A glycoprotein composed of “heavy” and “light” peptide chains; functions as antibody in serum and secretions. There are five major classes (IgG, IgA, IgM, IgE, and IgD), each with specialized functions.
A protein that acts as an antibody.
A member of a family of proteins from which antibodies are derived. There are five main classes in humans known as IgM, IgG, IgA, IgD and IgE.
A class of (blood) serum proteins representing antibodies. Often used, along with the more specific monoclonal antibodies, in health diagnostic reagents. In certain people who are genetically predisposed to foodbome allergies, immunoglobulin-E (IgE) initiates an immune system response to antigen( s) present on protein molecule(s) in the particular food that person is allergic to. Severe allergic reactions to foods may lead to death.
A protein of animal origin with known antibody activity.
A protein that can act as an antibody.
Serum globulin having antibody activity. Most of the antibody activity appears to be in the gamma fraction of globulin.
An antibody, a protein produced in blood plasma as protection against infection, the commonest being gamma globulin.
Proteins that develop in response to antigens.
A class of substances produced by the immune system, including antibodies. One type, immunoglobulin E (IgE), is mainly responsible for the reactions in allergy and asthma.
Any of the five classes of structurally distinct antibodies, produced in lymph tissue in response to the invasion of a foreign substance. The five major kinds are immunoglobulin A, D, E, G, and M. Also called immune serum globulin.
Glycoproteins produced by white blood cells that function as antibodies.
Proteins produced in the blood by the immune system. Many immunoglobulins are antibodies. Antibody molecules can be divided into distinct classes and subclasses based on their size, charge, solubility, and behavioral characteristics. In humans, the classes of antibody molecules are IgG, IgM, IgA, IgE, and IgD. These immunoglobulins each have a different role in the immune system’s strategy to defend the body from invasions of harmful antigens. IgG has four kinds of antibodies, all of which can enter tissue spaces and coat microorganisms with a substance called complement to increase the rate at which they are attacked by other cells in the immune system. IgM generally remains in the bloodstream where it is effective at destroying bacteria. There are two kinds of antibodies in the classification called IgA, and they are concentrated in body fluids, including tears, saliva, and secretions in the respiratory system and gastrointestinal tract; they are able to protect the body from antigens attempting to enter a system via these fluids and secretions. IgE normally occurs in only trace amounts. IgE possibly evolved as a defense against parasites, but it is the antibody that overreacts to n on harmful substances that can cause severe allergic reactions. IgD is located within the membranes of B cells and works to regulate the cell’s activation.
One of a group of structurally related proteins (gamma globulins) that act as antibodies. Several classes of Ig with different functions are distinguished: IgA, IgD, IgE, IgG, and IgM. They can be separated by immunoelectrophoresis.
Immunoglobulins are a group of naturally occurring proteins that act as antibodies. They are structurally related, their differences determining their biological behaviour. Humans have five types of immunoglobulin with different protective functions: IgA, IgD, IgE, IgG and IgM. In the laboratory these are separated and identified by a chemical process called electrophoresis. Most antibodies have a molecular weight of 160,000.
Any of a diverse group of plasma polypeptides that bind antigenic proteins and serve as one of the body’s primary defenses against disease. Two different forms exist. The first group of immunoglobulins lies on the surface of mature B cells, enabling them to bind to thousands of antigens. When the antigens are bound, the B plasma cells secrete the second type of immunoglobulins, antigen-specific antibodies, which circulate in the blood and accumulate in lymphoid tissue, esp. the spleen and lymph nodes, binding and destroying specific foreign antigens and stimulating other immune activity. Antibodies also activate the complement cascade, neutralize bacterial toxins and viruses, and function as opsonins, stimulating phagocytosis.
Also known as antibodies; soluble proteins produced by B cells that circulate in the bloodstream and bind to viruses and other antigens to neutralize them.
Any of five distinct antibodies in the serum and external secretions of the body.
A compound produced by B cells that counteracts specific disease-causing agents and microorganisms. It is also referred to as an “antibody.” Immunoglobulins are categorized into five classes: IgA, IgD, IgE, IgG, and IgM.
Also referred to as an antibody, this type of protein is found in blood and tissue fluids. They are generated by B-lymphocytes, a variety of white blood cells. Their purpose is to attach to foreign substances in the body, known as antigens, like proteins found on the surfaces of bacteria and viruses. This attachment is vital for the elimination of microorganisms carrying these antigens. Immunoglobulins also have a significant role in allergies and hypersensitivity responses.
There are five primary classes of immunoglobulin (antibodies) in the blood: IgA, IgD, IgE, IgG, and IgM. IgA is mainly located in the secretions of the respiratory system, intestines, and urinary tract. IgD exists in relatively low quantities in the body and its exact function remains unknown. IgE plays a role in the immune response to worm infestations and is also produced in high quantities to combat atopic (allergic) conditions. IgG represents the predominant class of immunoglobulin and is divided into four subclasses. Its structure consists of two parts, one part binds to an antigen while the other to the immune system’s cells. These cells then consume the microorganisms that carry the antigen. The primary function of IgG is to combat bacterial infections. In the case of infection, IgM is produced rapidly and then its levels decrease. The presence of IgM in a newborn indicates a possible infection during pregnancy.
Immunoglobulins, or antibodies, can be obtained from the blood of individuals who have recovered from certain infectious diseases. These antibodies can then be utilized to provide passive immunization.