LAMP2 is encoded by the LAMP2 gene, which is located on the X chromosome in both humans and mice . The protein itself is a type I membrane glycoprotein, meaning it has a single transmembrane domain with a large luminal domain and a short cytoplasmic tail . The luminal domain is heavily glycosylated, which is essential for its function and stability .
LAMP2 has several critical functions within the cell:
Lysosomal Protection: LAMP2 protects the lysosomal membrane from the proteolytic enzymes contained within the lysosome . This is vital for maintaining the integrity of the lysosome and preventing the release of these enzymes into the cytoplasm, which could cause cellular damage.
Autophagy: LAMP2 plays a significant role in chaperone-mediated autophagy, a process that selectively degrades cytosolic proteins in the lysosome . It binds to target proteins and facilitates their translocation into the lysosome for degradation.
Lysosomal pH Regulation: LAMP2 is involved in regulating the pH within the lysosome by acting as a direct inhibitor of the proton channel TMEM175, which is crucial for lysosomal acidification and optimal hydrolase activity .
Cell Adhesion and Metastasis: LAMP2 provides selectins with carbohydrate ligands, which may play a role in tumor cell metastasis . This function highlights its potential involvement in cancer biology.
Recombinant LAMP2 (Mouse) is produced using recombinant DNA technology, which involves inserting the LAMP2 gene into an expression system, such as bacteria or mammalian cells, to produce the protein in vitro. This recombinant protein can be used in various research applications, including studies on lysosomal function, autophagy, and disease mechanisms.