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Products
Pharmacology
Type
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- Custom services
- Ordering
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- Technical support
- Resources
Tat-D3S2
Cat. No. PP-340
Structure:
H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Gly-Ser-Lys-Ser-Gly-Asp-Gly-Asn-Arg-Ala-Leu-Gln-Arg-His-Val-Ile-Ala-Arg-OH
Other Names:
DIRAS3 switch II-derived peptide, TatD3S2
Activity:
DIRAS3 - beclin1 interaction inhibitor
Tat-D3S2 is a peptide derived from the sequence of the switch II region of the small GTPase DIRAS3, conjugated with the HIV-1 Tat protein transduction domain to enhance cellular permeability. DIRAS3 can induce autophagy and plays an important role in forming the autophagosome initiation complex (AIC) with beclin1. In disease states autophagy can protect cancer cells from acute starvation and enhance resistance to chemotherapy. Due to similarity to the binding region of DIRAS3, Tat-D3S2 can bind to beclin 1 and inhibit the beclin1 - DIRAS3 interaction necessary for the induction of autophagy, and in ovarian cancer cells where autophagy is induced by amino acid deprivation, Tat-D3S2 significantly inhibits cell viability.
Sutton et al (2019) DIRAS3-Derived Peptide Inhibits Autophagy in Ovarian Cancer Cells by Binding to Beclin1. Cancers 11(4) 557 PMID: 31003488
Related areas
All cell penetrating peptides >
All protein-protein interaction modulators >
All regulated cell death research categories >
All cancer research categories >
Technical Data
| Structure | H-Tyr-Gly-Arg-Lys-Lys-Arg-Arg-Gln-Arg-Arg-Arg-Gly-Gly-Ser-Lys-Ser-Gly-Asp-Gly-Asn-Arg-Ala-Leu-Gln-Arg-His-Val-Ile-Ala-Arg-OH |
| Molecular Weight | 3521.02 |
| Formula | C144H255N65O39 |
| Sequence | YGRKKRRQRRRGGSKSGDGNRALQRHVIAR |
| Modifications | None |
Solubility and Storage
| Solubility | Soluble in water |
| Appearance | Freeze dried solid |
| Storage | Store dry, frozen and in the dark |
Batch Specific Data
| Purity | >95% by hplc |
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Recent citations
A new publication from the University of Ljubljana uses MCA-AVLQSGFR-Lys(Dnp)-Lys-NH2, the FRET substrate for the severe acute respiratory syndrome coronavirus main protease (SARS-CoV Mpro), to determine the inhibitory potential of plant polyphenols
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