albumin - publications

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1. Protein Expr Purif. 2012 May 16. [Epub ahead of print]

Expression, purification and characterization of recombinant human
interleukin-2-serum albumin (rhIL-2-HSA) fusion protein in Pichia pastoris.

Lei J, Guan B, Li B, Duan Z, Chen Y, Li H, Jin J.

Key Laboratory of Industrial Biotechnology, Ministry of Education, School of
Biotechnology, Jiangnan University, Wuxi 214122, PR China.

Interleukin-2 (IL-2) plays important roles in variety of immune functions.
Recombinant IL-2 has become an important therapeutic protein for therapy of
melanoma and renal cell carcinoma. Previously, it was proved that the therapeutic
efficacy of rIL-2 expressed in Saccharomyces cerevisiae was improved by
prolonging its in vivo half-life through genetic fusion with albumin. In this
study, a fusion protein composed of hIL-2 genetically fused to HSA was expressed
as a secretory protein under AOX1(2) (alcohol oxidase 1) promoter in Pichia
pastoris. An effective strategy was established to express rhIL-2-HSA fusion
protein in 5 L scale and the optimal purification procedure was investigated. The
purity of rhIL-2-HSA in final product was about 95%. The purified rhIL-2-HSA
fusion protein could be recognized by both anti-hIL-2 and anti-human serum
albumin monoclonal antibody. Bioactivity analysis showed that the purified
rhIL-2-HSA fusion protein displayed high level activity on proliferation in IL-2
dependent manner in CTLL2-cells. rhIL-2-HSA fusion protein also showed a extended
half-life in plasma compared with IL-2 when tested in a BALB/c mouse model. This
study provides an alternative strategy for large-scale production of bioactive
rhIL-2-HSA fusion protein using Pichia pastoris as an expression host.

Copyright © 2012. Published by Elsevier Inc.

PMID: 22609631 [PubMed - as supplied by publisher]