bak

This peptide, generated from the BH3 domain of Bak (Flu-BakBH3), has been shown to have high-affinity binding to a surface pocket of the Bcl-XL protein that is required for its death antagonist function.

Bak BH3 (72-87), TAMRA-labeled, is a bioactive peptide.

PUMA BH3 acetate (PUMA BH3 Free base) is a p53 positive regulator of apoptosis (PUMA) BH3 domain polypeptide that acts as a direct activator of Bak with a Kd of 26 nM.

PUMA BH3 (TFA) is a p53 upregulated modulator of apoptosis (PUMA) BH3 domain peptide, acts as a direct activator of Bak, with a Kd of 26 nM.

Bid BH3 (80-99) is a biologically active peptide known as a pro-apoptotic member of the 'BH3-only' (BOPS) subset within the BCL-2 protein family, pivotal in apoptosis regulation. It notably interacts with Bcl-2, Bax, and Bak, initiating their activation or inactivation, thus inducing cell death. Additionally, Bid translocates from the cytosol to the mitochondrial membrane as part of its functional mechanism. The presence of Pyroglutamyl (pGlu) peptides, which can spontaneously arise from Glutamine (Q) or Glutamic acid (E) at the N-terminus of sequences, is a natural process. The hydrophobic γ-lactam ring of pGlu is theorized to enhance peptide stability, providing resistance to gastrointestinal proteases, making these peptides a recognized variant within peptide analyses, including HPLC purity assessments.

PUMA BH3 (TFA), a peptide from the BH3 domain of the p53 upregulated modulator of apoptosis (PUMA), directly activates Bak with a dissociation constant (Kd) of 26 nM [1].

PUMA BH3 is a p53 upregulated modulator of apoptosis (PUMA) BH3 domain peptide, acts as a direct activator of Bak, with a Kd of 26 nM.This is a PUMA BH3 domain peptide. PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome C releas

LTX-315 (Oncopore), the oncolytic peptide, inhibits cancer cells through Bax/Bak-regulated mitochondrial membrane permeabilization.

PUMA BH3, a peptide that includes the BH3 domain from the p53-upregulated modulator of apoptosis (PUMA) and activates the pro-apoptotic protein Bak, demonstrates binding affinity to Bak with dissociation constants (Kds) of 290 nM in HEPES buffer and 26 nM in CHAPS buffer. This interaction with Bak induces its homo-oligomerization and facilitates Bak-mediated membrane permeabilization.

BH3 hydrochloride, a peptide that crosses the blood-brain barrier, induces apoptosis either through direct activation of the pro-apoptotic proteins Bax/Bak or by inhibiting anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1, and A-1) through their BH3 domain [1][2].