Half-Life Extension Service by Bioactive Natural Protein Conjugation

For Research Use Only. Not for Clinical Use.

Nowadays, more than 200 approved recombinant protein therapeutics are available for application in various indications, while the research aimed to extend their half-life attracts more attention owing to ease of use and adherence to the treatment regime. With the new progress of protein engineering technology, bioactive natural protein conjugation as a competitive means to prolong the half-life of drugs becomes more accepted owing to reduced toxic side effects. Creative Biolabs is a world-leading service provider that is fully committed to offering the most suitable and inexpensive half-life extension service by bioactive natural protein conjugation based on our powerful technologies in chemical synthesis, genetic engineering, and recombinant protein expression. By this method, the best strategy will be chosen to meet the unique requirements of every client.

Introduction of Half-Life Extension Service by Bioactive Natural Protein Conjugation

The two most-used methods for half-life extension. (Tan, 2018)Fig. 1 The two most-used methods for half-life extension. (Tan, 2018)

Therapeutic peptides and proteins have received increasing attention because of their high binding affinity, low toxicity, specificity, and solubility. However, many proteins drugs suffer from short plasma half-life due to small molecular mass and endogenous clearance mechanism. There are few natural protein molecules that have an exceptionally long circulation half-life. Therefore, proteins like serum albumin and transferrin were first considered as half-life extension moieties of other therapeutic proteins. The long half-life of transferrin is due to clathrin-dependent transferrin receptor binding, whereas albumin's long half-life is the result of neonatal Fc receptor (FcRn) dependent recycling. Therefore, through the conjugation with albumin or transferrin, protein drug molecules can reduce renal clearance by increasing their molecular size and escape from enzymatic degradation. Unlike most natural proteins, IgG has an exceptionally long plasma half-life (about 21days) due to the stabilization of the Fc region. Like albumin, Fc fragment also can be modified on target protein molecules to enhance Half-Life by FcRn dependent recycling. Moreover, Fc fusion offered some added benefits such as divalent binding and physiological properties improvement.

Custom Services of Half-Life Extension by Bioactive Natural Protein Conjugation

Creative Biolabs provides multifarious methods of bioactive natural protein conjugation service to half-life extension of drugs.

As a mature Half-Life Extension technology, Albumin conjugation has been widely used in various protein drugs in the market. Through chemical or biological modification, we can support albumin on protein drugs in covalent or non-covalent form, hoping to improve their pharmacokinetic properties.

Fc-Fusion technique is commonly suitable for most therapeutic protein modification and achieved excellent improvement in half-life extension as well as therapeutic effect and physical property. Our highly experienced staff can offer comprehensive Fc-fusion based half-life extension service to advance target drug research.

Transferrin fusion is a novel strategy to realize half-life extension which is not involved in FcRn dependent recycling and has potential clinical application. As a leading biotechnology company in the world, we always keep keen sense of new protein engineering evolution. We will be honored to offer transferrin fusion based half-life extension service to support your project.

If you have any needs in the half-life extension service, please feel free to contact us.


  1. Tan, H.; et al. Recent Advances in Half-life Extension Strategies for Therapeutic Peptides and Proteins. Current Pharmaceutical Design.2018, 24, 4932-4946.

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For Research Use Only. Not for Clinical Use.