TD1, Transdermal peptide
Main Page-BBa_K1074000
TD1 is a short synthetic peptide(ACSSSPSKHCG)identified by in vivo phage display, facilitated efficient transdermal protein delivery through intact skin. Studies suggested that the peptide creates a transient opening in the skin barrier to enable macromolecular material to reach systemic circulation

Pgrac+RBS+SamyQ+TD1+GFP
Main Page-BBa_K1074006 This is the main circuit of our project to allow high expression of target protein(antigen,adjuvant).GFP can be substituted by various proteins via a modular PCR or standard cut/ligation method.

PHT43
PHT43 is a E.coli-B.subtilis shuttle vector allowing high-level expression of secreted proteins in B.subtilis. It is based on the strong σA-dependent promoter preceding the groE operon of B. subtilis which has been converted into an efficiently controllable (IPTGinducible)promoter by addition of the lac operator. An efficient Shine-Dalgarno (SD) sequence as well as a multiple cloning site (BamH I, Xba I, Aat II, Sma I) were also inserted. To obtain secretion of recombinant proteins, the coding region for the signal peptide of the amyQ gene encoding an α-amylase was fused to the SD sequence.

HBsAg
HBsAg is the surface antigen of the hepatitis B virus (HBV). It indicates current hepatitis B infection. Sequence and Features

Ag85b
The antigen 85 proteins (FbpA, FbpB, FbpC) are responsible for the high affinity of mycobacteria for fibronectin, a large adhesive glycoprotein, which facilitates the attachment of M.tuberculosis to murine alveolar macrophages (AMs). They also help to maintain the integrity of the cell wall by catalyzing the transfer of mycolic acids to cell wall arabinogalactan and through the synthesis of alpha,alpha-trehalose dimycolate (TDM, cord factor). They catalyze the transfer of a mycoloyl residue from one molecule of alpha,alpha-trehalose monomycolate (TMM) to another TMM, leading to the formation of TDM. Sequence and Features

Protective Antigen Domain 4
Protective antigen (PA) is the central component of the three-part protein toxin secreted by Bacillus anthracis, the organism responsible for anthrax. Homologues of PA have been found in several spore-forming Gram-positive bacteria, and share the ability to translocate toxic enzymes into the host cytosol.The PA monomer is organised mainly into antiparallel beta-sheets and has four domains: an N-terminal domain (domain 1) containing two calcium ions and the cleavage site for activating proteases; a heptamerisation domain (domain 2) containing a large flexible loop implicated in membrane insertion; a small domain of unknown function (domain 3); and a carboxy-terminal receptor- binding domain (domain 4) [PMID: 9039918]. This entry represents domain 4 of PA, which has an immunoglobulin-like fold. Domain 4 plays a key role in cellular receptor recognition, as well as in pH- dependent pore formation[PMID: 19722284].