Insect baculovirus expression vector system introduction
Insect baculovirus expression vector system (BEVS) is a system in which baculovirus worked as a vector of foreign genes, by infect insect cells or insect larvae to produce exogenous proteins. It is an important part of the eukaryotic expression system.
Advantages of insect baculovirus expression system
2). Large capacity of carrying foreign genes
3). High expression level of exogenous protein
4). The expressed eukaryotic gene products can be properly folded and modified, thus have good bioactivity.
Compared to mammalian cell expression system:
1). The culture conditions are relatively simple and do not require the CO2
2). The cost is relatively reasonable
3). Not easy contaminated by bacteria
4). High protein content
The technical advantages of Leading Biology
1. We use classic Bac-to-Bac technology to create a fast, simple and efficient baculovirus expression platform. The technique can produce recombinant virus quickly, and do not require tedious plaque assay, which greatly improves the efficiency.
2. The production cycle is short and the flux is large. Can achieve the process of both small scale cell culture and large scale fermentation, the protein products can even reach the level of 50mg.
3. Provide free virus ion amplification and storage services, and the shelf-life can as long as half a year.
The expression of Rsignal1 recombinant protein in Sf9 cells.
After codon optimization, the Rsignal1 target gene is constructed on the insect expression vector, then transfected with Sf9 cells to get P1 baculovirus. Through a series of virus amplification and optimal MOI exploration and high yield affinity purification, finally obtained the high quality Rsignal1 protein.
Fig1.P1 expression test
Fig.2 The optimal MOI test
Fig. 3 Purification test
Fig. 4 Final product
Introduction of insect baculovirus expression vector
Common expression vectors and their features
Strong AcMNPV polyhedron(PH) promoter for high level protein expression
Large multiple cloning site for simplified cloning
Strong polyhedron(PH) promoter for high-level protein expression
N-terminal 6His tag for purification of recombinant fusion protein using metal-chelating resin and aTEV protease cleavage site for removal of the 6His tag following protein purification
Vector supplied in 3 reading frames for simplified cloning
Two strong baculovirus promoters(PH and p10) to allow simultaneous expression of two proteins
Two large multiple cloning sites for simplified cloning
Common expression cells and their features
The Sf9 cell lineis a clonal isolatederived from IPLBSF21-AE (Sf21), and are originated from the ovary tissue of Spodoptera frugiperda chrysalis.
Suitable for transfection, purification, production of high titer virus, cell plating and recombinant protein expression.
Sf21 cellis also a clonal isolatederived from the IPLBSF-21 cell line and also are originated from the ovary tissue of the pupae of the Spodoptera frugiperda.
Also suitable for transfection, purification, production of high titer virus, cell plating and recombinant protein expression. Sometimes, Sf21 cells may have a higher protein expression rate than Sf9 cells
Hi5 cell lines discovered by Boyce Thompson Institute during the study of plants, they are originated from cabbage looper ovary cells and Trichoplusiani cells
Hi5 cells could express high quality recombinant virus. It is also widely used for transfection and plaque purification, moreover, the Hi5 cell line is more suitable for the expression of secretory recombinant protein.
S2 are late fruit fly embryo cells. Most of them are female tetraploid cells, and there are also some diploid cells.
It is suitable for the expression of recombinant protein
Protein Expression in Bacteria
Unique Protein Production Service
Protein Expression in Cell-Free System
Rich in Disulfide Bond Protein Expression
Protein Expression in Mammalian Cells
Protein Expression in Baculovirus
Protein Expression in Yeast
Protein Expression in Bacillus subtilis
Protein Expression in E coli
Virus-like particles/Phage library expression system based
Cell-free expression system
Whole cell-based protein expression system
Why Leading Biology?
At Leading Biology, we custom protein purification design for every single protein to ensure the production and recovery rate as high as possible.
Working with us, you will get stability, and it means a reliable partner to help streamline your R&D process.
Working with us, you will get the guaranteed service to accommodate your requirements.
- Innovative configurations of chromatography columns custom tailored to each protein
- Vigorous quality control system to ensure the required quality and reproducibility
- Production capacity of up to tens of grams
- Flexible scale-up protein production
- Competitive price with fast turnaround time
Please obtain a quote before ordering, and refer to the quote number when you place an order.
Orders are typically confirmed within 12 hours.
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By Phone: 1-661-524(LBI)-026d2 (USA)