Mucolipin-1 (F8F9Q) Rabbit mAb #27748
- WB
- IP
- IF
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 35-40, 65 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
- IF-Immunofluorescence
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:200 |
| Immunofluorescence (Immunocytochemistry) | 1:200 - 1:800 |
Storage
Protocol
Specificity / Sensitivity
Mucolipin-1 (F8F9Q) Rabbit mAb recognizes endogenous levels of total mucolipin-1 protein. This antibody detects the carboxyl terminal fragment produced following posttranslational cleavage.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues near the carboxy terminus of human mucolipin-1 protein.
Background
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).
- Zeevi, D.A. et al. (2007) Biochim Biophys Acta 1772, 851-8.
- Cheng, X. et al. (2010) FEBS Lett 584, 2013-21.
- Mirabelli-Badenier, M. et al. (2015) Metab Brain Dis 30, 681-6.
- Kiselyov, K. et al. (2005) J Biol Chem 280, 43218-23.
- Miedel, M.T. et al. (2006) J Biol Chem 281, 12751-9.
- Scotto Rosato, A. et al. (2019) Nat Commun 10, 5630.
- Zhang, X. et al. (2016) Nat Commun 7, 12109.
- Zhang, X. et al. (2016) Autophagy 12, 1954-1955.
- Onyenwoke, R.U. et al. (2015) Biochem J 470, 331-42.
- Yin, C. et al. (2019) Cancer Manag Res 11, 8607-8617.
- Xu, M. et al. (2019) Cell Calcium 79, 80-88.
- Yang, Y. et al. (2020) Cells 9, 2682-2688.
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