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SCN4A

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

Background

Sodium voltage-gated channel alpha subunit 4 (SCN4A) is an indispensable skeletal muscle-specific voltage-gated sodium channel encoded by the SCN4A gene, belonging to voltage-gated sodium channel superfamily and acting as the core effector of skeletal muscle action potential initiation and sarcolemmal electrical excitability. SCN4A is selectively enriched in skeletal muscle sarcolemma membranes, carrying evolutionarily conserved four-transmembrane-domain architecture and voltage-sensing modules across species, serving as an essential modulator for rapid sodium influx upon membrane depolarization and muscle contractile signal propagation. SCN4A-mediated sodium permeation exerts decisive effects on triggering muscle electrical signals and coordinating synchronous fiber contraction under physiological conditions. Furthermore, SCN4A coordinates downstream ion balance cascades governing muscle fiber homeostasis and sarcolemmal signal stability to sustain intact neuromuscular transmission. Distinct from neuronal sodium channel paralogs with tissue-restricted expression, SCN4A carries unique non-redundant functions in skeletal muscle electrogenesis, rendering it irreplaceable for normal muscle contraction and neuromuscular signal transmission.

SCN4A executes biological functions via conformational rearrangement triggered by membrane potential shifts, opening intramembrane sodium pores to drive rapid cation inward flux and generate regenerative muscle action potentials for long-distance contractile signal delivery. Its conserved voltage-sensing and pore-forming domains enable precise tuning of muscle firing threshold and electrical signal kinetics, maintaining balanced sarcolemmal excitability. SCN4A participates in an extensive spectrum of biological processes, including muscle action potential generation, sarcolemmal ion homeostasis, neuromuscular junction signal relay and skeletal fiber maturation. Mutations or dysfunction of SCN4A severely disrupt muscle electrical excitability, impair contractile signaling and raise susceptibility to hereditary myopathic disorders, including periodic paralysis and myotonia syndromes. Therefore, SCN4A constitutes a pivotal research target for skeletal muscle electrophysiology and hereditary neuromuscular disease mechanisms.

Fig. 1 Nav1.4 domain topology, auxiliary protein binding sites and disease mutation hotspots for recombinant antigen & mutant protein development. (OA Literature)Fig. 1 Linear topological architecture of human Nav1.4 (SCN4A) channel with four homologous domains (DI–DIV); mapped disease-causing mutation hotspots for hypokalemic periodic paralysis, congenital myopathy and myotonia, plus binding interfaces for Navβ1, ankyrin, calmodulin and syntrophin. Panel B displays positively charged arginine residues within S4 voltage-sensing helices across all four domains.1

SCN4A Protein Function: Core Roles in Skeletal Muscle Electrogenesis and Sarcolemmal Excitability

The biological functions of SCN4A are focused on voltage-sensing domain gating and sarcolemmal sodium permeation to drive muscle electrical signaling:

  • Voltage-Dependent Sodium Influx: Opens cation pores upon membrane depolarization to mediate rapid sodium entry into muscle fibers.
  • Muscle Action Potential Initiation: Generates regenerative electrical signals to propagate contractile commands across sarcolemma.
  • Neuromuscular Signal Relay: Transduces junction-derived electrical inputs to coordinate synchronous skeletal fiber contraction.
  • Sarcolemmal Ion Homeostasis: Stabilizes resting membrane potential to maintain balanced muscle excitability threshold.
  • Disease Relevance: Functional variants induce abnormal muscle firing patterns, triggering myotonia and periodic paralytic disorders.

SCN4A Protein Product

Creative Biolabs offers high-quality SCN4A proteins via optimized expression systems, covering full-length SCN4A and isolated voltage-sensing domain variants. These products are suitable for sarcolemmal electrophysiology, ion channel interaction and myopathy-targeted small molecule screening. All SCN4A proteins undergo rigorous quality control to guarantee consistent functional performance and reliable application across diverse research platforms.

SCN4A Protein Product

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

SCN4A Stable Cell Line Product

Creative Biolabs provides custom engineered SCN4A stable cell lines, including overexpression and gene silencing models. These cell lines are optimized for skeletal ion channel electrophysiology and myopathy phenotype research. Each cell line undergoes strict validation procedures to ensure steady target expression levels and uniform functional performance across multiple experimental scenarios.

SCN4A Stable Cell Line Product

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

SCN4A Recombinant Antibody Product

High-specificity recombinant antibodies targeting SCN4A are developed with advanced antibody engineering workflows, without cross-reactivity against other voltage-gated sodium channel isoforms. These antibodies receive multi-scenario functional validation, applicable to muscle membrane localization, channel expression profiling and ion channel interaction assessment, enabling precise characterization of SCN4A expression patterns under physiological and pathological states.

SCN4A Recombinant Antibody Product

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

Product Features

  • Native Sodium Conductance Activity: Preserves endogenous voltage gating and cation permeation function, supporting accurate skeletal muscle electrophysiology research.
  • Sodium Channel Isoform Specificity: Validated for exclusive SCN4A epitope recognition and stable membrane binding, delivering repeatable experimental readouts.
  • Neuromuscular Research Compatibility: Optimized for muscle excitability detection and myopathy therapeutic compound screening.
  • Comprehensive Customization Support: Facilitates end-to-end development of customized proteins, antibodies and stable cell lines to address skeletal ion channel research requirements.

Custom SCN4A Research Services

Beyond catalog products, Creative Biolabs offers specialized custom services for SCN4A research:

  • Custom SCN4A Protein Production: Tailored expression of SCN4A sequence variants and domain-truncated constructs for ion conductance research.
  • Custom Antibody Development: Generation of SCN4A-specific antibodies for sarcolemmal localization and channel expression analysis.
  • Stable Cell Line Engineering: Custom SCN4A-modified cell models for neuromuscular disorder functional research.
  • Functional Assay Development: Design of voltage-gated sodium flux and muscle excitability detection assays.

Frequently Asked Questions (FAQ)

  1. What is the primary function of SCN4A?

    SCN4A is a skeletal muscle voltage-gated sodium channel that mediates sarcolemmal sodium influx to generate muscle action potentials and sustain neuromuscular excitability.

  2. Why is SCN4A a significant research target?

    SCN4A is the sole major sodium channel of skeletal muscle; its pathogenic variants alter fiber excitability and cause hereditary myopathies, establishing it as a vital research target.

  3. Are Creative Biolabs' SCN4A products suitable for clinical use?

    No, all SCN4A products and services are strictly for research use only, not intended for clinical diagnosis or treatment.

  4. What types of SCN4A products does Creative Biolabs offer?

    Offerings include SCN4A proteins, high-specificity recombinant antibodies and custom stable cell lines for skeletal ion channel and myopathy research.

  5. How are SCN4A proteins validated for activity?

    SCN4A proteins undergo functional verification via sodium conductance and voltage gating capacity evaluation.

Reference
  1. Nicole, Sophie, and Philippe Lory. "New challenges resulting from the loss of function of Nav1. 4 in neuromuscular diseases." Frontiers in Pharmacology 12 (2021): 751095. Under Open Access license CC BY 4.0, without modification. https://doi.org/10.3389/fphar.2021.751095
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