Recombinant protein manufacturing involves inserting recombinant DNA into a vector and introducing it into a specific expression system, such as mammalian, bacterial, yeast, or insect cells, to induce gene expression and recombinant protein production. Our bioactive proteins, in particular, induce a biological effect or response within a system. Our premium-grade bioactive proteins set new benchmarks for consistency, purity, and bioactivity, ensuring ultra-low endotoxin levels, extensive validation, and optimal performance for high-impact research and cell culture applications.
For reliable biological research, it is essential to use pure, high-quality proteins with consistent batch-to-batch performance. Our extensive portfolio of recombinant proteins is developed using a range of expression systems - including bacterial, plant, fungal, insect, and mammalian (including human) cell lines - to meet the diverse needs of researchers. While prokaryotic expression systems provide a cost-effective solution for many applications, they do not support post-translational modifications (PTMs) such as glycosylation and phosphorylation, which may influence protein structure and function. To address this, we also offer proteins expressed in mammalian systems, ensuring optimal folding, stability, and biological activity for applications requiring native-like proteins. By providing proteins from multiple expression systems, we enable researchers to select the best option for their specific studies, balancing cost, scalability, and functional relevance.
Choosing the right expression system is essential for obtaining proteins with the necessary functionality, scalability, and cost-effectiveness for your research. We offer recombinant proteins produced using a variety of expression systems to meet different scientific needs.
Mammalian expression systems are ideal for researchers requiring fully bioactive proteins with native-like PTMs and proper folding. These proteins are optimal for functional and structural assays, protein interaction studies, and other preclinical studies.
Insect expression systems provide an excellent alternative for producing functional and complex proteins, including intracellular proteins and protein complexes. They are widely used for vaccine development and diagnostic assays due to their ability to support high cell densities and PTM processing similar to mammalian cells.
E. coli expression systems are the go-to choice for structural or functional analysis in small, cost-sensitive projects. They offer rapid, scalable protein production, making them ideal for protein interaction studies, antibody generation, and screening applications. However, bacterial expression does not support PTMs.
Yeast expression systems provide a balance between scalability and PTMs, making them useful for functional and structural studies, protein interaction research, and antibody production. They allow large-scale fermentation and perform eukaryotic PTMs, though these modifications are less complex than those in mammalian cells. Researchers needing more native-like glycosylation patterns may wish to choose mammalian-expressed proteins instead.
Cell-free expression systems offer a rapid production alternative, particularly useful for toxic proteins that would be lethal in host cells, labeled proteins for imaging, and complex proteins such as membrane proteins or those with disulfide bonds. These systems eliminate the need for cloning or transfection and proteins can be produced in an animal-free manner.
Browse All Recombinant Proteins Related Products
Click Here
Features
-
Our recombinant proteins are backed by unmatched scientific support, extensive research, and a guaranteed supply from our in-house production.
-
Bioactive grade proteins offer validated bioactivity. They are produced using mammalian, E. coli, insect, yeast, or wheat germ cell-free expression systems, have high purity (>90%), and are confirmed by SDS-PAGE. Their endotoxin level is below <1 EU per µg.
-
Our premium-grade bioactive proteins
- ensure consistent performance with reliable batch-to-batch consistency.
- are produced in mammalian expression systems, which provide proteins folded and modified like their native versions, thus offering native-like performance and function compared to bacterial-produced proteins.
- guarantees optimal bioactivity through our in-house production and thorough validation, allowing you to use less of the product while achieving the same results.
- have ultra-high purity by LC/MS (>95%) and SDS-PAGE (>99%), with ultra-low endotoxin levels (<0.005 EU per µg) and size confirmed by mass spectrometry.
- are produced through a robust process that ensures rigorous quality control, consistency of supply, and flexibility to adapt quickly to changing demand and customer needs.
- offer a cost-effective approach, as the stability provided by mammalian expression systems allows for longer-term storage with less degradation or clumping, allowing a small amount to go a long way while also saving time and money in clinical research by eliminating the need for validation steps and reducing the risk of early results being affected by non-native proteins.
Applications
- Bioactive grade proteins are ideal for cell culture and functional studies.
- Premium bioactive grade proteins are ideal for applications requiring functional bioactivity, such as cell-based assays testing viability, proliferation, cytotoxicity, or cell death, where a native-identical protein is essential for accurate results.
- Our premium-grade bioactive proteins are used in cell and gene therapy as well as drug discovery, development, and manufacturing.
What is the difference between a recombinant protein and a native protein ?
The main difference between a recombinant protein and a native protein is that recombinant proteins are produced through the introduction of the gene encoding the protein into a host organism (such as bacteria, yeast, or mammalian cells) for expression. Native proteins, on the other hand, are endogenously expressed proteins that are directly extracted from organisms or cells without the need for any genetic manipulation.
How is a recombinant protein produced?
A recombinant protein is produced by first isolating and cloning the gene encoding the protein of interest into a plasmid (a small DNA molecule). This plasmid is then introduced into a host organism, such as bacteria, yeast, or mammalian cells, through a process called transformation or transfection. The host cells express the gene, producing the protein, which is then harvested from the cell lysate or medium and purified for further use.
Why is the choice of expression system important?
The expression system determines a protein’s bioactivity, purity, scalability, and cost. Different systems offer unique advantages, such as accurate post-translational modifications (PTMs) in mammalian cells or rapid, cost-effective production in E. coli.
What makes premium-grade bioactive proteins stand out?
Premium-grade bioactive proteins are manufactured using mammalian expression systems to ensure human-relevant bioactivity, undergo stringent purity and endotoxin testing, and offer consistent, high-quality performance. These proteins are ideal for applications like cell culture and gene therapy, with in-house production guaranteeing optimal bioactivity, batch-to-batch consistency, and unmatched scientific support.