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BH3 hydrochloride, a BBB penetrated peptide, provoke apoptosis either by direct activation of pro-apoptotic Bax/Bak or by neutralizing anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1 and A-1) via their BH3 domian .
BH3I-1 is a Bcl-2 family antagonist, which inhibits the binding of the BakBH3 peptide to Bcl-xL with a Ki of 2.4±0.2 μM in FP assay. BH3I-1 has a Kd of 5.3 μM against the p53/MDM2 pair.
Bad BH3 (mouse) is a biological active peptide. (This is a bcl-2 binding peptide. This peptide is derived from the BH3 domain (a death domain) of Bad, amino acid residues 140 to 165.)
r8 Bid BH3 is a biological active peptide. (The Bid BH3 is a pro-apoptotic member of the 'BH3-only' subset of BCL-2 family proteins that constitute a critical control point in apoptosis. r8BIDBH3 is lethal to human leukemia cell lines that expresse Bcl-2. The Bcl-2 antagonists may have the potential to be efficacious in cancer therapy. Poly-D-arginine (d-isomer as denoted by rrrrrrrr) is fused to the Bid BH3 peptide to facilitate cellular uptake of the peptide.)
r8-Gly-Noxa A BH3 is a biological active peptide. (This cell permeable peptide is derived from the BH3 domain (a death domain) of Noxa A, amino acid residues 17 to 36. Eight D-Arginine residues and a Glycine linker residue are added to the amino terminal of the peptide.)
Bid BH3 (80-99) is a biological active peptide. (BID is a pro-apoptotic member of the 'BH3-only' (BOPS) subset of the BCL-2 family of proteins that constitute a critical control point in apoptosis. Bid is the first of the BOPs reported to bind and activate Bcl-2, Bax, and Bak. Bid serves as a death-inducing ligand that moves from the cytosol to the mitochondrial membrane to inactivate Bcl-2 or to activate Bax.Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.)
BMf-BH3 (BMF-Y) belongs to the Bcl-2 apoptosis mediator family. BH3-only protein, Bmf is a key molecule for histone deacetylase (HDAC) inhibitors mediated enhancing effect on ionizing radiation-induced cell death .
Murizatoclax (AMG 397) is a potent, selective and orally active inhibitor of myeloid leukemia 1 (MCL-1) inhibitor, with a Ki of 15 pM. Murizatoclax competitive binds to the BH3-binding groove of MCL1 with pro-apoptotic BCL-2 family members. Murizatoclax can be used for the research of cancer .
BFC1108 is a small molecule Bcl-2 functional converter. BFC1108 induces a conformational change in Bcl-2, resulting in the exposure of its BH3 domain both in vitro and in vivo. BFC1108 effectively induces apoptosis in Bcl-2 expressing cancers. .
(S)-Gossypol is the isomer of a natural product Gossypol. (S)-Gossypol binds to the BH3-binding groove of Bcl-xL and Bcl-2 proteins with high affinity.
Obatoclax Mesylate (GX15-070 Mesylate), a BH3 mimetic, is a pan-BCL-2 family proteins inhibitor with a Ki of 220 nM for BCL-2 . Obatoclax Mesylate induces autophagy-dependent cell death and targets cyclin D1 for proteasomal degradation. Obatoclax Mesylate has anti-cancer and broad-spectrum antiparasitic activity [3] .
Obatoclax (GX15-070), a BH3 mimetic, is a pan-BCL-2 family proteins inhibitor with a Ki of 220 nM for BCL-2 . Obatoclax induces autophagy-dependent cell death and targets cyclin D1 for proteasomal degradation. Obatoclax has anti-cancer and broad-spectrum antiparasitic activity [3] .
CBI1 is a covalent BAX inhibitor. CBI1 selectively derivatizes BAX at C126 and inhibits BAX activation by triggering ligands or point mutagenesis. CBI1 blocks t-2-hex lipidation and oligomerization of BAX. CBI1 inhibits BAX activation induced by BH3 ligands, F116A mutagenesis or t-2-hex .
AZD4320 is a novel BH3-mimicking dual BCL2/BCLxL inhibitor with IC50s of 26 nM, 17 nM, and 170 nM for KPUM-MS3, KPUM-UH1, and STR-428 cells, respectively.
ABT-737, a BH3 mimetic, is a potent Bcl-2, Bcl-xL and Bcl-w inhibitor with EC50s of 30.3 nM, 78.7 nM, and 197.8 nM, respectively. ABT-737 induces the disruption of the BCL-2/BAX complex and BAK-dependent but BIM-independent activation of the intrinsic apoptotic pathway. ABT-737 induces autophagy and has the potential for acute myeloid leukemia (AML) research [3].
Chelerythrine chloride is a potent, cell-permeable inhibitor of protein kinase C, with an IC50 of 660 nM. Chelerythrine chloride inhibits the Bcl-XL-Bak BH3 peptide binding with IC50 of 1.5 μM and displaces Bax from Bcl-XL. Chelerythrine chloride induces apoptosis and autophagy.
BAD (103-127) (human), FAM-labeled is a FAM-labeled human BAD (103-127) (HY-P2468). BAD (103-127) (human), the 25-mer Bad peptide, is derived from the BH3 domain of BAD, can antagonize the function of Bcl-xL .
BI-6C9 is a highly specific BH3 interacting domain (Bid) inhibitor, which prevents mitochondrial outer membrane potential (MOMP) and mitochondrial fission, and protects the cells from mitochondrial apoptosis inducing factor (AIF) release and caspase-independent cell death in neurons .
BAD (103-127) (human), the 25-mer Bad peptide, is derived from the BH3 domain of BAD, can antagonize the function of Bcl-xL. BAD (103-127) (human) is reported to have almost 800-fold higher affinity for Bcl-XL than the 16-mer peptide .
UMI-77 is a selective Mcl-1 inhibitor, which shows high binding affinity to Mcl-1 (IC50=0.31 μM). UMI-77 binds to the BH3 binding groove of Mcl-1 with Ki of 490 nM, showing selectivity over other members of anti-apoptotic Bcl-2 members.
Chelerythrine is a natural alkaloid, acts as a potent and selective Ca 2+/phospholopid-dependent PKC antagonist, with an IC50 of 0.7 μM . Chelerythrine has antitumor, antidiabetic and anti-inflammatory activity . Chelerythrine inhibits the BclXL-Bak BH3 peptide binding with IC50 of 1.5 μM and displaces Bax from BclXL. Chelerythrine triggers apoptosis and autophagy[3] .
UMI-77-d4 is the deuterium labeled UMI-77. UMI-77 is a selective Mcl-1 inhibitor, which shows high binding affinity to Mcl-1 (IC50=0.31 μM). UMI-77 binds to the BH3 binding groove of Mcl-1 with Ki of 490 nM, showing selectivity over other members of anti-apoptotic Bcl-2 members.
ABT 737-d8 is the deuterium labeled ABT-737. ABT-737, a BH3 mimetic, is a potent Bcl-2, Bcl-xL and Bcl-w inhibitor with EC50s of 30.3 nM, 78.7 nM, and 197.8 nM, respectively. ABT-737 induces the disruption of the BCL-2/BAX complex and BAK-dependent but BIM-independent activation of the intrinsic apoptotic pathway. ABT-737 induces autophagy and has the potential for acute myeloid leukemia (AML) research [3].
(S)-Sabutoclax ((S)-BI-97C1), an optically pure apogossypol derivative, is pan-active inhibitor of antiapoptotic B-cell lymphoma/leukemia-2 (Bcl-2) family proteins. (S)-Sabutoclax (Compound II) inhibits the binding of BH3 peptides to Bcl-XL, Bcl-2, Mcl-1, and Bfl-1 with IC50 values of 0.31, 0.32, 0.20, and 0.62 μM, respectively. (S)-Sabutoclax also potently inhibits cell growth of human prostate cancer, lung cancer, and lymphoma cell lines with EC50 values of 0.13, 0.56, and 0.049 μM, respectively. (S)-Sabutoclax can be used for the research of apoptosis-based therapies against cancer .
Bafetinib is an orally active Lyn/Bcr-Abl tyrosine kinase inhibitor. Bafetinib enhances the activity of several pro-apoptotic Bcl-2 homology (BH) 3-pure proteins (Bim, Bad, Bmf, and Bik) through intrinsic apoptotic pathways regulated by the Bcl-2 family, and induces apoptosis of Ph + leukemia cells. Bafetinib has antitumor activity [3].
MT 63-78 is a specific and potent direct AMPK activator with an EC50 of 25 μM. MT 63–78 also induces cell mitotic arrest and apoptosis. MT 63-78 blocks prostate cancer growth by inhibiting the lipogenesis and mTORC1 pathways. MT 63-78 has antitumor effects .
BH3 hydrochloride, a BBB penetrated peptide, provoke apoptosis either by direct activation of pro-apoptotic Bax/Bak or by neutralizing anti-apoptotic Bcl-2 proteins (Bcl-2, Bcl-XL, Bcl-w, Mcl-1 and A-1) via their BH3 domian .
Bad BH3 (mouse) is a biological active peptide. (This is a bcl-2 binding peptide. This peptide is derived from the BH3 domain (a death domain) of Bad, amino acid residues 140 to 165.)
r8 Bid BH3 is a biological active peptide. (The Bid BH3 is a pro-apoptotic member of the 'BH3-only' subset of BCL-2 family proteins that constitute a critical control point in apoptosis. r8BIDBH3 is lethal to human leukemia cell lines that expresse Bcl-2. The Bcl-2 antagonists may have the potential to be efficacious in cancer therapy. Poly-D-arginine (d-isomer as denoted by rrrrrrrr) is fused to the Bid BH3 peptide to facilitate cellular uptake of the peptide.)
r8-Gly-Noxa A BH3 is a biological active peptide. (This cell permeable peptide is derived from the BH3 domain (a death domain) of Noxa A, amino acid residues 17 to 36. Eight D-Arginine residues and a Glycine linker residue are added to the amino terminal of the peptide.)
Bid BH3 (80-99) is a biological active peptide. (BID is a pro-apoptotic member of the 'BH3-only' (BOPS) subset of the BCL-2 family of proteins that constitute a critical control point in apoptosis. Bid is the first of the BOPs reported to bind and activate Bcl-2, Bax, and Bak. Bid serves as a death-inducing ligand that moves from the cytosol to the mitochondrial membrane to inactivate Bcl-2 or to activate Bax.Pyroglutamyl (pGlu) peptides may spontaneously form when either Glutamine (Q) or Glutamic acid (E) is located at the sequence N-terminus. The conversion of Q or E to pGlu is a natural occurrence and in general it is believed that the hydrophobic γ-lactam ring of pGlu may play a role in peptide stability against gastrointestinal proteases. Pyroglutamyl peptides are therefore considered a normal subset of such peptides and are included as part of the peptide purity during HPLC analysis.)
BMf-BH3 (BMF-Y) belongs to the Bcl-2 apoptosis mediator family. BH3-only protein, Bmf is a key molecule for histone deacetylase (HDAC) inhibitors mediated enhancing effect on ionizing radiation-induced cell death .
BAD (103-127) (human), FAM-labeled is a FAM-labeled human BAD (103-127) (HY-P2468). BAD (103-127) (human), the 25-mer Bad peptide, is derived from the BH3 domain of BAD, can antagonize the function of Bcl-xL .
BAD (103-127) (human), the 25-mer Bad peptide, is derived from the BH3 domain of BAD, can antagonize the function of Bcl-xL. BAD (103-127) (human) is reported to have almost 800-fold higher affinity for Bcl-XL than the 16-mer peptide .
Chelerythrine chloride is a potent, cell-permeable inhibitor of protein kinase C, with an IC50 of 660 nM. Chelerythrine chloride inhibits the Bcl-XL-Bak BH3 peptide binding with IC50 of 1.5 μM and displaces Bax from Bcl-XL. Chelerythrine chloride induces apoptosis and autophagy.
Chelerythrine is a natural alkaloid, acts as a potent and selective Ca 2+/phospholopid-dependent PKC antagonist, with an IC50 of 0.7 μM . Chelerythrine has antitumor, antidiabetic and anti-inflammatory activity . Chelerythrine inhibits the BclXL-Bak BH3 peptide binding with IC50 of 1.5 μM and displaces Bax from BclXL. Chelerythrine triggers apoptosis and autophagy[3] .
BID Protein, Human expresses in E. coli. The BH3-only protein BID, a pro-apoptotic member of the Bcl-2 family, was initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways.
BID Protein, a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. BID Protein, Mouse (His) is the recombinant mouse-derived BID protein, expressed by E. coli , with C-His labeled tag. The total length of BID Protein, Mouse (His) is 195 a.a., with molecular weight of ~22.72 kDa.
BID Protein, a pro-apoptotic member of the Bcl-2 family, is initially discovered through binding to both pro-apoptotic Bax and anti-apoptotic Bcl-2. BID is activated in the BCL-2-regulated or mitochondrial apoptosis pathway and acts as a switch between the extrinsic and intrinsic cell death pathways. BID is susceptible to proteolytic cleavage by caspases, calpains, Granzyme B and cathepsins. BID Protein, Mouse (His-GST) is the recombinant mouse-derived BID protein, expressed by E. coli , with N-His, N-GST labeled tag. The total length of BID Protein, Mouse (His-GST) is 195 a.a., with molecular weight of ~48 kDa.
ABT 737-d8 is the deuterium labeled ABT-737. ABT-737, a BH3 mimetic, is a potent Bcl-2, Bcl-xL and Bcl-w inhibitor with EC50s of 30.3 nM, 78.7 nM, and 197.8 nM, respectively. ABT-737 induces the disruption of the BCL-2/BAX complex and BAK-dependent but BIM-independent activation of the intrinsic apoptotic pathway. ABT-737 induces autophagy and has the potential for acute myeloid leukemia (AML) research [3].
UMI-77-d4 is the deuterium labeled UMI-77. UMI-77 is a selective Mcl-1 inhibitor, which shows high binding affinity to Mcl-1 (IC50=0.31 μM). UMI-77 binds to the BH3 binding groove of Mcl-1 with Ki of 490 nM, showing selectivity over other members of anti-apoptotic Bcl-2 members.
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