EC Number   |
|---|
   1.13.12.13 | construction of a cold induced expression vector in Escherichia coli cells that consists of a histidine tag sequence for nickel chelate affinity purification, IgG-binding domain of protein A (ZZ-domain) and the multiple cloning sites, the role of ZZ-domain as a solubilizing partner at 15°C is demonstrated by expressing the imidazopyrazinone-type luciferase of Oplophorus |
| 1.13.12.13 | expressed in Escherichia coli |
| 1.13.12.13 | expression of 19 kDa subunit 19kOLase in Escherichia coli |
| 1.13.12.13 | recombinant expression and secretion of 19 kDa catalytic subunit mutant nanoKAZ from CHO-K1 cells. Mutant nanoKAZ lacks the amino-terminal signal peptide, is expressed in the cytoplasm, translocated to the cell membrane, and released into the culture medium through an endoplasmic reticulum-Golgi-independent pathway. Recombinant expression of His-tagged wild-type and mutant KAZs in Escherichia coli. The secreted proteins form aggregates |
| 1.13.12.13 | recombinant expression and secretion, using the signal peptide sequence of Gaussia luciferase, of catalytic 19 kDa protein KAZ of Oplophorus luciferase and its mutants in Escherichia coli and recombinant expression of His-tagged wild-type and mutant enzymes and KAZs in CHO-K1 cells |
| 1.13.12.13 | recombinant expression of His-tagged 19 kDa catalytic subunit mutant nanoKAZ in Escherichia coli strain BL21. In bacterial cells, wild-type KAZ is mainly expressed as inclusion bodies |
| 1.13.12.13 | the catalytic domain of Oplophorus luciferase (19kOLase) is expressed in Escherichia coli cells using the cold-induced vectors of pCold-KAZ. Cold induction for Escherichia coli cells is carried out at 15°C |
| 1.13.12.13 | the fused proteinof nanoKAZ with IgG-binding domain (ZZ domain) is expressed in the cytoplasm of Escherichia coli cells as a soluble form and purified. A secretory expression of nanoKAZ in CHO-K1 cells is performed using nanoKAZ fused with the signal peptide sequence of Gaussia luciferase |
