MOUSE ANTI DOG CD107b: RPE Antibody from MyBioSource.com

Mouse anti Dog CD107b antibody, clone AC17 recognizes canine CD107b, otherwise known as lysosome-associated membrane protein 2 or LAMP-2. Immunofluorescence staining of MDCK cells with mouse anti dog CD107b, clone AC17 demonstrates staining patterns consistent with localization to lysozomes. This is supported by coincident staining of an exogenous lysozomal glycoprotein, avian LEP100 transfected into MDCK cells and detected using the anti LEP100 antibody clone CV24 (Nabi et al.1991).
Mouse anti Dog CD107b antibody, clone AC17 immunoprecipitates a protein of ~95 kDa in MDCK cells which, following Endo F digestion to remove N-linked oligosaccharides, yields a core protein product of 40 kDa, indicating the heavily glycosylated nature of CD107b. The molecular weight of canine CD107b is typical of many lysozome-associated membrane proteins. While most (97%) CD107b resides in the lysozomal environment in adherent MDCK cells in vitro, early studies (Nabi et al.1991) indicated that a small percentage of total cellular CD107b, as revealed by radioimmune assay with clone AC17, is found associated with the cell membrane.
Lysosomes are membrane-bound organelles found within the cytoplasm of most cells, they contain hydrolytic enzymes and act as the major compartment for heterophagic and autophagic digestion. Members of the lysosomal-associated membrane protein family (LAMPS) are believed to play an important role in protecting the lysosomal membrane from protease degradation and are involved in lectin-mediated cell adhesion. CD107b has been shown to share high N-terminal amino acid sequence homology with human, mouse and rat CD107b (Nabi et al.1993).
Transfection of a mink type II lung epithelial cell line with beta1-6-N-acetylglucosaminyl transferase V demonstrates the formation of large lysozomal vacuoles, termed multilamellar bodies (MLBs), having a very distinct phenotype with expression of CD107b, as indicated by immunofluorescent staining with clone AC17. These MLBs require lysozomal degradation via an autophagic pathway for their formation and may have implications for lysozomal storage diseases (Hariri et al.2000). Evidence shows that CD107b is involved in the lysosomal uptake of cytosolic proteins and the endocytic pathway. Human studies have revealed a correlation between the level of surface expression of CD107b on tumor cells and their metastatic potential (Saitoh et al. 1992).
Mouse anti Dog CD107b antibody, clone AC17 has been shown as suitable for use in electron microscopy (Nabi et al.1991)