mouse monoclonal IgG1; MPO light chain Antibody (A-5) is an IgG1 κ mouse monoclonal MPO light chain antibody (also designated Myeloperoxidase expressing neutrophil granulocyte marker antibody, Myeloid differentiation peroxidase 15 kDa light chain antibody, neutrophil azurophilic granule marker MPO antibody, or 15 kDa Myeloperoxidase (MPO) light chain subunit antibody) that detects the MPO light chain protein of human origin by WB, IP, IF, IHC(P) and ELISA. MPO light chain Antibody (A-5) is available as both the non-conjugated anti-MPO light chain antibody form, as well as multiple conjugated forms of anti-MPO light chain antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. The heme protein myeloperoxidase (MPO) is a major component of azurophilic granules of neutrophils and polymorphonuclear leukocytes. Optimal oxygen-dependent microbiocidal activity depends on MPO as the critical enzyme for the generation of hypochlorous acid and other toxic oxygen products. The MPO precursor is synthesized during the promyelocytic stage of myeloid differentiation and is subsequently processed and transported intracellularly to the lysosomes. The precursor undergoes cotranslational N-linked glycosylation to produce a glycoprotein. Glucosidases in the endoplasmic reticulum (ER) or early cis Golgi convert the pro-MPO to a form which is sorted into a prelysosomal compartment, which undergoes final proteolytic maturation to native MPO, a pair of heavy-light protomers. In normal neutrophils, MPO is expressed as a dimer. Calreticulin, a calcium-binding protein residing in the ER, interacts specifically with fully glycosylated apopro-MPO. iMPO mRNA is abundant in human promyelocytic HL-60 and mouse myeloid leukemia NFS-60 cells. MPO is expressed at high levels in circulating neutrophils and monocytes but is not detectable in microglia, brain-specific macrophages or normal brain tissue.