in vitro analyses, a protein must be purified away from other cellular components. This process usually begins with cell lysis, in which a cell's membrane is disrupted and its internal contents released into a solution known as a crude lysate. The resulting mixture can be purified using ultracentrifugation, which fractionates the various cellular components into fractions containing soluble proteins; membrane lipids and proteins; cellular organelles, and nucleic acids. Precipitation by a method known as salting out can concentrate the proteins from this lysate. Various types of chromatography are then used to isolate the protein or proteins of interest based on properties such as molecular weight, net charge and binding affinity. The level of purification can be monitored using gel electrophoresis if the desired protein's molecular weight is known, by spectroscopy if the protein has distinguishable spectroscopic features, or by enzyme assays if the protein has enzymatic activity.\n\nFor natural proteins, a series of purification steps may be necessary to obtain protein sufficiently pure for laboratory applications. To simplify this process, genetic engineering is often used to add chemical features to proteins that make them easier to purify without affecting their structure or activity. Here, a "tag" consisting of a specific amino acid sequence, often a series of histidine residues (a "His-tag"), is attached to one terminus of the protein. As a result, when the lysate is passed over a chromatography column containing nickel, the histidine residues ligate the nickel and attach to the column while the untagged components of the lysate pass unimpeded.\n\n\n[edit] Cellular localization\n \nProteins in different cellular compartments and structures tagged with green fluorescent protein.The study of proteins in vivo is often concerned with the synthesis and localization of the protein within the cell. Although many intracellular proteins are synthesized in the cytoplasm and membrane-bound or secreted proteins in the endoplasmic reticulum, the specifics of how proteins are targeted to specific organelles or cellular structures is often unclear. A useful technique for assessing cellular localization uses genetic engineering to express in a cell a fusion protein or chimera consisting of the natural protein of interest linked to a "reporter" such as green fluorescent protein (GFP). The fused protein's position within the cell can be cleanly and efficiently visualized using microscopy, as shown in the figure opposite.\n\nThrough another genetic engineering application known as site-directed mutagenesis, researchers can alter the protein sequence and hence its structure, cellular localization, and susceptibility to regulation, which can be followed in vivo by GFP tagging or in vitro by enzyme kinetics and binding studies.\n\n\n[edit] Proteomics and bioinformatics\nMain articles: Proteomics and Bioinformatics\nThe total complement of proteins present in a cell or cell type is known as its proteome, and the study of such large-scale data sets defines the field of proteomics, named by analogy to the related field of genomics. Key experimental techniques in proteomics include protein microarrays, which allow the detection of the relative levels of a large number of proteins present in a cell, and two-hybrid screening, which allows the systematic exploration of protein-protein interactions. The total complement of biologically possible such interactions is known as the interactome. A systematic attempt to determine the structures of proteins representing every possible fold is known as structural genomics.\n\nThe large amount of genomic and proteomic data available for a variety of organisms, including the human genome, allows researchers to efficiently identify homologous proteins in distantly related organisms by sequence alignment. Sequence profiling tools can perform more speci
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Are you talking about using antibodies made in one species to treat human diseases?  This has been tried, and it hasn't worked.  The human immune system actually attacks the foreign antibody, and destroys it.  Also, antibodies from other species doesn't have the same effector binding sites as human antibodies.  That is, they are incapable of creating an immune response.  The solution?  Engineered antibodies.  This involves making chimera's, humanizing antibodies, and/or using viral vectors.  The engineered antibody can be made to have the human constant regions (the effector part) attached to another species' variable region (the part that recognizes the antigen).  Viral vectors are made by placing cDNA into viruses, and searching for the one that makes the specific antibody.  This virus is then separated from the others, and grown up to make antibodies.  There are really some ingenious ideas out there to make antibody therapy more useful.  There are some already in use- any medicine you see that ends in "mab" means it's a monoclonal antibody.\nOh, and they would almost definately have to be injected.  Antibodies are proteins, and would therefor be degraded by the digestive system.
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I assume the end of the question was "antibodies" or "antigens" and the answer is false for both.\n\nHowever there have been a few moderately successful attempts at engineering antibodies with catalytic activity. But in normal cellular physiology only specific enzymes speed up chemical reactions.
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try these links. they are a quite a helpful read. \n\nwww.merck.com/mrkshared/ mmanual/section11/chapter143/143c.jsp\n\nwww.pnas.org/cgi/content/full/102/2/419\n\nwww.autoimmuneinc.com/R_and_D/tech.html\n\nwww.sciencemag.org/cgi/content/figsonly/309/5739/1380\n\ngood luck and have fun!!!
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Are you looking at any protein in particular?  Look up in situ hybrdization for proteins ( at least it will give you an idea where it is localised).  I think that it would really depend on the system ad proteins that you want to study, so I am not sure how much else I can tell you, sorry.
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You need mRNA to act as a template, ribosomes to catalyze the reaction and tRNAs carrying the amino acids which will make the protein chain. Actually you need more stuff like GTP but these 3 are the basics.
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Affinity purification is a method commonly used in protein chemistry to isolate a product from a mixture that interacts with another known, and previously isolated, product.  Negative affinity purification, on the other hand, is a method used to deplete a known contaminant from a protein mixture based upon its ability to bind to a different molecule.\n\nFor example, a scientist wants to make an antibody specific for a novel protein. He/she produces the protein as a fusion product linked to GST (glutathione-S-transferase), since there are many methods to allow isolation of this fusion protein (by affinity purification techniques).  This fusion product is then injected into a mouse or rabbit and after some time the animal produces antibody in its blood.  \n\nWhile it might be acceptable to use the whole serum (containing the protein specific antibody) from this animal for subsequent experiments, the antibody of interest is only a small fraction of the total protein in the serum.  So, the scientist purifies the antibody directed against the protein of interest using a column containing the GST-fusion product used for inoculation (again, affinity purification) and elutes the antibody fraction that recognizes this protein.  Great, but the scientist knows that the GST component of the fusion protein will also induce the mouse to make antibodies, and that these GST-specific antibodies will be purified by the previous step.  So, he/she decides to do NEGATIVE Affinity Purification by passing the purified antibody mix over a column that contains the GST protein alone (not the fusion product) and then collects the antibody that DOES NOT bind to the GST alone.  Voila, protein specific antibody without contaminating GST-specific antibody... using negative affinity purification.
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Most common problem is when students treat a laboratory experiment as following a recipie or step-by-step instructions.  They don't have an understanding of what they are doing, or why they are doing it.  \n\nAn effective way of solving this is to have the students take an active role in defining the experiment.  Well ahead of the lab, the instructor presents the problem that needs to be solved and asks the students to design an experiment to solve it.  The students sumbit their proposals in time for the instructor to review (and correct as needed) before the actual lab.\n\nThis takes more effort from the students and teacher, but pays off well.\n\nAt a minimum, you could at least require the students to come prepared for lab by having them write an outline of the experiment and having them answer some questions in thier lab notebook before they are allowed to start.
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Your body does create antibodies, but some bacteria miltiply very quickly and simply over-power the body's immune system, and then you would never get better, you may suffer permanent damage, and you could possibly die. \n\nAntibiotics work in one of two ways. Some actually kill the infection, and others only prevent the growth of the infection, thus giving the body the time it needs to fight the bacteria itself.