FLAG Peptide Powder

FLAG Peptide Powder GMP Manufacturer in China | High-Purity DYKDDDDK Epitope Tag Peptide Supplier for Protein Expression & Affinity Purification

Key Product Highlights

• Specific DYKDDDDK epitope for accurate protein identification and purification
•  High hydrophilicity maintains native protein folding and biological activity
•  Enables mild non-denaturing elution to recover active fusion proteins
• Zero endogenous homology ensures ultra-low background interference
• Enterokinase cleavable design for precise tag excision

FLAG Peptide Powder is a synthetic hydrophilic octapeptide epitope tag with the amino acid sequence DYKDDDDK.It is one of the most widely used epitope tagging systems in molecular biology for recombinant protein expression, detection, affinity purification, and protein–protein interaction studies.

This product is supplied as a white to off-white lyophilized powder manufactured under strict GMP standards, using Fmoc solid-phase peptide synthesis (SPPS), followed by multi-step preparative HPLC purification, desalting, and sterile lyophilization.

Truncated sequences, deletion peptides, and isomeric impurities are strictly controlled to ensure high batch reproducibility and minimal experimental background interference.

1. Why Does It Provide Extremely Low Background Signal?

FLAG peptide is an artificial epitope sequence with no known homologs in common biological systems, minimizing non-specific antibody binding and reducing experimental background noise.

2. How Does It Preserve Native Protein Conformation?

Its short and highly hydrophilic structure does not interfere with protein folding, assembly, or biological activity, ensuring native-like protein conformation is maintained.

3. Why Is It Suitable for Non-Denaturing Elution?

It enables competitive elution under mild, non-denaturing buffer conditions, allowing recovery of functionally active proteins.

4. How Does It Enable Precise Tag Removal?

An enterokinase recognition sequence allows site-specific enzymatic cleavage, enabling removal of the FLAG tag and recovery of near-native target protein.

5. Why Is It Highly Versatile in Molecular Biology?

It is compatible with N-terminal and C-terminal fusion constructs and widely used in Western blotting, immunoprecipitation, co-immunoprecipitation, affinity chromatography, and ELISA assays.

6. Why Is It Suitable for Reproducible Research?

Standardized synthesis and purification processes ensure consistent physicochemical properties and high batch-to-batch reproducibility.

• Recombinant protein expression validation
• Western blot detection systems
• Affinity purification of FLAG-tagged proteins
• Immunoprecipitation and protein interaction studies
• Structural biology and protein engineering research
• Molecular biology reagent development

1. How Does It Enable Specific Antibody Recognition?

The DYKDDDDK sequence functions as a highly specific epitope recognized by anti-FLAG monoclonal antibodies (e.g., M2), enabling selective detection of tagged proteins.

2. How Does Competitive Elution Work?

Free FLAG peptide competitively binds to anti-FLAG antibodies immobilized on affinity resins, displacing FLAG-tagged proteins under mild conditions without denaturation.

3. How Does Enzymatic Tag Removal Work?

Enterokinase specifically cleaves the recognition sequence, removing the FLAG tag while preserving the structural integrity of the target protein.

4. Why Does It Not Disrupt Protein Folding?

Its small size and hydrophilic nature prevent interference with protein tertiary structure, folding pathways, and biological activity.

• GMP-certified cleanroom manufacturing environment
• Strict raw material qualification and supplier audit system
• Full batch traceability across all production stages
• Long-term and accelerated stability
• Optional third-party analytical verification available

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