Recombinant Protein

The vascular endothelial growth factor (VEGF) family comprises five secreted homodimeric glycoproteins—VEGF-A, VEGF-B, VEGF-C, VEGF-D and placental growth factor (PlGF)—that selectively bind to VEGFR-1, -2, -3 and the co-receptors neuropilin-1/2, thereby orchestrating angiogenesis, lymphangiogenesis and vascular permeability.

Interleukins (ILs) are a group of cytokines (secreted proteins and signal molecules) that were first seen to be expressed by white blood cells (leukocytes). The function of the immune system depends in a large part on interleukins, and rare deficiencies of a number of them have been described, all featuring autoimmune diseases or immune deficiency.

The interferon (IFN) family comprises three classes: type I (IFN-α/β/κ/ε/ω), type II (IFN-γ) and type III (IFN-λ1/2/3).

The transforming growth factor-β (TGF-β) superfamily comprises over 30 members, including TGF-β, Activin, Inhibin, bone morphogenetic proteins (BMPs), and growth differentiation factors (GDFs).

The colony-stimulating factor (CSF) family comprises soluble glycoproteins that govern the survival, proliferation and lineage-specific differentiation of hematopoietic progenitors while activating mature blood cells.

The Escherichia coli expression system is a cornerstone in recombinant protein production, favored for its well-characterized metabolic pathways, rapid cell growth, high protein expression levels, and clear genetic background. Despite these advantages, a significant challenge in using this system is the propensity for protein aggregation into inclusion bodies.

Insect cell expression systems have emerged as a powerful tool for the production of recombinant proteins, particularly for applications requiring complex post-translational modifications.

Mammalian protein expression systems are now widely used in the biopharmaceutical industry for producing complex recombinant proteins. These systems use mammalian cell lines like Chinese hamster ovary (CHO) cells and human embryonic kidney (HEK) 293 cells.

Pichia pastoris, a methylotrophic yeast, has emerged as a highly efficient and widely used eukaryotic host for the production of recombinant proteins. This system combines the advantages of eukaryotic post-translational modifications with the rapid growth and scalability of yeast-based expression systems, making it particularly suitable for the production of complex proteins that require glycosylation and other modifications for proper folding and functionality.

Escherichia coli (E. coli) is one of the most widely used prokaryotic expression systems for the production of recombinant proteins. Its popularity stems from several key advantages, including ease of genetic manipulation, rapid growth rate, and cost-effectiveness. E. coli has been extensively studied and optimized for protein expression, making it a cornerstone in both research and industrial applications.