|Reactivity||Human, Mouse, Rat|
|Calculated MW||65506 Da|
|Homology||Human, rat- 12/14 amino acid residues identical.|
|Other Names||Mucolipin-1, Mucolipidin, Mcoln1|
|Related products for control experiments||Control peptide antigen (supplied with the antibody free of charge).|
|Target/Specificity||Peptide (C)GRRASETERLLTPN, corresponding to amino acid residuesֲ 6-19 of mouse TRPLM1 (Accession Q99J21). Intracellular, N-terminus (cytoplasmic).|
|Peptide Confirmation||Confirmed by amino acid analysis.|
|Format||Affinity purified antibody, lyophilized powder|
|Reconstitution||50 µl or 0.2 ml deionized water, depending on the sample size.|
|Antibody Concentration After Reconstitution||0.8 mg/ml.|
|Buffer After Reconstitution||Phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.|
|Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Storage After Reconstitution||The reconstituted solution can be stored at 4ºC for up to 2 weeks. For longer periods, small aliquots should be stored at -20ºC or below. Avoid multiple freezing and thawing. The further dilutions should be made using a carrier protein such as BSA (1%). Centrifuge all antibody preparations before use (10000 × g 5 min).|
|Control Antigen Storage Before Reconstitution||Lyophilized powder can be stored intact at room temperature for several weeks. For longer periods, it should be stored at -20°C.|
|Control Antigen Reconstitution||100 µl water.|
|Control Antigen Storage After Reconstitution||-20ºC.|
|Preadsorption Control||1 µg peptide per 1 µg antibody.|
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Provided below are standard protocols that you may find useful for product applications.
The endolysosome system takes part in important cellular functions such as membrane trafficking, protein transport, autophagy and signal transduction1. Endosomes result from endocytosis of the plasma membrane and lysosomes (which are derived from late endosomes) conatin mainly hydrolytic enzymes and generally have a low internal pH1. Like the endoplasmic reticulum (ER), endolysosomes also store Ca2+ (luminal Ca2+ concentration: 0.5 mM)1,2, and similarly to Ca2+ release from the ER, Ca2+ from endolysosomes may also play an important role in various signaling events. To date such candidates include members of the TRP super-family of ion channels and the two-pore Ca2+ channels (TPCs)1,3,4. TRPMLs, also termed mucolipins, are members of the TRP channels. In mammals, three TRPMLs are known to date (TRPML1-3 or MCOLN1-3). They are all localized to endolysosomes, although when over expressed in heterologous systems, TRPML3 is found on the plasma membrane1,5. These channels are Ca2+ permeable and display inward rectifying current properties1,5. Like all members of this family, TRPMLs have six transmembrane domains and intracellular N- and C-termini (relatively short tails compared to other members). They are characterized by an exceptionally large extracellular (luminal) loop between transmembrane domains 1 and 2, and N-glycosylation sites are present in the first extracellular (luminal) loop5. In mammals, TRPML1 is expressed in a ubiquitous manner and shows highest expression in the brain, kidney, spleen, liver and heart1,6. TRPML2 and TRPML3 are less widely expressed. Interestingly, in mouse, two splice variants exist for TRPML2. The shorter variant is more broadly expressed and is dominant over the longer variant in the thymus, spleen and kidney1,7. TRPML3 is highly detected in the thymus, lung, kidney, spleen and eye1,7,8, some epithelial cells1,9 and brain10. Pathologies related to these channels include type IV mucolipidosis, a neurodegenetative disease characterized by retardation and retinal degeneration caused by a loss of function mutation in the gene encoding TRPML1. In contrast, a gain of function mutation in TRPML3, in mice, causes deafness, and pigmentation defects11. Abgent is pleased to offer a highly specific antibody directed against an epitope of mouse TRPML1. Anti-TRPML1 antibody (#AG1330) can be used in western blot analysis. It has been designed to recognize TRPML1 from human, rat and mouse samples.
References 1. Cheng, X. et al. (2010) FEBS Lett. 584, 2013. 2. Christensen, K.A. et al. (2002) Curr. Opin. Cell. Biol. 17, 135. 3. Lange, I. et al. (2009) Sci. Signal. 2, ra23. 4. Calcraft, P.J. et al. (2009) Nature 459, 596. 5. Puertollano, R. and Kiselyov, K. (2009) Am. J. Physiol. 296, F1245. 6. Sun, M. et al. (2000) Hum. Mol. Genet. 9, 2471. 7. Samie, M.A. et al. (2009) Pflugers Arch. 459, 463. 8. Cuajungco, M.P. et al. (2008) Pflugers Arch. 457, 463. 9. Nagata, K. et al. (2008) Proc. Natl. Acad. Sci. U.S.A. 105, 353. 10. Kim, H.J. et al. (2007) J. Biol. Chem. 282, 36138. 11. Di Palma, F. et al. (2002) Proc. Natl. Acad. Sci. U.S.A. 99, 14994.
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