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Catalog Number: (10231-974)
Supplier: Bioss
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (10328-316)
Supplier: Bioss
Description: Cleaves P(1)-P(3)-bis(5'-adenosyl) triphosphate (Ap3A) to yield AMP and ADP. Can also hydrolyze P(1)-P(4)-bis(5'-adenosyl) tetraphosphate (Ap4A), but has extremely low activity with ATP. Modulates transcriptional activation by CTNNB1 and thereby contributes to regulate the expression of genes essential for cell proliferation and survival, such as CCND1 and BIRC5. Plays a role in the induction of apoptosis via SRC and AKT1 signaling pathways. Inhibits MDM2-mediated proteasomal degradation of p53/TP53 and thereby plays a role in p53/TP53-mediated apoptosis. Induction of apoptosis depends on the ability of FHIT to bind P(1)-P(3)-bis(5'-adenosyl) triphosphate or related compounds, but does not require its catalytic activity, it may in part come from the mitochondrial form, which sensitizes the low-affinity Ca(2+) transporters, enhancing mitochondrial calcium uptake. Functions as tumor suppressor.


Catalog Number: (10232-004)
Supplier: Bioss
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (10232-002)
Supplier: Bioss
Description: Accelerates programmed cell death by binding to, and antagonizing the apoptosis repressor BCL2 or its adenovirus homolog E1B 19k protein. Under stress conditions, undergoes a conformation change that causes translocation to the mitochondrion membrane, leading to the release of cytochrome c that then triggers apoptosis. Promotes activation of CASP3, and thereby apoptosis.


Catalog Number: (10107-330)
Supplier: Prosci
Description: PEG3 induces apoptosis in cooperation with SIAH1A and acts as a mediator between TP53/p53 and BAX in a neuronal death pathway that is activated by DNA damage. PEG3 acts synergistically with TRAF2 and inhibits TNF induced apoptosis through activation of NF-kappa-B. PEG3 also possesses a tumor suppressing activity in glioma cells.


Catalog Number: (77438-750)
Supplier: Bioss
Description: DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA.


Catalog Number: (89415-386)
Supplier: Prosci
Description: Survivin Antibody: Apoptosis, or programmed cell death, is related to many diseases, such as cancer. Apoptosis is triggered by a variety of stimuli including members in the TNF family and prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. A novel IAP protein was recently identified and designated survivin, apoptosis inhibitor 4 (API4), and TIAP. Survivin/TIAP interacted with the processed form of caspase-3 and inhibited its proteolytic activity. Survivin/TIAP is predominantly expressed in tissues of embryos, transformed cell lines, and many human cancers and lymphomas.


Catalog Number: (10813-702)
Supplier: Prosci
Description: Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. Implicated in Notch signaling cross-over.


Catalog Number: (75793-246)
Supplier: Prosci
Description: PIDD promotes apoptosis downstream of the tumor suppressor as component of the DNA damage/stress response pathway that connects p53/TP53 to apoptosis. It associates with NEMO/IKBKG and RIP1 and enhances sumoylation and ubiquitination of NEMO/IKBKG which is important for activation of the transcription factor NF-kappa-B. It associates with caspase-2 and RAIDD, and induces activation of caspase-2 which is an important regulator in the apoptotic pathways.


Catalog Number: (75790-850)
Supplier: Prosci
Description: Cytochrome C (CYCS) is a small heme protein that belongs to the cytochrome c family. It is found loosely associated with the inner membrane of the mitochondrion. Cytochrome C is a highly soluble protein that functions as a central component of the electron transport chain in mitochondria. CYCS transfers electrons between Complexes III (Coenzyme Q - Cyt C reductase) and IV (Cyt C oxidase). CYCS plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of Cytochrome C to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.


Catalog Number: (10813-724)
Supplier: Prosci
Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.


Catalog Number: (10419-944)
Supplier: Bioss
Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.


Catalog Number: (10420-340)
Supplier: Bioss
Description: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions including proliferation, differentiation, apoptosis, survival and oncogenic transformation. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that comprises a sequential phosphorylation of the dual-specific MAPK kinases (MAP2K1/MEK1 and MAP2K2/MEK2) and the extracellular signal-regulated kinases (MAPK3/ERK1 and MAPK1/ERK2). The phosphorylated form of RAF1 (on residues Ser-338 and Ser-339, by PAK1) phosphorylates BAD/Bcl2-antagonist of cell death at 'Ser-75'. Phosphorylates adenylyl cyclases: ADCY2, ADCY5 and ADCY6, resulting in their activation. Phosphorylates PPP1R12A resulting in inhibition of the phosphatase activity. Phosphorylates TNNT2/cardiac muscle troponin T. Can promote NF-kB activation and inhibit signal transducers involved in motility (ROCK2), apoptosis (MAP3K5/ASK1 and STK3/MST2), proliferation and angiogenesis (RB1). Can protect cells from apoptosis also by translocating to the mitochondria where it binds BCL2 and displaces BAD/Bcl2-antagonist of cell death. Regulates Rho signaling and migration, and is required for normal wound healing. Plays a role in the oncogenic transformation of epithelial cells via repression of the TJ protein, occludin (OCLN) by inducing the up-regulation of a transcriptional repressor SNAI2/SLUG, which induces down-regulation of OCLN. Restricts caspase activation in response to selected stimuli, notably Fas stimulation, pathogen-mediated macrophage apoptosis, and erythroid differentiation.


Catalog Number: (10461-256)
Supplier: Bioss
Description: Apoptosis is regulated by death domain (DD) and/or caspase recruitment domain (CARD)bcontaining molecules and a caspase family of proteases. CARD containing cell death regulators include RAIDD, RICK, BCL10, Apaf 1, caspase 9 and caspase 2. Apoptosis repressor with CARD is a CARD domain containing protein that interacts with caspase 2 and 8 to inhibit enzymatic activity of caspase 8. Apoptosis repressor with CARD suppresses apoptosis induced by cell death adapters FADD and TRADD and by cell death receptors Fas, TNFR 1, and DR3. The mRNA of Apoptosis repressor with CARD is primarily expressed in skeletal muscle and cardiac tissue. The nuclear isoform (1/Nop30) may be involved in RNA splicing and the cytoplasmic isoform (2/Myp) may inhibit apoptosis.


Catalog Number: (10749-324)
Supplier: Prosci
Description: DRAK1 Antibody: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 for DAP kinase-related apoptosis-inducing protein kinases. DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. Overexpression of DRAK1 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK1 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.


Catalog Number: (10749-326)
Supplier: Prosci
Description: DRAK2 Antibody: Apoptosis is mediated by death domain containing adapter molecules and a caspase family of proteases. Certain serine/threonine protein kinases, such as ASK-1 and RIP, are mediators of apoptosis. Two novel serine/threonine kinases that induce apoptosis were recently identified and designated DRAK1 and DRAK2 (for DAP kinase-related apoptosis-inducing protein kinases). DRAKs contain an N-terminal kinase domain and a C-terminal regulation domain. Overexpression of DRAK2 induces apoptosis. DRAKs have high sequence homology to DAP and ZIP kinases, and they represent a novel family of serine/threonine kinases, which mediates apoptosis through their catalytic activities. DRAK2 is located in nucleus and the messenger RNA was ubiquitously expressed in human tissues.


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