LAMP1/CD107a Protein, Mouse (HEK293, His)

LAMP1/CD107a, a lysosomal membrane glycoprotein, assumes a crucial role in lysosome biogenesis, lysosomal pH regulation, autophagy, and cholesterol homeostasis. It serves as a direct inhibitor of the proton channel TMEM175, playing a pivotal role in lysosomal lumen pH regulation and facilitating optimal lysosomal acidification for efficient hydrolase activity. Additionally, LAMP1 is integral to NK-cell cytotoxicity, participating in cytotoxic granule movement to the cell surface and perforin trafficking to the lytic granule. Remarkably, it safeguards NK-cells from degranulation-associated damage induced by their own cytotoxic granule content. LAMP1's involvement in presenting carbohydrate ligands to selectins, its role in tumor cell metastasis, and its interactions with proteins such as ABCB9 and FURIN underscore its multifaceted contributions to cellular processes. Notably, the interaction with TMEM175 highlights its inhibitory role in the proton channel activity of TMEM175, further emphasizing its regulatory function in lysosomal processes.