SUMMARY, EXPLANATION AND LIMITATIONS:
Immunoglobulins belong to a group of related glycoproteins which make up 20% of serum proteins. Antigens and immunoglobulins react to confer immunity to individuals. Immunoglobulins have similar structures of two identical heavy chains and two identical light chains. Both the heavy chains and the light chains are divided into constant and variable regions. The constant regions have the same amino acid sequences between all the immunoglobulin classes. The variable regions have approximately 110 amino acids with high sequence variability. The amino acid sequence of the heavy chain determines the class of an immunoglobulin. The five types of immunoglobulin heavy chains are known as: IgG, IgA, IgM, IgD, and IgE. IgG is divided into four subclasses, and IgA is divided into two subclasses. In serum IgA and IgG are monomers with a single 4 polypeptide unit; while, IgM is a pen tamer. IgA may also form polymers. Kappa light chain antibody can be used for the identification of leukemias, plasmacytomas and certain non Hodgkin’s lymphomas. Kappa light chain contains one immunoglobulin like domain.
Isotype: Rabbit IgG
Immunogen: Pool of human kappa light chain isolated from the urine of patients with Bence Jones Proteinuria.
Staining pattern: Cytoplasmatic and secreted.
Positive control: Tissue sample from tonsil.
This antibody is designed for the specific localization of human Kappa Light Chain using IF techniques in formalin-fixed, paraffin-embedded tissue sections and frozen tissue.