BestBac™ Linearized Baculovirus DNA
Expression Systems’ popular BestBac Linearized Baculovirus DNA backbone has been engineered to deliver highly efficient recombination with all polyhedron gene locus based transfer vectors. The resulting virus vector provides superior stability and purity compared to other systems. BestBac is available with a deletion or wild-type at the V-cath/chiA region and sold individually or in kits.
For technicians who depend on a reliable and straightforward process to meet deadlines, minimize costs and avoid the frustration of delays, Expression Systems’ BestBac offers powerful advantages over the older and antiquated Bac-to-Bac technology. See a comparison here.
Powered by Bioz- Unmatched productivity and stability for BEVS
- Improved production methodology can reduce need for plaque purification
- Produces high titers of 5 E8 to 3 E9 IU/ml of recombinant baculovirus in P1 stock
- Generates P1 stock as quickly as Bac-to-Bac® and other systems
- Each BestBac vial contains enough material for a minimum of five cotransfections
- Suitable for other expression systems including BacMamTM
- See the process comparison of BestBac vs Bac-to-Bac here
Available in Two Versions
- BestBac 1.0 is wild type at the cathepsin and chitinase (v-cath/chiA) loci, preferred for some applications.
- BestBac 2.0 is a deletion mutant of BestBac 1.0. The v-cath/chiA deletion removes a potentially detrimental protease and may reduce competition for resources for protein synthesis during late gene expression. The v-cath/chiA deletion can improve the integrity of your expressed protein resulting in a significant increase of functional protein yield.
Also Available in a Cotransfection Kit
Contains everything you need to perform cotransfections with your transfer vector. Included in the kit are:
- BestBac DNA
- Transfection medium
- Expres2 TR transfection reagent
| Media type | Linearized Baculovirus DNA |
| Shipping condition | 2–8⁰C |
| Storage condition | 2-8⁰C, protect from light |
| Use-by date | One year from date of manufacture |
COA Search
Enter Lot # for productZou Y, Weis WI, Kobilka BK (2012) N-Terminal T4 Lysozyme Fusion Facilitates Crystallization of a G Protein Coupled Receptor. PLoS ONE 7(10): e46039. doi:10.1371/journal.pone.0046039 Abeywickrema, P. D., Patel, S. B., Byrne, N. J., Diehl, R. E., Hall, D. L., Ford, R. E., … Sharma, S. (2010). Expression, purification and crystallization of human prolylcarboxypeptidase. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 66(Pt 6), 702–705. http://doi.org/10.1107/S1744309110014041 Resurrecting KIR2DP1: A Key Intermediate in the Evolution of Human Inhibitory NK Cell Receptors That Recognize HLA-C. Hugo G. Hilton, Jeroen H. Blokhuis, Lisbeth A. Guethlein, Paul J. Norman and Peter Parham J Immunol January 25, 2017, 1601835; DOI: https://doi.org/10.4049/jimmunol.1601835