Rhipicephalus appendiculatus, also known as the brown dog tick, is a species of hard tick found in parts of Europe, Africa, the Middle East, and Asia. It is a species of medical and veterinary importance due to its potential to transmit diseases to humans and animals. The tick is a small, flat, reddish-brown arachnid with a scutum, or hardened plate, covering its dorsal region. It is well-adapted to living in a wide range of climates and habitats, and can be found in urban and rural areas, as well as in woodlands, grasslands, and other habitats. The tick is known to feed on both wild and domestic animals, and can transmit several diseases, including canine babesiosis, canine ehrlichiosis, and canine hepatozoonosis. It is also capable of transmitting diseases such as tick-borne encephalitis, Lyme disease, and Rocky Mountain spotted fever to humans. Control of R. appendiculatus can be achieved using acaricides, repellents, and other tick control measures.

One of the major components of this cement substance is Cement Protein 64P-BA1. Researchers are interested in understanding the role of this protein in the tick’s ability to attach to its host and feed for long periods. The protein is also being investigated as a potential target for developing novel tick control strategies.

Rhipicephalus appendiculatus antigen Bm86-like protein (RappBm86) was used to immunize rabbits. The immune serum was evaluated by indirect ELISA and western blotting. The results showed that the immune serum had a high titer against RappBm86 and recognized the recombinant RappBm86 in western blotting. This suggests that the immune serum can be used to detect RappBm86 in various applications.

The use of recombinant proteins/cDNA in academic research and therapeutic applications has skyrocketed. However, in heterologous expression systems, successful recombinant protein expression is dependent on a variety of factors, including codon preference, RNA secondary structure, and GC content. When compared to pre-optimization, more and more experimental results demonstrated that the expression level was dramatically increased, ranging from two to hundred times depending on the gene. Bioclone has created a proprietary technology platform that has resulted in the creation of over 6,000 artificially synthesized codon-optimized cDNA clones (cloned in E. coli expression Vector), which are ready for production of the recombinant proteins.