LAMP2/CD107b Protein, Mouse (HEK293, His)

LAMP2/CD107b protein, a lysosomal membrane glycoprotein, plays a crucial role in lysosome biogenesis, lysosomal pH regulation, and autophagy. Acting as a direct inhibitor of the proton channel TMEM175, LAMP2 facilitates lysosomal acidification, optimizing hydrolase activity. Additionally, it is a key regulator of chaperone-mediated autophagy, binding target proteins like GAPDH, NLRP3, and MLLT11, and guiding them for lysosomal degradation. Functioning downstream of chaperones such as HSPA8/HSC70, LAMP2 aids in the recruitment of substrate proteins to lysosomes. LAMP2 is vital for lysosomal protein degradation in response to starvation and is essential for the fusion of autophagosomes with lysosomes during autophagy. Its absence leads to impaired fusion and inefficient degradation of autophagic contents. Furthermore, LAMP2 contributes to MHCII-mediated presentation of exogenous antigens. Structurally, LAMP2 exists as a monomer and forms large homooligomers, interacting with proteins like HSPA8, HSP90, MLLT11, ABCB9, FURIN, and TMEM175 to execute its diverse cellular functions.