LAMP2/CD107b Protein, Human (HEK293, His)

LAMP2, a lysosomal membrane glycoprotein, assumes a pivotal role in lysosome biogenesis, lysosomal pH regulation, and autophagy. It acts as a crucial regulator of lysosomal lumen pH by directly inhibiting the proton channel TMEM175, facilitating optimal lysosomal acidification for effective hydrolase activity. LAMP2 plays a significant role in chaperone-mediated autophagy, participating in the lysosomal degradation of proteins during various stresses and as part of the normal turnover of long-lived proteins. This function involves binding target proteins such as GAPDH, NLRP3, and MLLT11 and directing them for lysosomal degradation. In chaperone-mediated autophagy, LAMP2 operates downstream of chaperones like HSPA8/HSC70, which recognize and bind substrate proteins, mediating their recruitment to lysosomes where LAMP2 facilitates binding. Furthermore, LAMP2 is essential for the fusion of autophagosomes with lysosomes during autophagy, influencing the degradation of autophagosomal contents. Additionally, LAMP2 is required for the efficient presentation of exogenous antigens via MHCII-mediated pathways, as it modulates chaperone-mediated autophagy and decreases the presentation of endogenous antigens by MHCII, highlighting its multifaceted roles in cellular processes.