Recombinant HIV-1 TAT Clade B C31A-C34A is produced in E.coli and is mutate in the cystein-rich region. It Is a single, non-glycosylated, polypeptidic chain containing 86 amino acids encoded by two exons.
Recombinant TAT Clade B C27A-C31A Mutant
The redox state of cysteine-rich region of HIV tat protein is known to play a crucial role in tat biological activity. The cysteine-rich region, encompassing seven cysteine residues, is highly conserved among the different HIV-1 strains and isolates. Its redox state is known to be important for protein function and activity. In particular, variation of the tat cysteine motif known as “cysteine 30-cysteine 31” (C30C31) is associated with clade-specific tat neurotoxicity. Formation of tat homodimers also depends on the oxidation state of the protein, as dimerization requires metal ions binding to free sulphydryl groups present in the cysteine region. In the presence of oxygen and in absence of reducing agents, tat protein rapidly oxidises forming intra-molecular disulfide bonds which prevent the interaction with metal ions.
HIV-1 regulatory tat protein plays an essential role in viral replication and infectivity. In addition, during acute infection tat is released in the extracellular environment by infected cells and is taken up by neighbouring cells where it transactivates viral replication and increases virus infectivity. The HIV-1 tat protein is a molecule of 86 aminoacids encoded by two exons.
|Clinical diagnostics| Life Sciences
|Reagents for research
|TAT Protein (Transactivating regulatory protein)
|Not biologically Active protein
|Lyophilized with 0.1% glycerol.
|WB, SDS-PAGE, Endotoxins, Up-take, Rescue assay
|The protein should be reconstituted in apirogenic sterile water or 1X PBS
|Shipped in dry ice. The lyophilized protein is stable for 24 months if stored at -80°C. The reconstituted solution has to be used immediately. Avoid freeze-thaw cycles.
|For Laboratory Research Use Only