Anti-LAMP2 Antibody

Plays an important role in chaperone-mediated autophagy, a process that mediates lysosomal degradation of proteins in response to various stresses and as part of the normal turnover of proteins with a long biological half-live (PubMed:10972293). Functions by binding target proteins, such as GAPDH and MLLT11, and targeting them for lysosomal degradation (By similarity). Required for the fusion of autophagosomes with lysosomes during autophagy (PubMed:27628032). Cells that lack LAMP2 express normal levels of VAMP8, but fail to accumulate STX17 on autophagosomes, which is the most likely explanation for the lack of fusion between autophagosomes and lysosomes (PubMed:27628032). Required for normal degradation of the contents of autophagosomes (PubMed:10972293, PubMed:12221139). Plays a role in lysosomal protein degradation in response to starvation (PubMed:27628032). Required for efficient MHCII-mediated presentation of exogenous antigens via its function in lysosomal protein degradation; antigenic peptides generated by proteases in the endosomal/lysosomal compartment are captured by nascent MHCII subunits. Is not required for efficient MHCII-mediated presentation of endogenous antigens (By similarity). {UniProtKB:P13473, UniProtKB:P17046, PubMed:10972293, PubMed:12221139, PubMed:27628032}.

Immunoblotting: Use at 1-2ug/mL. A band of ~100-110kDa (glycosylated) is detected. <br><br>Immunofluorescence: Use at 1-2ug/mL. This antibody labels lysosomes and late endosomes in cells permeabilized with saponin. <br><br>These are recommended concentrations. <br><br>Enduser should determine optimal concentrations for their application.

Lysosome-associated membrane proteins (LAMP1 and LAMP2) are major constituents of the lysosomal membrane. These two proteins have closely related structures with 37% sequence homology. Both are transmembrane glycoproteins localized primarily in lysosomes and late endosomes. LAMP2 has also been detected at the plasma membrane of cells undergoing differentiation and activation and in cells that secrete lysosomal hydrolases. Cell surface LAMP1 and LAMP2 promote adhesion of human peripheral blood mononuclear cells (PBMC) to vascular endothelium which suggests that the LAMP proteins are involved in adhesion of PBMC to sites of inflammation. Defects in LAMP2 are associated with Danon disease.