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Anti-TRPML1 (Mucolipin 1) Antibody

Mcoln1, Mucolipidin

Cat #: ACC-081
Alternative Name Mcoln1, Mucolipidin
Lyophilized Powder yes
Type: Polyclonal
Host: Rabbit
Reactivity: h, m, r
Immunogen
  • Peptide (C)GRRASETERLLTPN, corresponding to amino acid residues 6-19 of mouse TRPLM1 (Accession Q99J21). Intracellular, N-terminus (cytoplasmic).
Accession (Uniprot) Number Q99J21
Gene ID 94178
Peptide confirmation Confirmed by amino acid analysis and mass spectrometry.
Homology Human, rat - 12/14 amino acid residues identical.
RRID AB_10915894.
Purity Affinity purified on immobilized antigen.
Form Lyophilized powder. Reconstituted antibody contains phosphate buffered saline (PBS), pH 7.4, 1% BSA, 0.05% NaN3.
Isotype Rabbit IgG.
Storage before reconstitution The antibody ships as a lyophilized powder at room temperature. Upon arrival, it should be stored at -20°C.
Reconstitution 25 µl, 50 µl or 0.2 ml double distilled water (DDW), depending on the sample size.
Antibody concentration after reconstitution 0.8 mg/ml.
Storage after reconstitution The reconstituted solution can be stored at 4°C for up to 1 week. For longer periods, small aliquots should be stored at -20°C. Avoid multiple freezing and thawing. Centrifuge all antibody preparations before use (10000 x g 5 min).
Standard quality control of each lot Western blot analysis.
Applications: wb
May also work in: ic*, ifc*, ih*, ip*
Western blot
  • Western blot analysis of rat kidney (lanes 1 and 2) and HEK-293 cells (lanes 3 and 4) lysates:
    Western blot analysis of rat kidney (lanes 1 and 2) and HEK-293 cells (lanes 3 and 4) lysates:
    1,3. Anti-TRPML1 (Mucolipin 1) Antibody (#ACC-081), (1:200).
    2,4. Anti-TRPML1 (Mucolipin 1) Antibody, preincubated with TRPML1/Mucolipin 1 Blocking Peptide (#BLP-CC081).
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, 79.
  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.
Scientific background

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.

Application key:

CBE- Cell-based ELISA, FC- Flow cytometry, ICC- Immunocytochemistry, IE- Indirect ELISA, IF- Immunofluorescence, IFC- Indirect flow cytometry, IHC- Immunohistochemistry, IP- Immunoprecipitation, LCI- Live cell imaging, N- Neutralization, WB- Western blot

Species reactivity key:

H- Human, M- Mouse, R- Rat
Last update: 11/04/2021

Alomone Labs is pleased to offer a highly specific antibody directed against an epitope of mouse TRPML1. Anti-TRPML1 (Mucolipin 1) Antibody (#ACC-081) can be used in western blot analysis. It has been designed to recognize TRPML1 from human, rat and mouse samples.

For research purposes only, not for human use

Applications

Specifications

Scientific Background

Citations

Citations
Western blot citations
  1. Mouse NSC-34 motor neuron cell lysate (1:1000). Tested in siRNA-treated cells.
    Tedeschi Vet al. (2019) Sci Rep9, 10743.
Immunoprecipitation citations
  1. Mouse NSC-34 motor neuron cell lysate (1:200).
    Tedeschi Vet al. (2019) Sci Rep9, 10743.
Immunocytochemistry citations
  1. Mouse NSC-34 motor neuron cells (1:1000). Tested in siRNA-treated cells.
    Tedeschi Vet al. (2019) Sci Rep9, 10743.
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