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Recombinant proteins

Power your functional assays with high-purity recombinant proteins engineered for maximum bioactivity and ultra-low endotoxin levels across multiple expression systems. Part of a specialized portfolio of over 15,000 proteins and cell lines with 7,000+ citations, these reagents deliver the consistency required for reliable experimental results.

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Table of contents

Validated bioactivity proteins

Optimal bioactivity proteins

Expression systems

About recombinant proteins

Recombinant proteins are laboratory-produced proteins generated by expressing a target gene in a host system such as mammalian, bacterial, or insect cells. They are widely used in life science research to study protein function, enable assays, and ensure consistent, reproducible experimental outcomes.

Our recombinant proteins are engineered for consistency, purity, and biological relevance. Choose from validated, bioactive, ultra-pure formats optimized for sensitive assays and functional studies. With multiple expression systems, including mammalian, E. coli, and insect, you can select the right protein for your workflow needs.

Every product is rigorously tested to ensure low endotoxin levels, correct folding, and reproducible results. This quality control helps reduce variability and supports faster progression from experiment to insight, particularly in demanding or high-sensitivity applications.

Explore the functional potential of high-quality recombinant proteins across diverse research applications, including assay development, pathway analysis, and drug discovery workflows.

Validated bioactivity proteins

Select recombinant proteins with validated bioactivity for reliable biological research outcomes. Produced across multiple expression systems, these proteins combine high purity with low endotoxin levels, ensuring consistent performance in functional assays and cell-based studies.

Optimal bioactivity proteins

Choose ultra-high-purity recombinant proteins for critical experiments where precise bioactivity and minimal endotoxin contamination are essential. These proteins are suitable for highly sensitive applications and include detailed validation data confirming protein size, structure, and purity.

Expression systems

Choose from a range of expression systems tailored to your research needs, including mammalian, E. coli, and insect-based platforms. Each system is optimized to balance protein yield, folding accuracy, and biological functionality, enabling flexibility across different experimental requirements.

Our recombinant proteins are engineered for purity, activity, and low endotoxin levels, making them suitable for even the most sensitive applications. Validated using advanced analytical techniques such as LC/MS, these proteins reduce experimental variability and minimize the need for reruns.

Available in flexible formats and quantities, these recombinant proteins support a wide range of workflows, from high-throughput screening to focused mechanistic studies. This ensures dependable, reproducible results across experiments and accelerates progress in life science research.

Expression system
Key advantages
Consideration
Best use case
Mammalian
Native folding, post-translational modifications
Lower yield, higher cost
Functional studies, therapeutic research
E. coli
High yield, fast, cost-effective
Limited folding, no complex PTMs
Screening assays, non-complex proteins
Insect
Balanced folding and yield
Moderate cost and complexity
Protein production requiring some PTMs

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References

1. Gasser B. et al. Protein folding and conformational stress in microbial cells producing recombinant proteins. Microb Cell Fact. 2008. (PMCID: PMC2322954)

2. Kamoshida G. et al. Development of endotoxin-free recombinant protein production systems. PNAS Nexus. 2024.

3. Ojima-Kato T. Advances in recombinant protein production in microorganisms. Biosci Biotechnol Biochem. 2025.

4. Rosano GL. & Ceccarelli EA. Recombinant protein expression in E. coli: advances and challenges. Microb Cell Fact. 2025.

5. Nature Scientific Reports (2022) – Endotoxin contamination in recombinant protein production.