The camelid has an antibody comprised only of H chain, and the variable region is called VHH antibody. The VHH antibody has high stability to temperature and pH, and low-cost production is possible with a microbe. We can screen VHH antibody gene efficiently by using the high quality VHH antibody gene library and the cDNA display technology. The provided VHH antibody can be produced by Brevibacillus secretion system at high productivity. We perform one-stop service of production of VHH antibody protein from the acquisition of the genetic information.
• Screening of VHH antibody gene
• Typical deliverables from such a project are 3 VHH clones, sequences of VHH clones, 0.5 mg amounts of purified VHHs.
• The time involved for the whole process is about 4 months.
• Naturally occurring antibodies devoid of light chains. Hamers-Casterman C1, Atarhouch T, Muyldermans S, Robinson G, Hamers C, Songa EB, Bendahman N, Hamers R.
Nature. 1993 Jun 3;363(6428):446-8. PMID: 8502296
• Nanobodies – from llamas to therapeutic proteins.
Drug Discov Today Technol. 2010 Summer;7(2):e95-e146. PMID: 24103724
• Single domain camel antibodies: current status. Muyldermans S.
J Biotechnol. 2001 Jun;74(4):277-302. PMID: 11526908
• Cell-penetrating anti-GFAP VHH and corresponding fluorescent fusion protein VHH-GFP spontaneously cross the blood-brain barrier and specifically recognize astrocytes: application to brain imaging.
Li T, Bourgeois JP, Celli S, Glacial F, Le Sourd AM, Mecheri S, Weksler B, Romero I, Couraud PO, Rougeon F, Lafaye P.
FASEB J. 2012 Oct;26(10):3969-79. PMID: 22730440
• Comparison of physical chemical properties of llama VHH antibody fragments and mouse monoclonal antibodies.
van der Linden RH, Frenken LG, de Geus B, Harmsen MM, Ruuls RC, Stok W, de Ron L, Wilson S, Davis P, Verrips CT.
Biochim Biophys Acta. 1999 Apr 12;1431(1):37-46. PMID: 10209277