Close
Loading...
CONTACT US
:
:
:
Call us at:
:
:
:
Fax:
Email:

TRPML1

Products

Loading...

All listed services and products are For Research Use Only. Do Not use in any diagnostic or therapeutic applications.

Background

MCOLN1/TRPML1 is a six-transmembrane endolysosomal cation channel encoded by MCOLN1. Tetrameric assembly within lysosomal compartments is required for channel activity; channel gating is directly modulated by lysosomal PI(3,5)P₂, while luminal pH and membrane lipids act as auxiliary regulatory factors under distinct cellular states. This channel protein can be detected across multiple epithelial and secretory cell groups with abundant lysosomal structures.

The protein mediates cation efflux from lysosomal compartments to cytoplasmic regions, regulating a series of downstream signaling events associated with intracellular membrane transport and autophagic progression. Cation release via assembled TRPML1 complexes may activate the calcineurin-TFEB signaling cascade, which can modulate transcriptional programs linked to lysosomal biogenesis and intracellular substance clearance. Complete tetramer assembly is necessary to maintain steady cation transfer across lysosomal boundary structures.

Perturbation of MCOLN1 expression or channel functionality may disrupt lysosomal cation balance and substance degradation, which has been associated with abnormal intracellular substrate accumulation in relevant pathological models. In existing research, this channel serves as a common research target for exploring lysosomal ion transport and autophagy-related biological processes.

Fig. 1 Schematic of lysosomal ion related signaling networks, highlighting conserved TRPML1 TFEB axis for lysosomal homeostasis and autophagy research with TRPML1 reagents. (OA Literature)Fig. 1 Schematic of lysosomal ion‑dependent signaling networks. The TRPML1‑driven cation efflux‑calcineurin‑TFEB cascade facilitates lysosomal biogenesis and autophagic turnover.1

TRPML1 Protein Function: Recorded Biological Roles in Lysosomal Channel Assembly and Cation Balance

The documented biological activities of TRPML1 center on lysosomal channel complex formation, intracellular cation signal transmission and cellular metabolic equilibrium:

  • Regulation of lysosomal channel assembly: it can assemble on lysosomal membrane to form a cation permeable tetramer functional structure, stably maintain the steady state of cation gradient in lysosomal cavity, and accurately regulate the activation intensity of downstream lysosomal degradation signal pathway, which is a classic lysosomal regulation mechanism confirmed by literature.
  • Lysosomal cascade signal modulation: relying on the mature TRPML1 functional complex on the membrane to mediate the cation outflow in lysosomes, start the intracellular multi-level signal cascade reaction, reshape the lysosomal function-related transcription program, and dynamically regulate the overall degradation response level of cells.
  • Intracellular cation homeostasis maintenance: continuously support the efficient operation of lysosomal substance clearance pathway, coordinate and control the decomposition and turnover process of intracellular metabolic substrates, and ensure the orderly progress of cell basic metabolism homeostasis.
  • Regulation of cellular metabolic function: by regulating the signal response mode of pH-dependent lysosomes, the clearance efficiency of intracellular aging substances and metabolic residues can be stably maintained, and the metabolic balance in the intracellular environment can be maintained.
  • Correlation characteristics of pathological research: There is obvious abnormal expression of TRPML1 in lysosomal storage disease model, and it is highly coupled with the accumulation phenotype of intracellular undegraded substrates, which is the classic core target for the study of lysosomal ion signal mechanism and metabolic disorder.

TRPML1 Protein Product

Creative Biolabs offers purified TRPML1 membrane samples via standardized expression workflows, including full-length MCOLN1/TRPML1 constructs and isolated luminal structural variants with modified glycosylation profiles. Isolated luminal structural fragments cannot form complete transmembrane assemblies and do not sustain cation permeability or autophagy-/TFEB related regulatory behaviors. Full-length constructs can be applied to lysosomal ion transport research, while truncated fragments fit structural and binding-related research projects. All samples undergo standardized internal quality screening; assessments targeting channel-associated behaviors are conducted exclusively with full-length constructs in simulated lysosomal membrane environments.

TRPML1 Membrane Protein Product

Not finding the membrane protein product you need? Contact us to start your one-stop custom service!

TRPML1 Stable Cell Line Product

Creative Biolabs provides customizable cell models with modified TRPML1 expression levels, applicable to research exploring channel assembly, lysosomal signal cascades and lysosomal regulatory molecule screening. Sample characterization covers steady expression identification and general channel function assessment.

TRPML1 Stable Cell Line Product

Not finding the stable cell line product you need? Contact us to start your one-stop custom service!

TRPML1 Recombinant Antibody Product

TRPML1 Recombinant Antibody Product

Not finding the recombinant antibody product you need? Contact us to start your one-stop custom service!

Product Features

  • Channel Assembly Binding Compatibility: Retains native spatial conformation of TRPML1, suited for laboratory analysis of endogenous lysosomal cation transport and degradative signaling pathways.
  • Lysosomal Channel Binding Compatibility: Interacts specifically with characteristic structural regions of TRPML1, suitable for research focused on lysosomal cation signaling mechanisms.
  • Lysosomal Storage Research Adaptability: Designed for laboratory analysis of lysosomal clearance regulatory pathways in standard cell research models.
  • Full Customization Support: Customized TRPML1 membrane protein, antibody and cell model development can be arranged to match diverse lysosomal transport research demands.

Custom TRPML1 Research Services

Beyond standard catalog reagents, Creative Biolabs offers tailored analytical support centered on TRPML1 related laboratory exploration:

  • Custom Membrane Protein Preparation: Custom expression of modified TRPML1 constructs, including functionally deficient variants and tagged protein formats.
  • Custom Antibody Generation: Development of antibodies targeting TRPML1 for localization and channel complex analytical workflows.
  • Custom Cell Model Construction: Generation of cell systems with adjusted TRPML1 expression levels for channel assembly and signal output analysis.
  • Custom Analytical Assay Design: Custom detection workflows for lysosomal cation transfer and autophagy signal measurement.

Frequently Asked Questions (FAQ)

  1. What is the primary function of TRPML1?

    TRPML1 is an endolysosomal mucolipin TRP cation channel subunit that forms tetrameric channels in endolysosomal and lysosomal limiting membranes to regulate ion flux, maintain lysosomal homeostasis, and support autophagic cargo processing and clearance following PI(3,5)P₂-dependent channel activation.

  2. Why is TRPML1 a significant research target?

    TRPML1 serves as a major regulatory mediator of lysosomal metal homeostasis and autophagic degradative signaling; its dysfunction drives intracellular substrate buildup and lysosomal storage lesions, rendering it a vital research object for lysosomal TRP channel and metabolic disorder investigations.

  3. Are Creative Biolabs' TRPML1 products suitable for clinical use?

    No, all TRPML1 products and services are strictly for research use only, not intended for clinical diagnosis or treatment.

  4. What types of TRPML1 products does Creative Biolabs offer?

    Offerings include TRPML1 proteins (full-length, luminal pore domain variants), specific recombinant antibodies, and custom stable cell research models, supporting lysosomal metal transport and storage disorder research.

  5. How are TRPML1 proteins analyzed for channel activity?

    Laboratory analytical workflows cover TRPML channel oligomer binding assays and tests measuring lysosomal clearance signal regulation, to assess native channel performance in lysosomal transport research.

Reference
  1. Abuammar, Hussein, et al. "Ion channels and pumps in autophagy: a reciprocal relationship." Cells 10.12 (2021): 3537. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.3390/cells10123537
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us
© 2026 Creative Biolabs. | Contact Us
;