Custom Protein Production

High-Quality Recombinant Protein Production

From gene synthesis to protein purification—accelerate your research with our comprehensive custom protein expression platforms. Multiple expression systems available: E. coli, Mammalian, Insect, and Cell-Free.

Multiple Systems

High Success Rate

Purity >95%

View Specifications

Trusted by leading research and pharmaceutical institutions

MIT

Pfizer

Stanford

Roche

Johns Hopkins

Merck

Why Choose Us

Multiple expression platforms

Comprehensive QC included

Expert technical consultation

Scalable from μg to kg

Gene Optimization

Professional codon optimization

Multiple Systems

E. coli, CHO, HEK293, Insect

Advanced Purification

Multi-step chromatography

Success Rate

High

Service Overview

Complete Gene-to-Protein Solutions

Industry-leading protein expression services tailored to your research needs.

Gene Synthesis & Optimization

Professional codon optimization and gene synthesis to maximize expression efficiency. Our algorithms ensure optimal translation in your chosen expression system.

Codon usage optimization
GC content balancing
mRNA structure minimization

Multiple Expression Platforms

Choose from E. coli, Mammalian (CHO/HEK293), Insect (Baculovirus), or Cell-Free systems. Each optimized for specific protein types and applications.

E. coli for rapid production
Mammalian for complex PTMs
Insect for large proteins

E. coli Expression

Rapid, cost-effective production for simple proteins.

Mammalian Systems

CHO and HEK293 for human-like PTMs.

Insect Cells

Baculovirus system for complex proteins.

Cell-Free Systems

Fast delivery for toxic proteins.

Technology Platform

Advanced Expression Technologies

Cutting-edge platforms optimized for maximum protein yield and quality.

E. coli Expression

Rapid expression with proven efficiency for bacterial, antigen, and cytokine proteins.

4-6 Weeks Cost-Effective

Mammalian Systems

CHO and HEK293 for human-like post-translational modifications and superior bioactivity.

6-10 Weeks Full PTMs

Baculovirus-Insect

Sf9, Sf21, and Hi-5 cell lines for complex eukaryotic proteins and structural biology.

8-12 Weeks Large Proteins

Cell-Free Expression

Ultra-fast delivery bypassing cellular limitations. Perfect for toxic proteins and screening.

5-7 Days Rapid

Quality Control

SDS-PAGE Purity analysis

SEC-HPLC Aggregate detection

MS Mass spectrometry verification

COA Certificate of Analysis included

Purification Options

Affinity His, Flag, GST, MBP tags

IEX Ion exchange chromatography

SEC Size exclusion polishing

HIC Hydrophobic interaction

Parameter	E. coli	Mammalian (CHO/HEK)	Baculovirus-Insect	Cell-Free
Production Scale	μg to kg	μg to kg	μg to g	μg to mg
Post-Translational Modifications	Limited	Full human-like	Mammalian-like	Defined
Glycosylation	None	Complex N-glycans	Simple N-glycans	Limited
Disulfide Bonds	Periplasmic/specialized strains	Yes	Yes	Yes (controlled)
Cost Efficiency	High	Medium	Medium-High	Medium

Parameter

E. coli

Mammalian (CHO/HEK)

Baculovirus-Insect

Cell-Free

Production Scale

μg to kg

μg to g

μg to mg

Post-Translational Modifications

Limited

Full human-like

Mammalian-like

Defined

Glycosylation

None

Complex N-glycans

Simple N-glycans

Limited

Disulfide Bonds

Periplasmic/specialized strains

Yes

Yes (controlled)

Cost Efficiency

High

Medium

Medium-High

Medium

Applications

Wide Range of Applications

Solutions for research, therapeutic, and industrial needs.

Research Applications

Comprehensive solutions for academic and industrial research projects requiring recombinant proteins.

Structural biology studies (X-ray, Cryo-EM)
Functional assays and binding studies
Antibody generation and validation
Enzyme characterization and optimization

10K+

Projects Delivered

Therapeutic Development

GMP-ready production for preclinical and clinical development of therapeutic proteins.

Antibody and Fc fusion proteins
Cytokines and growth factors
Vaccine antigens and virus-like particles
Biosimilar development support

GMP

Manufacturing Ready

Diagnostics

High-purity proteins for diagnostic reagent development and quality control.

ELISA standards and controls
Immunohistochemistry reagents
Lateral flow assay components
Reference standards for QC

>95%

Purity Guaranteed

Testimonials

What Our Clients Say

Trusted by researchers worldwide for quality and reliability.

"Their mammalian expression system delivered exceptional results for our membrane protein project. The protein was properly folded and functional for our Cryo-EM studies."

Principal Scientist

Biotechnology Company

"We've been using their E. coli service for over 3 years. Consistent quality, excellent technical support, and they always meet their timelines."

Research Director

Academic Research Institution

"The cell-free expression option saved us weeks on our toxic protein project. Fast, efficient, and the purity exceeded our expectations."

Lead Researcher

Pharmaceutical Company

Scientific Literature

Scientific Foundation

Our platform is backed by peer-reviewed research.

85 Citations

A concise guide to choosing suitable gene expression systems for recombinant protein production

Schutz A, Bernhard F, Berrow N, Buyel JF, Ferreira-da-Silva F, Haustraete J, et al. STAR Protocols. 2023.

Comprehensive guide covering E. coli, yeast, mammalian, and insect expression systems for recombinant protein production.

View DOI

28 Citations

High-yield vesicle-packaged recombinant protein production from E. coli

Eastwood TA, Baker K, Streather BR, Allen N, Wang L, Botchway SW, et al. Cell Reports Methods. 2023.

Innovative system for producing recombinant proteins as membrane-bound vesicles in E. coli.

View DOI

156 Citations

Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity

Zhang ZX, Nong FT, Wang YZ, Yan CX, Gu Y, Song P, Sun XM. Frontiers in Bioengineering and Biotechnology. 2022.

Optimization strategies for high-level recombinant protein production in E. coli.

View DOI

42 Citations

Protein production from HEK293 cell line-derived stable pools with high protein quality and quantity to support discovery research

Sun H, Wang SY, Lu M, Tinberg CE, Alba BM. PLoS ONE. 2023.

Robust method for protein expression using HEK293-derived stable pools for discovery research.

View DOI

38 Citations

Cell-Free PURE System: Evolution and Achievements

Cui Y, Chen XJ, Wang Z, Lu Y. Biodesign Research. 2022.

Comprehensive review of PURE system applications in synthetic biology and protein production.

View DOI

FAQ

Frequently Asked Questions

Find answers to common questions about our protein production services.

Which expression system should I choose for my protein?

The choice depends on your protein's characteristics and intended application. E. coli is best for simple proteins without complex PTMs, rapid turnaround needed, or budget constraints. Mammalian systems are required for proteins needing human-like glycosylation, antibodies, or maximum bioactivity. Insect cells are ideal for complex eukaryotic proteins, large proteins, or structural biology studies. Cell-Free systems are perfect for toxic proteins, rapid screening, or incorporating non-natural amino acids.

What information do you need to start a project?

We typically need: protein sequence (amino acid sequence or gene sequence), UniProt or NCBI accession number (if available), target expression system preference, required purity level and quantity, downstream application (for QC optimization), and timeline requirements. If you don't have a sequence, we can design optimized gene sequences based on protein function or homolog information.

What purification methods are available?

We offer comprehensive purification options including affinity chromatography (His-tag, Flag-tag, Fc-tag, GST, MBP, SUMO), ion exchange (anion and cation exchange), size exclusion (gel filtration), hydrophobic interaction chromatography, and tag removal using proteases (TEV, SUMO protease, thrombin). Standard service includes affinity plus optional orthogonal polishing steps.

What quality control data is provided?

All projects include comprehensive QC: SDS-PAGE analysis (reducing and non-reducing), protein concentration determination (A280), SEC-HPLC purity analysis, and mass spectrometry verification (upon request). Optional add-ons include endotoxin testing (LAL assay), bioactivity assays, thermal stability analysis, and binding assays (SPR, BLI).

What are the typical yields for different systems?

Yields vary by expression system and protein. E. coli typically produces 1-50 mg/L (soluble). Mammalian (CHO) produces 0.5-5 g/L for antibodies, 10-500 mg/L for other proteins. Mammalian (HEK293) produces 0.1-1 g/L transient, higher for stable pools. Insect cells produce 1-50 mg/L depending on protein complexity. Cell-Free systems produce 0.1-5 mg/mL reaction (highly concentrated).

Can you handle difficult-to-express proteins?

Absolutely. We specialize in challenging proteins including membrane proteins (specialized vectors and detergent screening), multi-subunit complexes (co-expression strategies), proteins with multiple disulfide bonds (optimized folding conditions), toxic proteins (cell-free system or specialized bacterial strains), and large proteins over 150 kDa (insect and mammalian systems).

Do you offer scalable production for large quantities?

Yes, we support scales from micrograms to kilograms. Pilot scale provides 10-100 mg production for initial studies. Pre-clinical scale offers 100 mg to 1 g for formulation development. Industrial scale delivers 1 g to kg range with GMP-ready facilities. Our facilities include bioreactors ranging from 2L to 1500L capacity for seamless scale-up.

What mammalian cell lines do you support?

We offer multiple mammalian expression platforms: CHO-K1 (industry standard for therapeutic proteins), CHO-DG44 (DHFR-based selection for high-yield stable pools), HEK293 (suspension) for rapid transient expression, HEK293F (high-density suspension culture optimized), and BHK-21 for specific viral applications. Each platform can be configured for transient transfection or stable cell line generation.

Ready to Start Your Project?

Get a customized quote for your Custom Protein Production Services project. Our experts will respond within 24 hours.

No obligation

24h response

Expert consultation

Request a Quote

High-Quality Recombinant Protein Production

Why Choose Us

Gene Optimization

Multiple Systems

Advanced Purification

Complete Gene-to-Protein Solutions

Gene Synthesis & Optimization

Multiple Expression Platforms

E. coli Expression

Mammalian Systems

Insect Cells

Cell-Free Systems

Ready to Accelerate Your Research?

Advanced Expression Technologies

E. coli Expression

Mammalian Systems

Baculovirus-Insect

Cell-Free Expression

Quality Control

Purification Options

Service Specifications

Purity Guarantee: >95%

Streamlined Service Workflow

Project Consultation

Gene Synthesis

Expression Testing

Purification

QC & Delivery

Wide Range of Applications

Research Applications

Therapeutic Development

Diagnostics

What Our Clients Say

Scientific Foundation

A concise guide to choosing suitable gene expression systems for recombinant protein production

High-yield vesicle-packaged recombinant protein production from E. coli

Strategies for efficient production of recombinant proteins in Escherichia coli: alleviating the host burden and enhancing protein activity

Protein production from HEK293 cell line-derived stable pools with high protein quality and quantity to support discovery research

Cell-Free PURE System: Evolution and Achievements

Frequently Asked Questions

Ready to Start Your Project?

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