Bcl-2 Binding Peptide, Cell-Permeable

A cell-permeable Bcl-2 binding peptide that induces apoptosis in Bcl-2 expressing cells with no apparent effect on normal peripheral lymphocytes. Also reported to diminish the growth of human myeloid leukemia in severe combined immunodeficient mice. The peptide is derived from the BH3 domain (residues 140-165, a death domain) of Bad and is modified to be cell-permeable by attaching a decanoyl moiety at the N-terminus.

A cell-permeable peptide that binds to Bcl-2 with high affinity (IC₅₀ = 130 nM in a competition binding study) and induces apoptosis. Displays antitumor activity in cells overexpressing Bcl-2 with no apparent effect on normal peripheral lymphocytes. The peptide is derived from the BH3 domain (residues 140 - 165, a “death domain”) of Bad and is modified to be cell permeant by attaching a decanoyl moiety at the N-terminus.

Cell permeable: yes

Primary Target
Bcl-2

Product does not compete with ATP.

Reversible: no

Target IC₅₀: 130 nM against Bcl-2

Packaged under inert gas

Supplied as a trifluoroacetate salt.

Following reconstitution, aliquot and freeze at -20°C. Stock solutions are stable for up to 2 weeks at -20°C.

CH₃(CH₂)₈CONH-Lys-Asn-Leu-Trp-Ala-Ala-Gln-Arg-Tyr-Gly-Arg-Glu-Leu-Arg-Arg-Met-Ser-Asp-Glu-Phe-Glu-Gly-Ser-Phe-Lys-Gly-Leu-OH

Wang, J-L., et al. 2000. Cancer Res.60, 1498.
Kelekar, A., et al. 1997. Mol. Cell. Biol.17, 7040.

CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany

Toxicity: Standard Handling (A)