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MCOLN1 Antibody (C-term) Blocking peptide
Synthetic peptide
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | Q9GZU1 |
|---|---|
| Clone Names | 100427292 |
| Gene ID | 57192 |
|---|---|
| Other Names | Mucolipin-1, MG-2, Mucolipidin, MCOLN1, ML4 |
| Target/Specificity | The synthetic peptide sequence used to generate the antibody AP13551b was selected from the C-term region of MCOLN1. A 10 to 100 fold molar excess to antibody is recommended. Precise conditions should be optimized for a particular assay. |
| Format | Peptides are lyophilized in a solid powder format. Peptides can be reconstituted in solution using the appropriate buffer as needed. |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C. |
| Precautions | This product is for research use only. Not for use in diagnostic or therapeutic procedures. |
| Name | MCOLN1 {ECO:0000303|PubMed:25720963, ECO:0000312|HGNC:HGNC:13356} |
|---|---|
| Function | Nonselective cation channel probably playing a role in the regulation of membrane trafficking events and of metal homeostasis (PubMed:11013137, PubMed:12459486, PubMed:15336987, PubMed:14749347, PubMed:29019983, PubMed:27623384). Proposed to play a major role in Ca(2+) release from late endosome and lysosome vesicles to the cytoplasm, which is important for many lysosome-dependent cellular events, including the fusion and trafficking of these organelles, exocytosis and autophagy (PubMed:11013137, PubMed:12459486, PubMed:15336987, PubMed:14749347, PubMed:25720963, PubMed:29019983, PubMed:27623384). Required for efficient uptake of large particles in macrophages in which Ca(2+) release from the lysosomes triggers lysosomal exocytosis. May also play a role in phagosome-lysosome fusion (By similarity). Involved in lactosylceramide trafficking indicative for a role in the regulation of late endocytic membrane fusion/fission events (PubMed:16978393). By mediating lysosomal Ca(2+) release is involved in regulation of mTORC1 signaling and in mTOR/TFEB-dependent lysosomal adaptation to environmental cues such as nutrient levels (PubMed:25720963, PubMed:25733853, PubMed:27787197). Seems to act as lysosomal active oxygen species (ROS) sensor involved in ROS-induced TFEB activation and autophagy (PubMed:27357649). Functions as a Fe(2+) permeable channel in late endosomes and lysosomes (PubMed:18794901). Proposed to play a role in zinc homeostasis probably implicating its association with TMEM163 (PubMed:25130899) In adaptive immunity, TRPML2 and TRPML1 may play redundant roles in the function of the specialized lysosomes of B cells (By similarity). |
| Cellular Location | Late endosome membrane; Multi-pass membrane protein. Lysosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle membrane; Multi-pass membrane protein. Cell projection, phagocytic cup {ECO:0000250|UniProtKB:Q99J21}. Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:Q99J21}; Multi-pass membrane protein. Cell membrane; Multi-pass membrane protein. Note=Delivery from the trans-Golgi to lysosomes seems to occur mainly in a direct intracellular manner without intermediate delivery to the plasma membrane (PubMed:16497227) Under normal conditions, restricted to intracellular compartments so that only a very minor proportion is present at the cell membrane (PubMed:12459486, PubMed:18794901, PubMed:28112729, PubMed:29019983) |
| Tissue Location | Widely expressed in adult and fetal tissues. |
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Provided below are standard protocols that you may find useful for product applications.
Background
This gene encodes a memberof the transient receptorpotential (TRP) cation channel gene family. The transmembraneprotein localizes to intracellular vesicular membranes includinglysosomes, and functions in the late endocytic pathway and in theregulation of lysosomal exocytosis. The channel is permeable toCa(2+), Fe(2+), Na(+), K(+), and H(+), and is modulated by changesin Ca(2+) concentration. Mutations in this gene result inmucolipidosis type IV.
References
Eichelsdoerfer, J.L., et al. J. Biol. Chem. 285(45):34304-34308(2010)Curcio-Morelli, C., et al. J. Cell. Physiol. 222(2):328-335(2010)Vergarajauregui, S., et al. J. Biol. Chem. 284(52):36357-36366(2009)Ballif, B.A., et al. Mol. Cell Proteomics 3(11):1093-1101(2004)LaPlante, J.M., et al. FEBS Lett. 532 (1-2), 183-187 (2002) :
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