The E.Coli derived recombinant 6xHis tag fusion protein is a multimer having a molecular mass of 15kDa and contains the Trp. Pallidum p15 immunodominant regions and six histidines fused at the C- terminus.
Treponema pallidum is a spirochete bacterium responsible for syphilis, a chronic and complex sexually transmitted disease. The bacterium has a small genome of approximately 1.14 million base pairs, reflecting its adaptation to the rich environment of mammalian tissue . The p15 protein of Treponema pallidum is a significant immunogen during natural syphilis infection in humans and experimental infection in other hosts .
The p15 protein is a 15 kDa lipoprotein that plays a crucial role in the immune response to Treponema pallidum. It is a major membrane immunogen, meaning it is a key target for the immune system during infection . The humoral and cellular immune responses to this molecule appear late in infection as resistance to reinfection is developing .
The recombinant p15 (partial) protein is produced using Escherichia coli (E. coli) expression systems. This recombinant protein includes the immunodominant regions of the p15 protein and is fused with a His tag at the C-terminus . The His tag facilitates purification and detection of the recombinant protein.
The recombinant p15 (partial) protein is used in various applications, including: