PHAP peptide Reference: GTX26238 Apoptosis is related to many diseases and development. Caspase-9 plays a central role in cell death induced by a variety of apoptosis activators. Cytochrome c, after released from mitochondria, binds to Apaf-1, which forms an apoptosome that in turn binds to and activates procaspase-9. Activated caspase-9 cleaves and activates the effector caspases (caspase-3, -6 and -7), which are responsible for the proteolytic cleavage of many key proteins in apoptosis. The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were recently identified as important regulators of mitochondrion apoptosis. PHAP appears to facilitate apoptosome-mediated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both Ras- and Myc-medicated cell transformation.
PHAP peptide Reference: GTX26239 Apoptosis is related to many diseases and development. Caspase-9 plays a central role in cell death induced by a variety of apoptosis activators. Cytochrome c, after release from mitochondria, binds to Apaf-1, which forms an apoptosome that in turn binds to and activate procaspase-9. Activated caspase-9 cleaves and activates the effector caspases (caspase-3, -6 and -7), which are responsible for the proteolytic cleavage of many key proteins in apoptosis. The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were recently identified as important regulators of mitochondrion apoptosis. PHAP appears to facilitate apoptosome-mediated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both Ras- and Myc-mediated cell transformation.
ANP32A peptide Reference: GTX26240 Apoptosis is related to many diseases and development. Caspase-9 plays a central role in cell death induced by a variety of apoptosis activators. Cytochrome c, after release from mitochondria, binds to Apaf-1, which forms an apoptosome that in turn binds to and activates procaspase-9. Activated caspase-9 cleaves and activates the effector caspases (caspase-3, -6 and -7), which are responsible for the proteolytic cleavage of many key proteins in apoptosis. The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were recently identified as important regulators of mitochondrion apoptosis. PHAP appears to facilitate apoptosome-mediated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both Ras- and Myc-mediated cell transformation.
IP-10 (CXCL10), rat, recombinant Reference: E-65340 Recombinant Rat IFN Inducible Protein 10 (CXCL10)
ANP32A peptide Reference: GTX26241 Apoptosis is related to many diseases and development. Caspase-9 plays a central role in cell death induced by a variety of apoptosis activators. Cytochrome c, after release from mitochondria, binds to Apaf-1, which forms an apoptosome that in turn binds to and activates procaspase-9. Activated caspase-9 cleaves and activates the effector caspases (caspase-3, -6 and -7), which are responsible for the proteolytic cleavage of many key proteins in apoptosis. The tumor suppressor putative HLA-DR-associated proteins (PHAPs) were recently identified as important regulators of mitochondrion apoptosis. PHAP appears to facilitate apoptosome-mediated caspase-9 activation and to stimulate the mitochondrial apoptotic pathway. PHAP was also shown to oppose both Ras- and Myc-mediated cell transformation.
GRO-alpha (KC, CXCL1), rat, recombinant Reference: E-65420 Recombinant Rat Growth Regulated Oncogene alpha (KC, CXCL1)
MTA2 peptide Reference: GTX26243 The p53 tumor-suppressor gene integrates numerous signals that control cell life and death. Several novel molecules involved in the p53 pathway, including Chk2, p53R2, p53AIP1, Noxa, PIDD, and PID/MTA2, were recently discovered. The transcriptional activity of p53 is modulated by protein stability and acetylation. PID/MTA2, also termed MTA1-L1, was found to be a subunit of nucleosome remodeling and deacetylating (NRD/NuRD) complex. PID/MTA2 modulates the enzymatic activity of the histone deacetylase complex and its expression reduces the levels of acetylated p53. Deacetylation of p53 by PID/MTA2 represses p53-dependent transcriptional activation and modulates p53-mediated cell growth arrest and apoptosis. PID/MTA2 is ubiquitously expressed in human tissues.
TACI peptide Reference: GTX26244 Members in the TNF superfamily regulate immune responses and induce apoptosis. Two novel members in the TNF family were recently identified and designated BAFF/BLyS/TALL-1/THANK/zTNF4and April/TALL2, respectively. BAFF was characterized as a B cell activator since it induced B cell proliferation and immunoglobulin secretion. April regulates immunological and non-immunological cell growth. Three receptors, BCMA, TACI, and BAFF-R, for BAFF and April were recently identified. TACI, like BCMA, binds BAFF and April. TACI and its ligands regulate humoral immune responses, activate NF-kB and c-jun N-terminal kinase, and are involved in B cell associated autoimmune diseases.