Other Proteins

Human IgG F(ab')2 Fragment Agarose Conjugated is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. Human IgG F(ab')2 molecules lack the Fc portion of Human IgG and therefore receptors that bind Human IgG Fc will not bind Human IgG F(ab')2 molecules. This product possesses the F(ab')2 fragment, recognized by the two F(ab) fragments yielded from the digestion of the antibody below the disulfide bond hinge region followed by agarose conjugation.

Human IgG purified protein (Immunoglobulin G) are antibody molecules. Human IgG is composed of four peptide chains — two heavy chains gamma and two light chains. Human IgG has two antigen binding sites. Other Immunoglobulins may be described in terms of polymers with the IgG structure considered the monomer. Human IgG typically constitutes 75% of serum immunoglobulins. Human IgG molecules are synthesized and secreted by plasma B cells.

Human IgG Fc purified protein is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme papain under controlled conditions of temperature, time and pH. Receptors bind the Fc portion of Human IgG and often this fragment is removed from immunoglobulins to minimize receptor binding and lower background reactivity.

Human IgG F(ab')2 purified protein is a proteolytic fragment of immunoglobulin G (IgG) obtained by limited digestion with the enzyme pepsin under controlled conditions of temperature, time and pH. Human IgG F(ab')2 molecules lack the Fc portion of Human IgG and therefore receptors that bind Human IgG Fc will not bind Human IgG F(ab')2 molecules.

Secreted as part of the adaptive immune response by plasma B cells, immunoglobulin G constitutes 75% of serum immunoglobulins. Immunoglobulin G binds to viruses, bacteria, as well as fungi and facilitates their destruction or neutralization via agglutination (and thereby immobilizing them), activation of the compliment cascade, and opsonization for phagocytosis. The F(ab) fragment is the portion of the antibody that binds to the antigen target. The immunoglobulin Fab also possesses one constant and one variable region of both the heavy and light chain.

Immunoglobulin A is the primary responder in muscosal immunity, and comprises close to 75% of the total immunoglobulin produced. IgA can also be secreted and is protected from degradation by many proteolytic enzymes (which allows it to be secreted along the gastrointestinal tract). Immunoglobulin A only weakly activates the complement system and is not readily opsonized.

Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. Formed from covalently linking 5 immunoglobulins together, the approximate molecular weight of IgM is 900kDa and possesses 10 binding sites (though due to the size of most antigens, not all sites are capable of binding at once). Due to this large size, IgM is typically isolated to the serum.

Human IgM Fab mu is ideal for investigators involved in serum protein component research. IgM is by far the physically largest antibody in the human circulatory system. It is the first antibody to appear in response to initial exposure to antigen. The spleen is the major site of specific IgM production. Distinct heavy chains differ in size and composition; alpha and gamma contain approximately 450 amino acids, while μ and ε have approximately 550 amino acids.

Human IgM (myeloma) Fc5µ fragment consists of only the µ (mu) chain of the Fc fragment. Immunoglobulin M is the largest antibody isotype and the first to be secreted against an initial exposure to antigen. IgM is predominantly produced in the spleen. IgM is formed from covalently linking 5 immunoglobulins together. Due to this large size, IgM is typically isolated to the serum.