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When an antibody attaches onto an antigen it destroys the antigen to help your body fight off a disease.
Wiki User
∙ 13y ago
Wiki User
∙ 13y agoYes is does.
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Are anitgens proteins?
Yes. An antigen is a substance that stimulates an animal in order to produce an antibody reaction to counteract the substance by a specific binding antibody-antigen. Most of the times this antigen is a molecule of protein.
What is meant by unexpected antibody in human blood?
An unexpected antibody in human blood means that a person does not have the antigen required to make a certain antibody because it is foreign to them. Unexpected antibodies are usually alloantibodies.
Macfarlane burnet theory about antigen antibody reaction?
The Burnet theory about antigen antibody reaction is a basic concept about how we make antibodies specific to a foreign substance which has the ability to induce an immune response (antigen). Each B cell displas one unique type of B cell receptor on their surface (which is basically a membrane bound antibody). Therefore many B cells, each expressing its own type of B cell receptor are needed to cover the inexhaustable number of antigens that are possible, in the hope that one type of B cell receptor will be able to recognise the shape of that antigen. If one B cell does recognise the antigen in question, then this B cell will become activated to make many clones of itself, which will obviously carry identical B cell recptors which fit the antigen. |Therefore the clonal selection theory by Burnet is about antibody antigen interactions which result in the 'best-fit' B cell receptor inducing a reaction to tell the B cell carrying the receptor to multiply and produce lots of identical antibodies which can then be secreted to bind to the antigen they are specific for.
What are antigens and how do lymphocytes recognize them?
it specifically recognise the antigenic determinants called epitopes and the similar sequence of that particular epitope will be produced by the antibody at is variable region(specifically hypervariable region) whch make an antibody to get more affinity over that particular antigen..almost antibodies are available for almost all the antigens in our body(memory cells)and they starts increasing in numbr once an antigen enters our body
What is the difference between a antigen and a processed antigen?
An antigen can be anything from virus to bacteria to a soluble protein from outside or inside a cell. This includes both foreign and self peptides. An antibody that finds an appropriate antigen will bind to it and your B and T cells determine if it's self or not. A processed antigen came from cytosol. A protein will be taken by ubiquitin to a proteosome where it is broken up into small peptides. These peptides will make their way into the endoplasmic reticulum (through TAP) where they are exposed to MHC's.
What is Elisa used for?
ELISA is a technique used to determine the presence of antigen or antibody in a sample. ELISA is used in diagnosis of HIV... ELISA is of three types: direct method, indirect method and sandwich method. The principle of three methods are same.
How are antibodies produced?
lymphocytes make antibodies by first getting the antigen marker from a pathogen. Then, using a 'toolkit' of various protein fragments, they use the marker as a 'blueprint' to make the antibody.
What is the commercial where paper cutouts of professors that make harmless things but turn them into something harmless?
they're already harmless...how does it go harmless to harmless
What are the 2 main parts of the immune system?
Primary versus Secondary Immune ResponseThe primary immune response occurs the first time that the immune system comes in contact with the antigen. During this time the immune system has to learn to recognize antigen and how to make antibody against it and eventually gain immunological memory. This primary response takes time (about two weeks) and during this time the person experiences signs of illness. IgM antibodies are the hallmark of a new infection because they are the first antibodies made when a person is exposed to an antigen for the first time. After the body learns to make IgM antibodies, it will start making IgG antibodies to the antigen.The secondary immune response occurs the second time (3rd, 4th, etc.) the person is exposed to the same antigen. At this point immunological memory has been established and the immune system can start making antibodies immediately. The antigen usually is killed within minutes and the person is not aware that he/she was attacked. The antibodies in this response are IgG and IgA or (in the case of allergy IgE).
What is an antibodie?
Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
What is an antibody and what do?
Antibodies (also known as immunoglobulins,abbreviated Ig) are gamma globulin proteins that are found in blood or other bodily fluids of vertebrates, and are used by the immune system to identify and neutralize foreign objects, such as bacteria and viruses. They are typically made of basic structural units-each with two large heavy chains and two small light chains-to form, for example, monomers with one unit, dimers with two units or pentamers with five units. Antibodies are produced by a kind of white blood cell called a plasma cell. There are several different types of antibody heavy chains, and several different kinds of antibodies, which are grouped into different isotypes based on which heavy chain they possess. Five different antibody isotypes are known in mammals, which perform different roles, and help direct the appropriate immune response for each different type of foreign object they encounter.Though the general structure of all antibodies is very similar, a small region at the tip of the protein is extremely variable, allowing millions of antibodies with slightly different tip structures, or antigen binding sites, to exist. This region is known as the hypervariable region. Each of these variants can bind to a different target, known as an antigen. This huge diversity of antibodies allows the immune system to recognize an equally wide diversity of antigens. The unique part of the antigen recognized by an antibody is called an epitope. These epitopes bind with their antibody in a highly specific interaction, called induced fit, that allows antibodies to identify and bind only their unique antigen in the midst of the millions of different molecules that make up an organism. Recognition of an antigen by an antibody tags it for attack by other parts of the immune system. Antibodies can also neutralize targets directly by, for example, binding to a part of a pathogen that it needs to cause an infection.The large and diverse population of antibodies is generated by random combinations of a set of gene segments that encode different antigen binding sites (or paratopes), followed by random mutations in this area of the antibody gene, which create further diversity. Antibody genes also re-organize in a process called class switching that changes the base of the heavy chain to another, creating a different isotype of the antibody that retains the antigen specific variable region. This allows a single antibody to be used by several different parts of the immune system. Production of antibodies is the main function of the humoral immune system.
How do white blood cells recognize particular types of pathogen?
Lymphocytes make a different antibody for each pathogens. They have this 'memory' of a pathogen they had previously come in contact with. The person is then said to be immune to that disease, as the lymphocytes know immediately which antibody to make.
