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>   home   >   Products   >   Primary Antibodies   >   Anti-Dog CD107b Antibody, clone AC17 (FITC)   

Anti-Dog CD107b Antibody, clone AC17

Mouse Anti-Dog Monoclonal Antibody

  • FC - Anti-Dog CD107b Antibody, clone AC17  ABD12302
    Peripheral dog granulocytes stained with Mouse anti Dog CD107b:RPE following permeabilisation with Leucoperm®
Product Information
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
Reactivity Dog
Host Mouse
Clonality Monoclonal
Isotype IgG1
Clone Names AC17
Additional Information
Other Species ,Mink,H
Purification Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Immunogen MDCK (Madin-Darby Canine Kidney) cells.
Shelf Life 18 months from date of despatch.
Target/Specificity Mouse anti-Dog CD107b antibody, clone AC17 is a monoclonal antibody specific for canine CD107b, otherwise known as lysosome-associated membrane protein 2 or LAMP-2. Immunofluorescence staining of MDCK cells with Mouse anti-Canine CD107b 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 (Nabiet al.1991).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 (Nabiet al.1991) indicate 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 (Nabiet 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 and expressing 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 (Haririet al.2000). Evidence shows that CD107b is involved in the lysosomal uptake of cytosolic proteins and the endocytic pathway and human studies have revealed a correlation between the level of surface expression of CD107b on tumor cells and their metastatic potential (Saitohet al.1992).Clone AC17 has been shown as suitable for use in electron microscopy (Nabiet al.1991).
Preservative & Stabilisers 0.09% Sodium Azide
Storage Store at +4℃ or at -20 ℃.
PrecautionsAnti-Dog CD107b Antibody, clone AC17 is for research use only and not for use in diagnostic or therapeutic procedures.
Citations (0)

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1. Nabi, I.R. et al. (1991) An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes.
J Cell Biol. 115 (6): 1573-84. 2. Nabi, I.R. & Rodriguez-Boulan, E. (1993) Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer.
Mol Biol Cell. 4 (6): 627-35. 3. Jou, T.S. et al. (2000) Selective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac1.
Mol Biol Cell. 11 (1): 287-304. 4. Ihrke, G. et al. (2001) Competing sorting signals guide endolyn along a novel route to lysosomes in MDCK cells.
EMBO J. 20 (22): 6256-64. 5. Pluhar, G.E. et al. (2010) Anti-tumor immune response correlates with neurological symptoms in a dog with spontaneous astrocytoma treated by gene and vaccine therapy.
Vaccine. 28 (19): 3371-8. 6. Cliffe, S.T. et al. (2009) SLC29A3 gene is mutated in pigmented hypertrichosis with insulin-dependent diabetes mellitus syndrome and interacts with the insulin signaling pathway.
Hum Mol Genet. 18: 2257-65. 7. Bai, Y. et al. (2011) Intracellular neutralization of viral infection in polarized epithelial cells by neonatal Fc receptor (FcRn)-mediated IgG transport.
Proc Natl Acad Sci U S A. 108 (45): 18406-11. 8. Nagahama, M. et al. (2011) Cellular vacuolation induced by Clostridium perfringensepsilon-toxin.
FEBS J. 278: 3395-407. 9. Nagahama, M. et al. (2012) Intracellular trafficking of Clostridium perfringens iota-toxin b.
Infect Immun. 80: 3410-6. 10. Hariri, M. et al. (2000) Biogenesis of multilamellar bodies via autophagy.
Mol Biol Cell. 11: 255-68.1. Fukuda, M. (1991) Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking.
J Biol Chem. 266 (32): 21327-30.

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Cat# ABD12302
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