Recombined extrasin alpha 1 two-strand body protein and preparation method thereof

Abstract

The invention relates to a recombined extrasin alpha 1 two-strand body protein and a preparation method thereof. Glycin and serine are connected in series with bimolecular extrasin alpha 1 (T alpha 1), a connection mode is as follows: T alpha 1-Gly-Ser=T alpha 1, and an extrasin alpha 1 two-strand body gene expression vector is constructed by synthesized extrasin alpha 1 two-strand body genes so that extrasin alpha 1 which can not be directly expressed in colon bacillus can be efficiently expressed in the colon bacillus in a two-strand body way. The purified extrasin alpha 1 two-strand body protein has biological activity and can promote lymphocytes of small mice to proliferate, restrain tumor cell strains from proliferating and obviously restrain the tumor growth of tumor-bearing mice, thereby establishing a base for the further research and the extensive application of the extrasin alpha 1.

Description

technical field [0001] The invention belongs to the field of biotechnology, and specifically relates to the construction, prokaryotic expression, purification and identification of recombinant plasmids of target proteins, in particular to thymosin alpha 1 (T alpha 1) dimer protein and its preparation method. Background technique [0002] 1. Biochemical properties of thymosin α1 [0003] 1.1 Thymosin family [0004] Thymosin is mainly produced by the thymus. It was originally prepared by Goldstein from the fetal bovine thymus protein extract. It contains more than 40 polypeptide components. According to the position of these polypeptides on the isoelectric focusing electrophoresis analysis map, they are divided into α, β, and γ. Three regions: α region pI<5, β region pI between 5 and 7, and γ region pI>7. The α-thymosin group includes thymosin α, prothymosin α and parathymosin α. Thymosin α1 (Tα1) is an N-terminal 28 amino acid fragment of prethymosin α that is produ...

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Problems solved by technology

[0031] Although the above methods can obtain active recombinant proteins, there are still many shortcomings. The process of obtaining thymosin α1 monomer by chemical cleavage is often very complicated in the later purification process; the recombinant protein purification process with His tag Requires expensive nickel column affinity purification, which greatly increases the cost and is not suitable for industrial production; and the His tag affects the application of recombinant proteins in clinical trials

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