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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 .
BFC1103 is a small-molecule compound whose primary mechanism of action involves interaction with a specific domain of Bcl-2, particularly its loop domain. This interaction induces a conformational change in Bcl-2, exposing its BH3 (Bcl-2 homology 3) domain, thereby switching Bcl-2's function from anti-apoptotic to pro-apoptotic. The cell death induced by BFC1103 is dependent on the presence of Bax or Bak, both of which are key proteins involved in the intrinsic apoptotic pathway mediated by mitochondria. BFC1103 has successfully inhibited lung metastasis of triple-negative breast cancer in mouse models. It can be utilized in studying the roles of Bcl-2 family proteins in cancer development and how they impact the survival and proliferation of cancer cells .
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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