Many reports illustrate that Coagulation factor XIIIa (FXIIIa) has diverse and crucial functions in thrombus for¬mation and stability. However, it is difficult to obtain large amounts of FXIII in the market. Therefore, obtaining large quantities of FXIIIa through genetic engineering technology is important for both clinical treatment and mechanism of protein expression.
The expression, purification and identification of recombinant human coagulation factor XIIIa in Pichia pastoris (a species of methylotrophic yeast) shows that it has biological activity, suggests a study conducted by a team of researchers at the Zhejiang Chinese Medical University led by Xu et al.
Recombinant pPICZαC-FXIIIa was expressed in Pichia pastoris, purified and then tested for biological activity by reacting it with plasma samples.
In this study, FXIIIa fragments in human placenta tissue was taken and inserted in an expression vector under the control of a yeast promoter for AOX1, which was constructed and expressed in Pichia pastoris (Figure 1). The findings suggest that the FXIIIa fragment of 2250 bp was inserted successfully into the pPICZαC vector. The expression and purification products about 83 kDa (the same molecular weight as human FXIIIa) were obtained, which solidified significantly when reacted with human plasma. The work shown that the expression and purification products were successful, with sufficient biological activity, which can be used as a candidate FXIIIa hemostatic agent in genetic engineering.
This study is significant as is reports an efficient expression system for the production of FXIIIa. This will not only facilitate further studies of FXIIIa, but also pave the way for possible large-scale production of biologically active FXIIIa. The researchers note that more work on recombinant FXIIIa production with higher purity and more activity would be investigated, to improve upon current results.
This article can be obtained from the following link: https://www.eurekaselect.com/node/183155/article/expression-purification-and-characterization-of-recombinant-human-coagulation-factor-xiiia-in-pichia-pastoris
