Cloning, expression and purification of the DNA binding domain of RFX protein.

Cloning, Expression and Purification of Clostridium botulinum Neurotoxin Type E Binding Domain

Cloning and evaluation of gene expression and purification of gene encoding recombinant protein containing binding subunit of coli surface antigens CS1 and CS2 from Enterotoxigenic Escherichia coli

Background & Objective: Enterotoxigenic Escherichia coli (ETEC) is a major causative agent of diarrhea. Enterotoxins and the colonization factors (CFs) are major virulence factors in ETEC infections. The bacterium binds to the intestinal epithelial cell surface through colonization factors and produces enterotoxins that cause excessive fluid and electrolyte secretion in the lumen of the intesti...

Molecular Cloning, Expression and Peroxidase Conjugation of Staphylococcus aureus Protein A

Background: Staphylococcal protein A (SPA) is a cell wall component of Staphylococcus aureus that binds to different IgG subclasses of human and several animal species. This bacterial protein can be used as an antibody detector in various immunological assays or as an isolation reagent for the purification of antibody molecules via immuno-chromatography procedures.Objectives: Molecular cl...

Cloning, Expression, Purification and Immunoreactivity Analysis of Gag Derived Protein p17 from HIV-1 CRF35 in Fusion with Thioredoxin from Human Subjects

So far, recombinant antigens of HIV-1, the etiologic cause of Acquired Immunodeficiency Syndrome (AIDS), have been widely used for the diagnosis and vaccine development. P17 or the matrix protein formed by the proteolytic cleavage of gag is strongly antigenic and is as conserved and immunogenic as p24. In some cases, antibodies to p17 are more prevalent than antibodies to p24 and the decline in...

بررسی خصوصیات ایمنی‌زایی پروتئین نوترکیب زنجیره‌ی سبک سم بوتولینوم تیپ A(840)

Background and Objective: Botulinum neurotoxin type A, structurally consists of a 50KD light chain and a 100 KD heavy chain linked by a disulfide bond. The protein can further be divided into three functional domains of which catalytic domain corresponds to the light chain. In this research we aimed to produce recombinant catalytic domain in order to obtain a protective protein. Materials and M...