recombinant HIV-1 Tat protein

Recombinant HIV-1 Tat protein is a laboratory-produced version of the transactivator of transcription (Tat) regulatory protein from human immunodeficiency virus type 1 (HIV-1). It is typically expressed in Escherichia coli and purified for use in research applications such as ELISA, western blotting, drug screening, and studies on viral replication and pathogenesis[2][4][5]. The full-length Tat protein consists of either 86 or 101 amino acids depending on the construct used[2][4][5]. Mechanistically, Tat plays an essential role in viral replication by binding to the TAR RNA element on nascent viral transcripts and recruiting host factors such as P-TEFb to enhance transcriptional elongation by RNA polymerase II[4][5][10]. Extracellularly released Tat can be taken up by neighboring cells where it further promotes viral gene expression and infectivity. Recombinant forms have been studied for their effects on immune modulation (e.g., upregulation of IL-6 and TGF-beta production)[3], apoptosis induction in T-cells via microtubule disruption[4], inhibition or modulation of latency establishment[6], and potential use as a vaccine antigen candidate due to its sequence conservation among clades and immunogenic properties[7].

Other names

recombinant human immunodeficiency virus type 1 Tat proteinrecombinant tat HIV-1 MNrecombinant HIV type 1 TAT Protein (a.a. 1-101)rTat-HIV-1rTat-HIV1rTat-HIV 1