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Lysosomal-Associated Membrane Protein 2 (LAMP2) antibody
|Synonyms||LAMPB, CD107b, LGP110, Mac3, Lamp-2, Lamp-2a, Lamp-2b, Lamp-2c, MGC82091, LAMP2, MGC127297, lamp2, DKFZp459J126|
Mouse (Murine), Rabbit
Alternatives Immunoprecipitation (IP), Immunocytochemistry (ICC)
|7 references available|
|Price||207.90 $ Plus shipping costs $45.00|
|Availability||Will be delivered in 3 to 4 Business Days|
|Immunogen||Purified preparation of mouse liver lysosomal membranes|
Lysosme associated membrane proteins, or LAMP1 and LAMP2, are major constituents of the lysosomal membrane. The two have closely related structures, with 37% sequence homology. They are both transmembrane glycoproteins that are localized primarily in lysosomes and late endosomes. Newly synthesized molecules are mostly transported from the trans-Golgi network directly to endosomes and then to lysosomes. A second pathway involves the lamps being delivered from the Golgi to the cell surface, and then along the endocytic pathway to the lysosomes. A minor pathway involves transport via the plasma membrane.LAMP2 has also been detected at the plasma membrane of cells, as well as in cells that secrete lysosomal hydrolases. A study in the developmental expresses patterns of membrane LAMP2 transcripts indicate a possible involvement of this protein in cell-cell or cell-extracellular matrix interaction, and appear to reflect tissue and cell type specific roles of lysosomes during morphogenesis. Upon stimulation, a rapid translocation of intracellular LAMPs to the cell membrane is dependent on a carboxyl-terminal tyrosine based motif (YXXI). This stimulation has also been shown to have an associated release of histamine, leukotriene C 9) and prostaglandin D 9), which shows that LAMP1 and LAMP2 are activation markers for normal mast cells. They have also been linked to the inflammatory response in that they promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium, and therefore possibly the adhesion of PBMC to the site of inflammation. LAMP2 has also been shown to be critical for autophagy, in conversion of early autophagic vacuoles to vacuoles which rapidly degrade their content.
Synonyms: CD107b, Igp110, Igp2, Lamp2C, LampB, MAC3
|Characteristics||Accession Number: NP_001017959.1|
|Specificity||Recommended for use in ICC. The antibody will label the presumptive lysosomes and late endosomes in cells that have been permeabilized with saponin.|
|Application Notes||1:500- 1:1000 (ICC)|
|Purification||Protein G Purified|
|Buffer||PBS, 50% glycerol|
|Storage||Store at -20° C. Shipping Conditions: Blue Ice or 4° C|
|Storage Shipping Temp Max||Blue Ice or 4 °C|
|Research Area||Chaperones, Organelles, Stem Cells, Hematopoietic Progenitors, Autophagy, Metabolism|
|Restrictions||For Research Use only|
|LAMP2 (GL2A7), IF showing distribution of lysosomes in CEC Courtesy of Eunduck E P Kay, Doheny Eye Institue.|
Granger, Green, Gabel et al.: "Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells." in: The Journal of biological chemistry, Vol. 265, Issue 20, pp. 12036-43, 1990 (PubMed).
Rohrer, Schweizer, Russell et al.: "The targeting of Lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane." in: The Journal of cell biology, Vol. 132, Issue 4, pp. 565-76, 1996 (PubMed).
Kannan, Stewart, Bounds et al.: "Lysosome-associated membrane proteins h-LAMP1 (CD107a) and h-LAMP2 (CD107b) are activation-dependent cell surface glycoproteins in human peripheral blood mononuclear cells which mediate cell adhesion to vascular endothelium." in: Cellular immunology, Vol. 171, Issue 1, pp. 10-9, 1996 (PubMed).
Hoening, Sandoval, von Figura: "A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3." in: The EMBO journal, Vol. 17, Issue 5, pp. 1304-14, 1998 (PubMed).
Lichter-Konecki, Moter, Krawisz et al.: "Expression patterns of murine lysosome-associated membrane protein 2 (Lamp-2) transcripts during morphogenesis." in: Differentiation; research in biological diversity, Vol. 65, Issue 1, pp. 43-58, 1999 (PubMed).
Tanaka, Guhde, Suter et al.: "Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice." in: Nature, Vol. 406, Issue 6798, pp. 902-6, 2000 (PubMed).
Gruetzkau, Smorodchenko, Lippert et al.: "LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells." in: Cytometry. Part A : the journal of the International Society for Analytical Cytology, Vol. 61, Issue 1, pp. 62-8, 2004 (PubMed).
|Hosts||Rat (60), Rabbit (48), Mouse (34), Goat (1)|
|Reactivities||Mouse (Murine) (80), Human (69), Rat (Rattus) (23), Dog (Canine) (20), Cow (Bovine) (14), Horse (Equine) (13), Pig (Porcine) (13), Rabbit (3), Cat (Feline) (1), Chicken (1)|
|Applications||Flow Cytometry (FACS) (80), Western Blotting (WB) (48), Immunoprecipitation (IP) (31), Immunofluorescence (IF) (27), ELISA (25), Immunocytochemistry (ICC) (19), Immunohistochemistry (IHC) (18), Immunohistochemistry (Paraffin-embedded Sections) (IHC (p)) (16), Immunohistochemistry (Fixed) (IHC (fx)) (12), Immunohistochemistry (Frozen Sections) (IHC (fro)) (7), Immunoelectron Microscopy (IEM) (3), Immunohistochemistry (Formalin-fixed Sections) (IHC (f)) (3)|
|Conjugates||FITC (26), Biotin (17), PE (9), APC (5), RPE (2), SPRD (2), Cy3 (1), Cy5 (1), Cy5,PE (1), Cy5.5 (1), Cy7 (1), Gold (1), HRP (1), PE,Cy3 (1), PE,Cy5 (1), PE,Cy7 (1)|
|Epitopes||C-Term (5), AA 29-192 (2), Internal Region (2), AA 400-411 (1), Center (1)|