Anti-Human IgG1 (Clone HP6001)- PE (I-1217-100ug)

Humans produce five classes of immunoglobulins, IgM, IgD, IgA, IgE, and IgG1. IgG is the most abundant class1 and functions in the humoral immune response2. There are four subclasses of IgG, and they are numbered according to decreasing abundance as IgG1 through IgG4. The four subclasses are highly conserved and consist of four polypeptide chains: two identical heavy chains and two identical light chains1. While the general structure is very similar between IgG subclasses, differences in their constant regions in the hinge and upper CH2 domain as well as in glycosylation affect their binding to antigens (e.g. pathogenic proteins, polysaccharides, allergens), C1q and Fc receptors, leading to differences in functionality. As a result, each IgG subclass has a unique response skewed to specific antigens. IgG1 is the most abundant subclass of IgG and is primarily induced by soluble protein antigens and membrane proteins1. For example, IgG1 can bind Haemophilus influenzae b polysaccharide during infection. IgG1 induces effector mechanisms when engaged by antigens via C1q complement activation. IgG1 also interacts with most FcγR. IgG1 has three main allelic isoforms: G1m (z,a), G1m(f), and G1m(f,a). HP6001 was generated by immunizing a BALB/c mouse with purified human immunoglobulin3. Spleen cells were fused with Sp2/0-Ag14 myeloma cells. The HP6001 binding epitope resides in the CH2 domain4.