The recombinant form of TNF-α from Rhesus Macaque (rRhTNF-α) is typically produced in Escherichia coli and consists of a single non-glycosylated polypeptide chain containing 157 amino acids . The molecular weight of this recombinant protein is approximately 17.3 kDa . Despite being non-glycosylated, the recombinant TNF-α retains comparable biological activity to its naturally occurring glycosylated counterpart .
TNF-α is known for its ability to induce cell death (apoptosis) and is involved in systemic inflammation. It exists in both a secreted, soluble form and a membrane-anchored form, both of which are biologically active . The biologically active native form of TNF-α is a trimer . The recombinant form is fully biologically active when compared to the standard, with a specific activity of more than 2.0 × 10^7 IU/mg in the presence of actinomycin D .
Rhesus Macaque TNF-α shares approximately 98% homology with human TNF-α at the amino acid level . This high degree of similarity makes it a valuable tool for research, particularly in studies related to inflammation, immune response, and cancer. The recombinant protein is used in various laboratory and research applications, including cytotoxicity assays and studies on the TNF-α signaling pathway .
The recombinant TNF-α is typically supplied as a sterile filtered, white lyophilized (freeze-dried) powder . It is recommended to reconstitute the protein in sterile distilled water or an aqueous buffer containing 0.1% BSA to a concentration of 0.1-1.0 mg/mL . For long-term storage, the reconstituted protein should be apportioned into working aliquots and stored at -20°C to -70°C . It is important to avoid repeated freeze-thaw cycles to maintain the protein’s stability and activity .