Schistosomiasis is a major neglected tropical disease of public health importance. It is caused due to penetration of the human skin by infectious larvae (cercariae) of Schistosomes, water-borne parasitic platyhelminths, which has infected ~252 million people worldwide. Host interactive schistosome protein, calpain (Sm-p80), plays an important role in the surface membrane renewal of schistosomes, which is employed by helminths to evade host immunity. At present, to our knowledge, Sm-p80 is the sole schistosome vaccine candidate that has been tested for its prophylactic and therapeutic efficacy in different vaccine formulations and approaches.

Due to lack of available literature, individual and combinatorial effects of the experimental conditions (such as selection of host strain, media compositions, inducer concentration and induction temperature) on expression of client’s proteins was not available. The initial screening procedures for these pre-clinical targets was a challenge for the client with respect to time and money.

A plethora of example suggests, overproduction of recombinant proteins in E. coli can form insoluble aggregates, misfolded conformations resulting functionally inactive product. Moreover, scaling up those proteins commonly leads to aggregation followed by precipitation resulting loss of productivity always been a painstaking experience.

CRM197, which retains the same inflammatory and immune-stimulant properties as diphtheria toxin but with reduced toxicity, has been used as a safe carrier in conjugated vaccines. Recently, CRM197 was produced as a single peptide where fragment A was linked to fragment B, forming an intramolecular disulphide bond. In addition to its vaccine adjuvant properties, there is also growing interest in CRM197 because of its potential antitumor activity related to its ability to bind the soluble form of HB-EGF, which is highly expressed in some human cancers.

Magnitude of heterosis is much lower in self-pollinated crops than cross-pollinated crops. Therefore, improvement of self-pollinated crops by producing hybrid varieties are necessary and is a major goal of plant breeding. Several biotechnological strategies have been deployed to restrict self–fertilization in plants. However, the only commercialized transgenic male sterility method is SeedLink^TM,

Viral capsid glycoprotein X (Due to confidentiality, we are not disclosing the information about protein) is the primary candidate for inclusion in a subunit vaccine against rotaviral diarrhea. Therefore, significant effort has been directed towards producing recombinant protein X that maintains the antigenic characteristics of the native molecule. A successful vaccine that will induce adequate neutralizing antibody will need to present protein X in a conformation similar to the mature virus.