In this study, we used Sf9 insect cell expression system to express recombinant H7 HA proteins H7-53WT, in which HA gene was derived from H7N9-53 strand, and H7-53TM CFLLCining CFLLC minidomian by replacing its TM domain with H3 HA TM.
Recombinant mouse CA XV was expressed in a baculovirus/insect cell expression system [27], and a polyclonal antibody was raised against the purified recombinant protein.
mCD36ED DNA, amplified by PCR with a hexa-histidine tag at its carboxyl-terminus (C-terminal His-tag), was cloned in a baculovirus transfer vector and mCD36ED protein was expressed using a baculovirus/insect cell expression system.
The baculovirus insect cell expression system was used to co-express soluble ECDs of all four muscle-type nicotinic acetylcholine receptor subunits (α, β, γ & δ-ECD) from Torpedo.
H5N1 Viet04 hemagglutinin was expressed using a baculovirus/ insect cell expression system and purified from culture supernatants, as previously described [27].
Purified recombinant human ADAM-10 (active ectodomain derived from an insect cell expression system) and pro-MMP-7 (expressed in a mouse myeloma cell line) were from R+D Systems, Abingdon, U. K. Pro-MMP-7 was activated with 1 mM p-amino-phenylmercuric acetate (AMPA) at 37°C for 1 h.
Subunits of γ-TuSC and γ-TuSCΔN-Spc98 were expressed with the baculovirus-insect cell expression system.
Cryptochrome 1a (gwCry1andand the photolyase-homology-region of Cry1 (gwCry1-PHR) from the migratory garden warbler were recombinantly expressed and purified from a baculovirus/Sf9 cell expression system.
Five C-terminally His-tagged human HSL variants were successfully cloned and expressed in Sf9 insect cells using the baculovirus/insect cell expression system.
In the course of our studies on the structure/function relationship of visual pigments, we have expressed the human green cone pigment in the baculovirus/insect cell expression system.
To investigate the effect of the peptide sequence in ERAP1 trimming we over-expressed the human enzyme in a baculovirus driven insect cell expression system and used the purified recombinant enzyme to screen collections of peptides for degradation of their N-terminal residues by ERAP1.
