bh3

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.

r8 Bid BH3, a biologically active peptide, is a pro-apoptotic member of the BH3-only subset within the BCL-2 family proteins, pivotal in regulating apoptosis. This compound exhibits lethality towards Bcl-2-expressing human leukemia cell lines, indicating its promise as a potential cancer therapeutic. The peptide is conjugated with poly-D-arginine (denoted by rrrrrrrr), enhancing cellular uptake.

Hrk BH3, a biologically active peptide comprising the BH3 domain of Hrk, exhibits functionality within cellular processes.

BMf-BH3 belongs to the Bcl-2 apoptosis mediator family. This peptide belongs to the Bcl-2 apoptosis mediator family. Bmf is a key player in histone deacetylase (HDAC) inhibition, which alters the balance between deacetylation and acetylation.

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].

Bid BH3 (80-99) is a biologically active peptide and a pro-apoptotic member of the 'BH3-only' (BOPS) subset within the BCL-2 protein family, crucial in apoptosis regulation. It interacts with Bcl-2, Bax, and Bak to initiate their activation or inactivation, inducing cell death. Bid translocates from the cytosol to the mitochondrial membrane as part of its mechanism. Pyroglutamyl (pGlu) peptides, which can arise from Glutamine (Q) or Glutamic acid (E) at the N-terminus, have a hydrophobic γ-lactam ring that enhances stability and provides resistance to gastrointestinal proteases. These peptides are recognized variants in peptide analyses, including HPLC purity assessments.

Bad BH3 (mouse) is a bioactive peptide derived from the BH3 domain (a death domain) of Bad, comprising amino acid residues 140 to 165, and functions by binding to bcl-2.

Bik BH3, a biologically active peptide derived from the BH3 domain of BIK, exhibits specific functions pertinent to its origin.

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

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

FAM-labeled Bid BH3 (80-99) is a biologically active peptide featuring a 5-FAM label at its N-terminus.

r8-Gly-Noxa A BH3 is a biologically active, cell-permeable peptide comprising amino acid residues 17 to 36 from the BH3 (death) domain of Noxa A, modified by eight D-Arginine residues and a Glycine linker at its amino terminus.

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.

Bim BH3, Peptide IV TFA is a 26-site residue of BH3 protein Bim, belonging to the pro-apoptotic group of bcl-2 protein family.

Bim BH3 is a bioactive peptide that belongs to the pro-apoptotic Bcl-2 family of proteins.

Bim BH3, Peptide IV TFA, is a 26-residue peptide derived from the BH3-only protein Bim, a member of the pro-apoptotic Bcl-2 protein family [1] [2].

This Bim peptide belongs to the pro-apoptotic group of the Bcl-2 family of proteins.

Noxa A BH3, a bioactive peptide, encompasses the BH3 domain of the Noxa protein.

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.

Bax BH3 peptide (55-74), wild type is a 20-amino acid peptide (Bax 1) known for its apoptosis-inducing capability in various cell line models.

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].

Angiopep-Bim BH3 hydrochloride, a peptode that penetrates the blood-brain barrier (BBB), may serve as a tool to study the permeability of central nervous system (CNS) therapeutics [1].

Noxa B BH3, a biologically active peptide encompassing the BH3 domain of the Noxa protein, displays targeted biological activity.

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.

BAD (103-127) (human) acetate is a 25-mer Bad polypeptide from the BAD BH3 domain that antagonizes the effects of Bcl-xl.

NoxaBH3, a cysteine-based cross-linked peptide, exhibits enhanced cell permeability and greater inhibitory efficacy against Mcl-1. It binds to the endogenous CXCR4 ligand, resulting in the formation of a ubiquitin-NoxaBH3 conjugate that is subsequently delivered to cancer cells [1].

BAD (103-127) (human), a FAM-labeled 25-mer peptide derived from the BH3 domain of human BAD, antagonizes the function of Bcl-xL [1].

BAD (103-127) (human) is a 25-mer peptide obtained from the BH3 domain of BAD. It effectively counteracts the activity of Bcl-xL. Notably, BAD (103-127) (human) exhibits an approximately 800-fold greater binding affinity for Bcl-xL compared to the 16-mer peptide.