Antibody heavy chains are components of immunoglobulins and play a central role in determining the structure, specificity, and effector functions of antibodies. Antibody heavy chains are encoded by a set of immunoglobulin heavy chain (IGH) genes on chromosome 14 within the Immunoglobulin Heavy Chain Locus (IGH locus). These genes undergo somatic recombination during B cell development in the bone marrow. The process involves the assembly of V (variable), D (diversity), and J (joining) gene segments, leading to the diversity of antibody heavy chain variable regions (VH). The constant region of the heavy chain determines the antibody isotype and subclass. In humans, there are five antibody isotypes: IgM, IgG, IgA, IgD, and IgE. Each isotype has specific biological properties and effector functions. IgG, for instance, is involved in opsonization and complement activation, whilst IgE is important in allergic responses. The heavy chain consists of multiple domains, each with specific functions. The variable region of the heavy chain (VH) contributes to antigen binding, whilst the constant region (CH) determines the antibody's class and effector functions. The hinge region provides binding flexibility, whilst a transmembrane region anchors membrane-bound antibodies. Disulphide bonds are introduced into antibody heavy chains during protein folding and assembly in the endoplasmic reticulum (ER). They contribute to the overall structural stability of antibodies and play a role in maintaining the correct conformation of the antigen-binding sites and the interaction between the heavy and light chains. The variable regions of both the heavy and light chains contribute to the antigen-binding site, allowing antibodies to recognize and bind specifically to a wide range of antigens. The heavy chain constant region dictates the effector functions of antibodies. For example, IgG antibodies can activate complement and interact with Fc receptors on immune cells, leading to opsonization, phagocytosis, and ADCC (antibody-dependent cellular cytotoxicity). Isotype switching allows B cells to change the heavy chain constant region, altering the functional properties of the antibody, whilst maintaining antigen specificity. In some antibody classes like IgM and IgA, heavy chains can form covalent dimers or multimers through additional disulphide bonds or J chain proteins, enhancing their functional properties. Multimerization involves the assembly of multiple antibodies and can include dimers, trimers, tetramers, and larger multimers. Examples of multimeric antibodies include IgM and pentameric IgM. Multimeric antibodies can bind to multiple antigens simultaneously, increasing binding strength, which can be important when antigens are present in high densities or when they have multiple epitopes. Multimerization also enhances the diversity of binding capabilities, allowing the antibody to recognize a wider range of antigens. Multimeric antibodies like IgM are also highly efficient at activating the complement system. The arrangement of antibody molecules in proximity on the pathogen's surface leads to more efficient complement activation and pathogen destruction. Multimeric antibodies can also cross-link antigens, causing them to aggregate. This aggregation can enhance opsonization, facilitate phagocytosis, and prevent pathogens from interacting with host cells. We provide a comprehensive product catalogue of research tools for investigating immunoglobulin heavy chains, including IgG antibodies, IgM antibodies, IgA antibodies, IgE antibodies, and IgG1 antibodies. Explore our full immunoglobulin heavy chains product range below and discover more, for less. Alternatively, you can explore our IgG, IgM, and IgA product ranges.