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The water-accessible surface area of an IgG antibody. Immunoglobulin G (IgG) is a type of antibody. Representing approximately 75% of serum antibodies in humans, IgG is the most common type of antibody found in blood circulation. [1] IgG molecules are created and released by plasma B cells. Each IgG antibody has two paratopes.
Immunohistochemistry can be performed on tissue that has been fixed and embedded in paraffin, but also cryopreservated (frozen) tissue.Based on the way the tissue is preserved, there are different steps to prepare the tissue for immunohistochemistry, but the general method includes proper fixation, antigen retrieval incubation with primary antibody, then incubation with secondary antibody.
Immunolabeling - Antigen Detection of Tissue via Tagged Antigen-specific Antibody. Immunolabeling is a biochemical process that enables the detection and localization of an antigen to a particular site within a cell, tissue, or organ.
An antibody elution removes bound antibody from the surface of a red blood cell to aid in the antibody identification process. An antibody elution is a clinical laboratory diagnostic procedure which removes sensitized antibodies from red blood cells, in order to determine the blood group system antigen the antibody targets. [1]
Photomicrograph of a histological section of human skin prepared for direct immunofluorescence using an anti-IgG antibody. The skin is from a patient with systemic lupus erythematosus and shows IgG deposit at two different places: The first is a band-like deposit along the epidermal basement membrane ("lupus band test" is positive).
This is a recombinant monoclonal antibody to human IgG. It has the ability to bind to all 4 human IgG subtypes: IgG1, IgG2, IgG3, and IgG4. [7] Anti-Human IgG [8E11] This is a recombinant monoclonal antibody to human IgG. However, it can screen for IgG in nonhuman primates including vervets, chimpanzees, and mangabeys.
Mechanism of class-switch recombination that allows isotype switching in activated B cells. Immunoglobulin class switching, also known as isotype switching, isotypic commutation or class-switch recombination (CSR), is a biological mechanism that changes a B cell's production of immunoglobulin from one type to another, such as from the isotype IgM to the isotype IgG. [1]
Each heavy chain has two regions: a constant region (which is the same for all immunoglobulins of the same class but differs between classes).. Heavy chains γ, α and δ have a constant region composed of three tandem (in a line next to each other) immunoglobulin domains but also have a hinge region for added flexibility.