References |
Synonyms |
- Lysosome Associated Membrane Proteins 2
|
Formulation |
Protein G-purified IgG at a concentration of 1 mg/ml in TBS, containing 0.09% sodium azide and 50% glycerol |
Stability |
1 year |
Storage |
-20°C |
Shipping |
Wet ice
in continental US; may vary elsewhere
|
Specificity |
Murine LAMP2 |
+ |
Rabbit LAMP2 |
+ |
|
Background Reading
Granger, B.L., Green, S.A., Gabel, C.A., et al. Characterization and cloning of lgp110, a lysosomal membrane glycoprotein from mouse and rat cells. J Biol Chem 265(20) 12036-12043 (1990).
Tanaka, Y., Guhde, G., Suter, A., et al. Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Nature 406 902-906 (2000).
Kannan, K., Stewart, R.M., Bounds, W., 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. Cell Immunol 171(1) 10-19 (1996).
Grützkau, A., Smorodchenko, A., Lippert, U., et al. LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells. Cytometry A 61(1) 62-68 (2004).
Lichter-Konecki, U., Moter, S.E., Krawisz, B.R., et al. Expression patterns of murine lysome-associated membrane protein 2 (Lamp-2) transcripts during morphogenesis. Differentiation 65(1) 43-58 (1999).
Rohrer, J., Schweizer, A., Russel, D., et al. The targeting of lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J Cell Biol 132(4) 565-576 (1996).
Höning, S., Sandoval, I.V., and von Figura, K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J 17(5) 1304-1314 (1998).
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Size |
Global Purchasing |
25 µg |
|
100 µg |
|
Description
Antigen:
purified preparation of murine liver lysosomal membranes
·
Clone designation:
clone GL2A7
·
Host:
rat
·
Isotype:
IgG1
·
Application(s):
IP and ICC
·
Lysosome associated membrane protein 1 (LAMP1) and LAMP2 are major constituents of the lysosomal membrane. The two have closley related structures, with 37% sequence homology.1 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.2 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 expression 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.3 Upon stimulation, a rapid translocation of intracellular LAMPs to the cell membrane is dependent on a carboxyl-terminal tyrosine based motif (YXXI).4 This stimulation has also been shown to have an associated release of histamine, leukotriene C4 and prostaglandin D2, which shows that LAMP1 and LAMP2 are activation markers for normal mast cells.4 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.5 LAMP2 has also been shown to be critical for autophagy, in conversion of early autophagic vacuoles to vacuoles which rapidly degrade their content.6
1
Höning, S., Sandoval, I.V., and von Figura, K. A di-leucine-based motif in the cytoplasmic tail of LIMP-II and tyrosinase mediates selective binding of AP-3. EMBO J 17(5) 1304-1314 (1998).
2
Rohrer, J., Schweizer, A., Russel, D., et al. The targeting of lamp1 to lysosomes is dependent on the spacing of its cytoplasmic tail tyrosine sorting motif relative to the membrane. J Cell Biol 132(4) 565-576 (1996).
3
Lichter-Konecki, U., Moter, S.E., Krawisz, B.R., et al. Expression patterns of murine lysome-associated membrane protein 2 (Lamp-2) transcripts during morphogenesis. Differentiation 65(1) 43-58 (1999).
4
Grützkau, A., Smorodchenko, A., Lippert, U., et al. LAMP-1 and LAMP-2, but not LAMP-3, are reliable markers for activation-induced secretion of human mast cells. Cytometry A 61(1) 62-68 (2004).
5
Kannan, K., Stewart, R.M., Bounds, W., 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. Cell Immunol 171(1) 10-19 (1996).
6
Tanaka, Y., Guhde, G., Suter, A., et al. Accumulation of autophagic vacuoles and cardiomyopathy in LAMP-2-deficient mice. Nature 406 902-906 (2000).
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