Myc Tag: A Versatile Molecular Tool Driving Innovations in Life Sciences

Myc Tag: A Versatile Molecular Tool Driving Innovations in Life Sciences

 

1. Concept

The Myc tag is a compact 10-amino acid peptide (sequence: EQKLISEEDL) originating from residues 410-419 of the human c-Myc proto-oncoprotein. As a prominent epitope tag in molecular biology, it boasts distinctive structural attributes: a negatively charged and polar N-terminus comprising glutamic acid (E410) and glutamine (Q411); a hydrophobic central core (L414-I415) that confers structural stability; and a C-terminal aspartic acid (D419) enhancing water solubility. With a low molecular weight (~1.2 kDa) and a near-neutral isoelectric point (pI≈4.5), the Myc tag exerts minimal impact on the structure and biological activity of fusion proteins—preserving over 90% of their functionality in most instances. Additionally, it exhibits a half-life of 20-24 hours in mammalian cells and low susceptibility to the ubiquitin-proteasome system, ensuring the stability of labeled proteins.

2. Research Frontiers

Recent advancements in Myc tag technology have focused on optimizing its performance and expanding its application scope. Structural studies via crystallography have revealed that the Myc tag adopts a β-turn conformation upon binding to specific antibodies (e.g., 9E10), with key antigenic epitopes mapped to residues E412, K413, L414, and E417. Antibody development has seen remarkable progress: novel antibodies generated through phage display (such as Myc-Tag[4A6]) offer superior thermal stability (retaining >95% activity after 30 minutes at 60℃) and a broader pH tolerance (pH 4-10) compared to the classic 9E10 monoclonal antibody. Engineered nanobodies (e.g., cAbMyc-1) with a smaller size (~15 kDa) have also emerged, enabling enhanced recognition of Myc-tagged fusion proteins hindered by steric effects.

In live cell imaging, technical breakthroughs include the integration of Myc tags with fluorescent proteins and anti-Myc nanobodies for precise subcellular localization verification (colocalization rate >90%). Super-resolution microscopy techniques like STORM, leveraging the specificity of Myc tag antibodies, achieve localization precision below 20 nm, facilitating the resolution of nanoscale protein arrangements (e.g., postsynaptic density proteins in neurons). The SunTag system, which incorporates 10-24 tandem repeats of the Myc tag, amplifies signal intensity by 5-10 fold, enabling single-molecule tracking. Photoactivatable anti-Myc antibodies (e.g., PA-Tag) further allow temporal (±30 seconds) and spatial (≈5 μm activation diameter) precision in labeling newly synthesized fusion proteins.

In gene therapy and drug delivery, Myc tag technology has opened new avenues. Its integration into AAV vectors enables sensitive tracking of vector expression (3-5 fold more sensitive than traditional Flag tags) without compromising therapeutic protein activity. In CAR-T cell therapy, Myc-tagged safety switches (e.g., iCasp9) facilitate rapid clearance of modified T cells (>90% within 30 minutes) via antibody-induced dimerization, mitigating cytokine storm risks. Myc-labeled exosomes and antibody-transduction domain conjugates have also enhanced targeted drug delivery efficiency and cellular internalization of functional proteins.

3. Research Significance

The Myc tag's unique properties make it an indispensable tool in modern life science research. Its minimal interference with fusion protein function, high specificity, and compatibility with diverse experimental techniques drive progress in protein biology, cell biology, immunology, and precision medicine. By enabling efficient protein purification, accurate subcellular localization, and reliable protein-protein interaction analysis, the Myc tag accelerates the discovery of molecular mechanisms underlying diseases and the development of novel therapeutic strategies. In gene therapy and drug delivery, it addresses critical challenges such as tracking therapeutic agents and improving targeting efficiency, paving the way for more effective and safer clinical interventions.

4. Related Mechanisms, Research Methods, and Product Applications

Mechanisms

The core utility of the Myc tag stems from its specific high-affinity binding to dedicated antibodies. This interaction is mediated by the β-turn conformation of the Myc tag, where key residues (E412, K413, L414, E417) form complementary contacts with the antibody's CDR region. For instance, the 9E10 antibody binds the Myc tag with a dissociation constant (Kd) of ~2.4 nM, primarily recognizing the EQKLISE sequence. Mutations in E412 or L414 abolish this binding, highlighting the specificity of the interaction.

Research Methods and Product Applications

  • Protein Purification: ANT BIO PTE. LTD.'s Myc tag-related products play a pivotal role in immunoaffinity purification. Agarose beads conjugated with anti-Myc antibodies (e.g., 9E10) enable the isolation of target proteins with >95% purity under mild elution conditions (e.g., pH 3.0 glycine buffer or competitive Myc peptide), achieving a recovery rate of 60-80%. Tandem tag systems (e.g., Myc/His6) combine Ni-NTA resin for rough purification and Myc antibody columns for fine purification, yielding >99% purity. Magnetic agarose beads (e.g., Rabbit Anti-Myc Tag Magnetic Agarose) simplify high-throughput workflows, completing purification from cell lysates within 1 hour. These tools are integral to pull-down assays combined with mass spectrometry, the gold standard for identifying low-abundance protein complexes (<100 copies/cell).
  • Immunodetection: ANT BIO PTE. LTD.'s recombinant anti-Myc antibodies (e.g., Myc tag Recombinant Rabbit mAb conjugated to APC, PE-Cy7, or Alexa Fluor® dyes) support diverse detection techniques. Western blotting achieves a detection limit of 0.1-0.5 ng, immunoprecipitation offers >90% binding efficiency, immunofluorescence provides a signal-to-noise ratio >20:1, and flow cytometry detects fusion proteins at >1,000 molecules/cell. These antibodies exhibit <0.1% cross-reactivity with endogenous c-Myc, ensuring reliable results.
  • Live Cell Imaging: Fusing the Myc tag with fluorescent proteins and using ANT BIO PTE. LTD.'s anti-Myc nanobodies enables dual verification of subcellular localization. Codon-optimized Myc variants (e.g., Myc3×) increase expression by 3-5 fold with <5% cytotoxicity, supporting long-term live cell observation. Super-resolution microscopy applications benefit from the high specificity of anti-Myc antibodies, resolving nanoscale protein structures.

5. Brand Mission

ANT BIO PTE. LTD. is committed to empowering the global life science community with high-quality, innovative reagents and tools. Guided by the principles of precision, reliability, and scientific excellence, we strive to develop and provide cutting-edge products—including antibodies, proteins, kits, and general reagents—that accelerate research progress and drive breakthroughs in biology and medicine. Our multi-platform development capabilities, adhering to international certifications such as EU 98/79/EC, ISO9001, and ISO13485, ensure that every product meets the rigorous demands of academic research and industrial applications. We aim to be a trusted partner for researchers worldwide, supporting their pursuit of scientific discovery and the development of life-changing therapies.

6. Related Product List

Product Catalog Number

Product Name

Host

Conjugation

S0B1848

Myc tag Recombinant Rabbit mAb (APC Conjugate) (S-114-13)

-

APC

S0B0383

S-RMab® Myc tag Recombinant Rabbit mAb (S-114-13)

Rabbit

Unconjugated

S0B0615

Myc tag Recombinant Rabbit mAb (PE-Cy7® Conjugate) (S-114-13)

Rabbit

PE-Cy7

S0B0209

Myc tag Recombinant Rabbit mAb (Alexa Fluor® 647 Conjugate) (S-114-13)

Rabbit

Alexa Fluor® 647

S0B1831

Myc tag Recombinant Rabbit mAb (FITC Conjugate) (S-114-13)

Rabbit

FITC

S0B0634

Myc tag Recombinant Rabbit mAb (Alexa Fluor® 488 Conjugate) (S-114-13)

Rabbit

Alexa Fluor® 488

S0B1642

Rabbit Anti-Myc tag agarose beads

Rabbit

Agarose beads

S0B1654

Rabbit Anti-Myc Tag Magnetic Agarose

Rabbit

Magnetic Agarose

7. AI Disclaimer

This article is AI-compiled and interpreted based on the original work. All intellectual property (e.g., images, data) of the original publication shall belong to the journal and the research team. For any infringement, please contact us promptly and we will take immediate action.

 

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