Anti-PYGL antibodies are used in the immunodetection of the protein glycogen phosphorylase L. In humans, the canonical protein has a reported length of 847 amino acid residues and a mass of 97.1 kDa. Its subcellular localization is in the cytoplasm. Up to 2 different isoforms have been reported for this protein. It is notably expressed in many tissues, such as the bone marrow and liver. A member of the Glycogen phosphorylase protein family, PYGL is reported to be an allosteric enzyme that catalyzes the rate-limiting step in glycogen catabolism, the phosphorolytic cleavage of glycogen to produce glucose-1-phosphate, and plays a central role in maintaining cellular and organismal glucose homeostasis. Post-translational modifications have been described, including acetylation and phosphorylation. Synonyms for this target antigen include glycogen phosphorylase, liver form, phosphorylase, glycogen, liver, and GSD6. PYGL gene orthologs have been reported in the mouse, rat, bovine, frog, zebrafish, chimpanzee and chicken species.