Mucolipin-1 (F8F9Q) Rabbit mAb recognizes endogenous levels of total mucolipin-1 protein. This antibody detects the carboxyl terminal fragment produced following posttranslational cleavage.

Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human mucolipin-1 protein.

Mucolipin-1 (MCOLN1, TRPML1), a member of the transient receptor potential ion channel superfamily, is a lysosomal/late endosome Ca²⁺ efflux channel that is important in lysosomal biogenesis (1,2). Mutations in the mucolipin-1 gene are responsible for the human lysosomal storage disease mucolipidosis type IV (MLIV), an autosomal recessive neurodegenerative disease (3). Mucolipin-1 is synthesized as a 580-amino acid protein with six transmembrane domains but can undergo cleavage in the long luminal loop between the first two transmembrane domains (4,5). Mucolipin-1 activity has been linked to autophagy and lysosomal biogenesis. Calcium influx through mucolipin-1 activates CaMKKβ and AMPK, which activate the autophagy kinase ULK1 (6). Calcium influx is also associated with activation of the calcium-dependent phosphatase calcineurin which can trigger activation of TFEB, a key transcription factor regulating autophagy and lysosomal biogenesis (7,8). Mucolipin-1 activity is upregulated by cellular stress, including reactive oxygen species (ROS) (7). Phosphorylation of mucolipin-1 by mTOR results in reduced channel activity and autophagic flux (9). Loss of mucolipin-1 or pharmacological inhibition suppresses autophagy and can reduce tumor growth and metastasis in non-small cell lung cancer and triple-negative breast cancer, suggesting the use of mucolipin-1 antagonists for cancer therapy (10-12).