Incorporation of Unnatural Amino Acids into protein Service

Background

As the core executor of life activities, the functional diversity of proteins depends on the chemical properties and permutations of amino acids. However, natural proteins are composed of only 20 standard amino acids, which are limited in number and the chemical properties of side chain groups (such as polarity, charge, and reactivity) are relatively conservative, resulting in inherent limitations in the functions and regulation of natural proteins, making it difficult to meet the innovative needs of protein engineering and drug development, and limiting their functional diversity and controllability.

Unnatural amino acids (UAA) can introduce new chemical properties and functions to proteins with their diverse side chain groups. Carefully designed amino acid molecules carry special chemical groups that natural amino acids do not have, such as photosensitive groups, bioorthogonal reaction groups, and metal chelation sites, which open up new possibilities for protein engineering. Through genetic code expansion technology, these unnatural amino acids can be precisely inserted into specific sites of proteins, achieving precise regulation of protein chemical properties, and the modified tRNA/aminoacyl-tRNA synthetases only specifically recognize UAA without interfering with the natural translation process, providing unprecedented possibilities for protein engineering and drug development.

Application

Protein structure and function research

The technology of incorporating non-natural amino acids into proteins can be used to study protein dynamics and functions, such as photo-crosslinking UAA to capture protein interactions, or directly simulating post-translational modifications to simplify mechanism analysis.

Biomedicine

UAA enables precise drug design, such as site-specific conjugation of antibody-drug conjugates, or the construction of long-acting PEGylated protein drugs to improve efficacy.

Enzyme engineering

It can be used to enhance enzyme stability (such as introducing fluorinated UAA to improve thermal stability) or catalytic activity (such as metal chelated UAA for artificial metalloenzymes).

Development of non-natural amino acid probes

As high-sensitivity markers, they are integrated into recombinant proteins to achieve quantitative detection of target proteins and fine structure and function analysis.

Service Procedure

Profacgen provide end-to-end solutions from design to production, delivering premium unnatural amino acid-incorporated protein services with guaranteed quality.

The following is our standardized service process:

Figure 1. Service Process.

Cas Study

Project: Customized protein expression using different tRNAs incorporating unnatural amino acids (UAAs).

Figure 2. Different unnatural amino acids (UAAs)

Figure 3. WB results of target protein containing different unnatural amino acids (Anti His tag)
M: Protein Marker; Lane 1: no tRNA;
Lane 2: AcPhe-tRNA; Lane 3: Phe(4-F)-tRNA;
Lane 4: Phe(4-I)-tRNA; Lane 5: propargyl-Gly-tRNA;
Lane 6: Phe(N3)-tRNA; Lane 7: Lys(N3)-tRNA.

Our Advantages

• Precision site-specific incorporation to meet diverse research needs.
• Optimized orthogonal translation system achieves high UAA incorporation efficiency with stable expression.
• Rigorous MS+HPLC quality control ensures correct UAA insertion and high protein purity (>95%).
• Cost-effective solutions with flexible collaboration models significantly reduce R&D costs and time investment.
• One-stop service from gene design to functional validation eliminates multi-platform coordination, saving time and effort.

FAQs

Please contact us to provide more detailed information for evaluation.