While "GLP6 Antibody" is not widely documented, antibodies in general, also known as immunoglobulins (Ig), are Y-shaped proteins utilized by the immune system to identify and neutralize foreign substances like bacteria and viruses . Each antibody recognizes specific antigens, which prompts the creation of antigen-specific antibodies . The tips of the antibody's "Y" contain a paratope that binds to an epitope on an antigen, facilitating precise binding . Antibodies can tag microbes or infected cells for immune system attack or neutralize them by blocking essential parts of viruses .
Antibodies are large proteins, approximately 150 kDa in size, with a Y-shaped structure formed by three globular regions .
Key structural features include:
Polypeptide Chains In humans and other mammals, an antibody unit consists of two identical heavy chains and two identical light chains linked by disulfide bonds .
Domains Each chain comprises a series of domains, which are similar sequences of about 110 amino acids each . Light chains have one variable domain $$V_L$$ and one constant domain $$C_L$$, while heavy chains have one variable domain $$V_H$$ and three to four constant domains $$C_{H1}, C_{H2}$$, etc .
Fragments An antibody is partitioned into two antigen-binding fragments (Fab), each containing one $$V_L$$, $$V_H$$, $$C_L$$, and $$C_{H1}$$ domain, and a crystallisable fragment (Fc) that forms the base of the Y shape .
Hinge Region A flexible hinge region between the Fab and Fc fragments allows antibodies to bind to epitopes at various distances and facilitates the formation of complexes .
Glucagon-like peptide-1 (GLP-1) enhances glucose-dependent insulin secretion by binding to GLP-1 receptors (GLP1Rs) on pancreatic beta cells . GLP-1 receptor antibodies can be developed to antagonize or block GLP-1R signaling .
Glp1R0017 A monoclonal antagonistic antibody to the GLP1R, Glp1R0017, has been shown to bind to GLP1R on pancreatic beta cells and block the actions of GLP-1 in vivo . This antibody has the potential for use in studying the physiological importance of GLP1R signaling in extrapancreatic tissues . In vitro, Glp1R0017 antagonized mouse, human, rat, cynomolgus monkey, and dog GLP1R, and attenuated GLP-1-stimulated cAMP and insulin secretion in INS-1 832/3 cells . In vivo, it reversed the glucose-lowering effect of liraglutide and reduced glucose tolerance by blocking endogenous GLP-1 action .
Generalized Myasthenia Gravis (gMG) gMG is a chronic, rare, autoantibody-driven disease affecting an estimated 700,000 people worldwide . Nipocalimab, a fully human IgG1 antibody, has demonstrated a reduction in autoantibody levels, one of the underlying causes of gMG .
Autoantibody Diseases Nipocalimab is being investigated as a therapy to lower immunoglobulin G (IgG), including pathogenic IgG, one of the root causes of autoantibody diseases . It has shown a reduction in levels of common pathogenic IgG subclasses, including AChR antibody and MuSK antibody, without changes in total IgE, IgA, and IgM .
A monoclonal antibody of the IgG class can be prepared against rat liver glucose-6-phosphate dehydrogenase (G6PD) . The antibody does not affect the catalytic activity of the enzyme and shows crossreactivity with the palmitoyl CoA-inactivated G6PD . Such antibodies facilitate the isolation and characterization of inactive G6PD variants, which is valuable in studying metabolic regulation .
KEGG: ath:AT5G39100
UniGene: At.24199