China HIV-1 tat Protein (49-57) CAS NO.123251-89-8 Factories, Products

The primary biological mechanism of HIV-1 tat Protein (49-57) relies on its uniquely high positive charge density, derived from a sequence rich in arginine and lysine residues, which enables efficient translocation across the hydrophobic cell membrane lipid bilayer. Initially, the peptide engages in electrostatic interactions with anionic components on the cell surface, primarily heparan sulfate proteoglycans (HSPGs), which concentrate the peptide at the membrane interface. Following this adsorption, the peptide utilizes energy-dependent endocytic pathways, such as macropinocytosis, or potentially direct translocation mechanisms involving the formation of transient pores or inverted micelles, to traverse the plasma membrane. Once internalized, this cationic peptide can escape endosomal entrapment and release its conjugated bioactive cargo into the cytosol or facilitate nuclear localization, thereby bypassing the limitations of traditional membrane impermeability for large therapeutic molecules.

This product is indicated for preclinical research applications targeting professionals in drug delivery, molecular biology, and biochemistry who are engineering novel therapeutics, vaccines, and diagnostic probes capable of crossing biological barriers. It is particularly suitable for researchers utilizing the peptide as a covalent linker or fusion tag to deliver biologically active cargos like siRNAs, plasmids, antibodies, enzymes, and imaging agents into difficult-to-transfect cell lines and primary cells without the need for physical disruption or viral vectors. Furthermore, it is applicable for cell penetration studies, investigating the structure-activity relationships of arginine-rich motifs, and serving as a positive control or standard reference in assays measuring cellular uptake efficiency, endocytosis inhibition, and the development of next-generation non-viral transfection reagents in controlled laboratory settings.

As a raw biochemical research reagent not formulated for human therapeutic use, HIV-1 tat Protein (49-57) does not possess approved clinical efficacy, yet it demonstrates profound functional efficacy in extensive in vitro and in vivo preclinical studies as a delivery vehicle. Experimental data confirm that conjugating this peptide to various macromolecules—ranging from large proteins like β-galactosidase and antibodies to nucleic acids like DNA and siRNA—significantly enhances their cellular internalization rates and allows them to exert their biological functions intracellularly. Additionally, research validates its utility in animal models where systemic administration of Tat-fused proteins leads to tissue distribution and therapeutic effects, such as targeted tumor regression or gene silencing, underscoring its powerful role as a foundational tool in the design and optimization of clinically viable cell-penetrating peptide technologies rather than acting as a standalone drug.

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