Trimeric Protein Production Service

Protein trimerization is known as the formation of a protein trimer, a macromolecular structure consisting of three noncovalently associated identical or non-identical subunits.

Profacgen provides novel trimeric protein production service by designing and expressing proteins in disulfide bond-linked homo-trimeric forms. With years of experience, Profacgen has accomplished to significantly increase the expression level and optimize the purification scheme of recombinant trimeric fusion proteins, the scale can be quickly moved from preclinical stage towards the bedsides of millions of patients. Our protein trimerization technology has established a broadly applicable system for the production and characterization of trimeric proteins and generated new insights into the assembly and maturation of trimers that will have implications for the design of an effective vaccine.

Features of protein trimerization:

Naturally secreted trimer
Disulfide bond-linked
Mammalian expression system
High purity
Structurally stable

Currently major Tumor Necrosis Factor (TNF) biologic blockers are dimeric in structure, whereas some of the TNF family themselves are homotrimeric in nature. From a structural biology point of view, a homodimeric structure with a two-fold symmetry cannot perfectly dock to a homotrimeric structure with a three-fold symmetry, thus limiting the affinity between the two molecules.

Protein trimerization platform allows secreted protein to be made as covalently linked homotrimers with greatly increased avidity to their disease-causing targets, such as the TNF family of cytokines (TNFRII, TRAIL, etc), HIV gp120/gp41, Influenza HA, DR4, DR5, sCD4, and ApoAI. Constructs for all of these have already been made and are in development as biologic drugs against autoimmune diseases, cancer, AIDS, osteoporosis, and heart disease.

Reference: Haipeng Liu and Danmei Su, etc. Improvement of Pharmacokinetic Profile of TRAIL via Trimer-Tag Enhances its Antitumor Activity in vivo. Sci Rep. 2017; 7: 8953. doi: 10.1038/s41598-017-09518-1.