Lysosomal-Associated Membrane Protein 2 (LAMP2) antibody

Details for Product No. ABIN317432
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Antigen
Synonyms cd107b, lamp-2, lampb, LAMP2, lamp2, DKFZp459J126, LAMP-2, LGP-B, CD107b, Lamp-2, Lamp-2a, Lamp-2b, Lamp-2c, Mac3, LAMPB, LGP110
Reactivity
Dog (Canine), Human, Mink
(128), (116), (25), (18), (13), (13), (7), (1)
Host
Mouse
(92), (85), (51), (1)
Clonality (Clone)
Monoclonal ()
Conjugate
Un-conjugated
(32), (21), (16), (11), (5), (5), (3), (3), (2), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1), (1)
Application
Immunoelectron Microscopy (IEM), Flow Cytometry (FACS), Immunofluorescence (IF), Immunoprecipitation (IP), Western Blotting (WB)
(100), (99), (54), (51), (48), (41), (30), (29), (28), (10), (2), (2), (2), (1), (1)
Pubmed 5 references available
Quantity 0.25 mg
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Catalog No. ABIN317432
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Immunogen MDCK (Madin-Darby Canine Kidney) cells. Spleen cells from immunised Balb/c mice were fused with cells of the NS1 myeloma cellline.
Clone AC17
Isotype IgG1
Specificity This antibody recognises canine CD107b, otherwise known as LAMP-2, a 95 kDa heavily-glycosylated type I integral lysosomal glycoprotein, shown to share high N-terminal amino acid sequence homology with Human, Mouse and Rat CD107b. 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 (Nabi et 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 (Nabi et 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 (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 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 (Hariri et 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 (Saitoh et al. 1992).
Characteristics Synonyms: LAMP-2, LAMP-2C, LAMPB, Lysosome-associated membrane glycoprotein 2
Purification Purified IgG prepared by affinity chromatography on Protein G from tissue culture supernatant
Alternative Name CD107b / LAMP2
Background Lysosomes are membrane-bound organelles found within the cytoplasm of most cells, which 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. 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 tumour cells and their metastatic potential.Synonyms: LAMP-2, LAMP-2C, LAMPB, Lysosome-associated membrane glycoprotein 2
Gene ID 3920
UniProt P13473
Research Area CD Antigens, Surface Receptors of Immune Cells
Application Notes Flow Cytometry (Membrane permeabilisation is required). Immunoprecipitation. Western blot: 1/100-1/500. Immunofluorescence. Clone AC17 has been shown as suitable for use in Electron Microscopy (See Ref.1).
Other applications not tested.
Optimal dilutions are dependent on conditions and should be determined by the user.
Restrictions For Research Use only
Concentration 1.0 mg/mL
Buffer Phosphate buffered saline pH 7.4, 0.09 % Sodium Azide
Preservative Sodium azide
Precaution of Use This product contains sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage 4 °C/-20 °C
Storage Comment Store the antibody undiluted at 2-8 °C for one month or (in aliquots) at -20 °C for longer. Avoid repeated freezing and thawing. Should this product contain a precipitate werecommend microcentrifugation before use.
Shelf life: one year from despatch.
Expiry Date 12 months
Background publications Nabi, Le Bivic, Fambrough et al.: "An endogenous MDCK lysosomal membrane glycoprotein is targeted basolaterally before delivery to lysosomes." in: The Journal of cell biology, Vol. 115, Issue 6, pp. 1573-84, 1992 (PubMed).

Fukuda: "Lysosomal membrane glycoproteins. Structure, biosynthesis, and intracellular trafficking." in: The Journal of biological chemistry, Vol. 266, Issue 32, pp. 21327-30, 1991 (PubMed).

Nabi, Rodriguez-Boulan: "Increased LAMP-2 polylactosamine glycosylation is associated with its slower Golgi transit during establishment of a polarized MDCK epithelial monolayer." in: Molecular biology of the cell, Vol. 4, Issue 6, pp. 627-35, 1993 (PubMed).

Jou, Leung, Fung et al.: "Selective alterations in biosynthetic and endocytic protein traffic in Madin-Darby canine kidney epithelial cells expressing mutants of the small GTPase Rac1." in: Molecular biology of the cell, Vol. 11, Issue 1, pp. 287-304, 2000 (PubMed).

Ihrke, Bruns, Luzio et al.: "Competing sorting signals guide endolyn along a novel route to lysosomes in MDCK cells." in: The EMBO journal, Vol. 20, Issue 22, pp. 6256-64, 2001 (PubMed).

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