Caspase 12 peptide Reference: GTX28375 Three distinct signaling pathways lead to programmed cell death (apoptosis). The death receptor and mitochondrion pathways are the main ways in which the key apoptotic proteases capase-8 and caspase-9, respectively, are involved. The endoplasmic reticulum (ER) stress is the third apoptotic pathway and caspase-12 is involved. Caspase-12 is localized to the ER but not to cytoplasm or mitochondrion. Caspase-12 is activated by ER stress, including disruption of ER calcium homeostasis, and mediates ER stress-induced apoptosis. Caspase-12 is colocalized to the ER with several proteins that are involved in Alzheimers disease including g-secretase presenilin and b-amyloid precursor protein (APP). Caspase-12 mediates cytotoxicity induced by amyloid-b. Caspase-12 is ubiquitously expressed in mouse tissues.
Caspase 10 peptide Reference: GTX28377 Caspases are a family of intracellular proteases that mediate cell death and are the principal effectors of apoptosis. Caspase 1 (Mch4, ICE-LAP4, FLICE2) plays an important role in apoptosis induced by a variety of inducers such as TNF alpha and Anti-Fas antibody. It is a large prodomain caspase classified together with caspases 2, 8, and 9 as a signaling caspase. Four isoforms of caspase 1 (caspase 1a, 1b, 1c, and 1d) having the same prodomain but different mature large and small subdomain, have been described. Caspase 1 contains two death domains (DED) involved in linking to the death effector domain of the adapter protein FADD and recruiting the complex to TNFR1 and Fas. The inactive procaspase 1 is variably expressed in many tissues and cell lines as a cytosolic protein. The mature form of caspase 1 comprises two subunits, p23/p17 (splice isoforms) and p12. Interestingly, a caspase 9- dependent processing of caspase 1 by caspase 6 in cell-free extracts has recently been suggested. Caspase 1 can cleave and activate caspases 3, 4, 6, 7, 8, and 9. This is followed by cleavage of numerous key proteins, including the nuclear protein PARP.
DcR2 / CD264 peptide Reference: GTX28379 Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. TRAIL/Apo2L, a member of the TNF family, induces apoptosis of a variety of tumor cell lines. DR4 and DR5 are functional receptors for TRAIL, and DcR1/TRID is a decoy receptor. Another member of the TRAIL receptor family was identified and designated DcR2 (Marsters et al., 1997; Degli-Esposti et al., 1997; Pan et al., 1998). The DcR2 receptor is 386 amino acids in length and has an extracellular TRAIL binding domain, but lacks intracellular death domain and does not induce apoptosis. Although this receptor binds to the cytotoxic ligand TRAIL, it contains a truncated death domain and functions as an inhibitory receptor. When overexpressed, the DcR2 receptor can protect cells against TRAIL mediated cytotoxicity. Like DR4 and DR5, DcR2 transcript is widely expressed in a variety of normal human tissues but DcR2 is absent in most tumors. Ultraviolet radiation has been shown to upregulate DcR2 expression on human keratinocytes. Over expression of DcR2 attenuated TRAIL induced apoptosis.
Diablo peptide Reference: GTX28380 This gene encodes an inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. Multiple polyadenylation sites have been found for this gene. Several alternatively spliced transcript variants that encode distinct isoforms have been described for this gene but the validity of some transcripts, and their predicted ORFs, has not been determined conclusively.
Diablo peptide Reference: GTX28381 This gene encodes an inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. Multiple polyadenylation sites have been found for this gene. Several alternatively spliced transcript variants that encode distinct isoforms have been described for this gene but the validity of some transcripts, and their predicted ORFs, has not been determined conclusively.
SODD peptide Reference: GTX28382 Several cell surface receptors that are involved in apoptosis contain intracellular death domains and are capable of triggering apoptosis when activated by their respective ligands. Due to presence of these death domains and presence of various stimuli in the serum as well as overexpression leading to receptor oligomerization, which leads to constitutive activation of the apoptotic pathway, it has been extremely difficult to generate permanent cell lines overexpressing specific receptors in culture. However, in normal states, this death domain activity is silenced presumably due to presence of other cellular factors. Recently, a DR3 associated protein has been isolated by yeast two-hybrid interaction assays. This cDNA encoding a 457-amino acid protein has been named as SODD (Silencer of Death Domain). SODD also associates with the intracellular domains of TNF-R1, but not with those of TNF-R2, Fas, DR4, or DR5. SODD overexpression suppressed the TNF induced cell death as well as NF-kB activation. SODD may act as a negative regulatory protein that is normally associated with death domain of TNF-R1 and probably inhibit self-oligomerization properties of death domain and maintain TNF-R1 in an inactive, monomeric state.