Tat-Beclin 1 L11S Peptide - Scrambled Control

Unconjugated

Functional Assay

Cell-penetrating autophagy inducing peptides engineered in 2013 were demonstrated to induce autophagy through interaction with the autophagy suppressor GAPR-1/GLIPR2 (Nature, 2013; PMID 23364696). These Tat-Beclin 1 peptides were comprised of AA 267-284 of the autophagy inducer Beclin 1 (18 amino acids), a diglycine linker, and 11 amino acids of the HIV Tat protein transduction domain. Tat-Beclin 1 peptides were re-engineered to remove 7 AA from the beclin 1 domain. These shorter peptides, Tat-D11 [NBP2-49888] and Tat-L11 [NBP2-49886], demonstrate enhanced autophagy inducing function over the original Tat-Beclin 1 peptides and the inactive/scrambled control peptide Tat-L11S [NBP2-49887]. Tat-D11 and Tat-L11 are potent autophagy inducers which function both in vitro and in vivo to specifically induce autophagy while Tat-L11S is useful as a negative control. Tat-D11 and Tat-L11 peptides are comprised of 11 amino acids of the autophagy-inducing region of beclin 1 fused to the HIV Tat protein. Both Tat-D11 and Tat-L11 peptides function by binding the negative regulator of autophagy GAPR-1/GLIPR2. Upon peptide binding, beclin 1 bound to GARP-1 is released, resulting in beclin 1 mediated autophagosome formation and autophagy induction. Data indicate Tat-D11 is more potent than both Tat-L11 and Tat-Beclin 1 in vivo. In addition, initial data derived from HeLa cells also suggests Tat-D11 is more potent than Tat-L11 in vitro. However, ongoing experiments indicate Tat-L11 may be more potent than Tat-D11 in select cell lines.

3.08 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.

Peptide