"Prosci"

Supplier: Prosci

DAD1 Antibody: Defender of cell death 1 (DAD1) was initially discovered in BHK21 cells as a negative regulator of programmed cell death, a process important for normal organism development and tissue homeostasis. DAD1 was later shown to be a subunit of the mammalian oligosaccharyltransferase complex and is required for its function and structural integrity. Mice lacking DAD1 express abnormal N-linked glycoproteins and undergo increased apoptotic-associated embryonic death. Furthermore, overexpression of DAD1 mRNA is seen in some human hepatocellular carcinomas, indicating it may also play a role in carcinogenesis. It should be noted that DAD1 is not related to the inhibitor of apoptosis proteins (IAP) family and does not contain any baculoviral IAP repeat (BIR) domains.

Supplier: Prosci

NAIP Antibody: Neuronal apoptosis inhibitor protein (NAIP) was the first human inhibitor of apoptosis protein (IAP) identified and was discovered by its association with the neurodegenerative disorder spinal muscular atrophy. Members of the IAP family contain one to three copies of an approximately 70 amino acid motif termed baculovirus IAP repeat (BIR); these BIRs promote protein-protein interactions with various caspases such as caspase-3, -7, and -9 as well as members of the TRAF family of signal molecules. Unlike other IAPs however, NAIP requires ATP to bind caspase-9 and is not inhibited by the IAP-inhibiting molecule Smac/DIABLO, suggesting that NAIP is unique among the IAPs in its regulation of its activity. Finally, although only one human NAIP protein has been identified, other shorter NAIP mRNA transcripts have been reported.

Supplier: Prosci

OMI Antibody: Inhibitor of apoptosis proteins (IAPs) were initially identified in baculoviruses as proteins that inhibit apoptosis of the host cells to allow time for viral replication. Cellular homologues containing at least one baculoviral IAP repeat (BIR) motif essential for their anti-apoptosis activity have been identified in yeasts and higher organisms and often act by binding and inhibiting processed caspases. The activity of these proteins can be modulated by the expression of proteins such as Smac/DIABLO and XAF-1 which displace or prevent the binding of caspases by IAPs. Recently, a mitochondrial serine protease termed Omi/HtrA2 has been found to bind IAPs. Similar to Smac, Omi possesses a conserved IAP-binding motif, but acts to cleave IAPs to irreversibly inactivate IAPs and promote apoptosis.

Supplier: Prosci

PIKE Antibody: Phosphoinositide 3 kinase enhancer (PIKE) is a recently identified nuclear GTPase that interacts with nuclear phosphoinositide 3-kinase (PI3 kinase) to stimulate its lipid kinase activity. PIKE exists in multiple isoforms; a shorter C-terminal isoform (PIKE-A) has also been identified as centaurin gamma 1. The longest isoform (PIKE-L) has been shown to bind to the adaptor protein Homer and thereby link to metabotropic glutamate receptors, leading to activation of PI3 kinase activity and prevention of neuronal apoptosis. Overexpression of PIKE-A enhances Akt activity and promotes cancer cell invasion, whereas decreased expression of PIKE-A via dominant negative expression of PIKE-A or PIKE-A knockdown inhibits these processes. In many human cancers, expression of PIKE-A is enhanced, leading to increased Akt activity and preventing apoptosis.

Supplier: Prosci

cIAP 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 can be prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. The two isoforms of c-IAP (c-IAP1 and c-IAP2) are structurally related to XIAP, containing 3 baculoviral IAP repeat (BIR) motifs that are essential and sufficient for the binding and inhibition of caspases-3, -7. The c-IAPs can associate with the death receptor TNF-R2, and mediate the ubiquitinization of TRAF2 following the binding of TNF-alpha by its receptor. Omi, a negative regulator of c-IAP, inhibits its activity by catalytically cleaving c-IAP. Another negative regulator, Smac/DIABLO, acts by enhancing the auto-ubiquitization activity of c-IAP.

Supplier: Prosci

XIAP 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 can be prevented by the inhibitor of apoptosis (IAP) proteins. IAP proteins form a conserved gene family that binds to and inhibits cell death proteases. The X-chromosome linked inhibitor of apoptosis (XIAP) contains 3 baculoviral IAP repeat (BIR) motifs that are essential and sufficient for the binding and inhibition of caspases-3, -7, and -9. Upregulation of XIAP expression can protect cells from apoptosis induced by low level radiation; conversely, decreased XIAP expression by antisense targeting resulted in increased cell death following low level radiation. Two negative regulators, termed XAF-1 and Smac, can bind and inhibit XIAP activity.

Supplier: Prosci

Bcl-2 Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. Bcl-2 is the founding member of a family of over 20 proteins that are critical regulators of apoptosis. These can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bcl-2 is an inner mitochondrial membrane protein that inhibits apoptosis. It is thought to act by interacting with pro-apoptotic Bcl-2 family members such as Bak and Bad. Overexpression of Bcl-2 has been linked to human cancers such as B-cell lymphoma and prostate cancer.

Supplier: Prosci

Bcl-2 Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. Bcl-2 is the founding member of a family of over 20 proteins that are critical regulators of apoptosis. These can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bcl-2 is an inner mitochondrial membrane protein that inhibits apoptosis. It is thought to act by interacting with pro-apoptotic Bcl-2 family members such as Bak and Bad. Overexpression of Bcl-2 has been linked to human cancers such as B-cell lymphoma and prostate cancer.

Supplier: Prosci

Bcl-xL Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. Bcl-xL is a member of the Bcl-2 family of proteins that are critical regulators of apoptosis. These can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bcl-xL is an anti-apoptotic mitochondrial protein related to Bcl-w and the major transcript of the bcl-x gene. Its high expression in tumors is correlated with advanced disease and poor prognosis. Bcl-xL expression level increases in response to several stimuli such as ionizing radiation and treatment with chemotherapeutic agents.

Supplier: Prosci

BAD Antibody: Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain containing pro-apoptotic proteins, such as Bax, Bid, and Bik, form a growing subclass of the Bcl-2 family. Another such protein is the Bcl-2-antagonist of cell death (Bad). Bad regulates apoptosis by forming heterodimers with anti-apoptotic proteins Bcl-2 and Bcl-xL, thereby preventing them from binding with Bax. Bad activity is regulated by its phosphorylation; it is inactivated by kinases such as Akt and MAP kinase and thus promotes cell survival, whereas JNK-induced phosphorylation promotes the apoptotic role of Bad.

Supplier: Prosci

Bak Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bak, a pro-apoptotic Bcl-2 family member, is an oligomeric protein that localizes to the mitochondria. It is thought to share significant functional homology with Bax, another pro-apoptotic Bcl-2 family member, as disruption of bak or bax has little effect on cell death, but mice lacking both genes display multiple developmental defects and cells lacking bak and bax show decreased apoptotic capability.

Supplier: Prosci

Bax Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bax, a pro-apoptotic Bcl-2 family member, is a cytosolic protein that changes conformation and translocates to the mitochondria following apoptotic stimuli. It is thought to share significant functional homology with Bak, another pro-apoptotic Bcl-2 family member, as disruption of bax or bak has little effect on cell death, but mice lacking both genes display multiple developmental defects and cells lacking both show decreased apoptotic capability.

Supplier: Prosci

Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.

Supplier: Prosci

Bid Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. Bid, a pro-apoptotic Bcl-2 family member, is cleaved by caspase-8 in response to apoptotic signals, exposing the Bcl-2 homology 3 (BH3) domain which is normally buried in the full-length protein. The cleaved complex is myris-toylated and translocated to the mitochondrial membrane where it may induce mitochondrial Bax and Bak to oligomerize.

Supplier: Prosci

BOK Antibody: Apoptosis plays a major role in normal organism development, tissue homeostasis, and removal of damaged cells. Disruption of this process has been implicated in a variety of diseases such as cancer. The Bcl-2 family of proteins is comprised of critical regulators of apoptosis that can be divided into two classes: those that inhibit apoptosis and those that promote cell death. BOK, a pro-apoptotic Bcl-2 family member, was initially identified in the ovary, and was found to interact with other Bcl-2 family members such as Mcl-1 and Bfl-1. BOK expression is high during early placental development, suggesting that it may also play a role in regulating trophoblast cell proliferation.

Supplier: Prosci

NADE Antibody: The p75 neurotrophin receptor (p75NTR) is a member of the tumor necrosis receptor superfamily and can mediate cell death and cell survival in response to nerve growth factor (NGF). The p75NTR-associated cell death executor (NADE) mediates apoptosis by interacting with the cell death domain of p75NTR following the binding of NGF by p75NTR. Recent studies have shown that NADE also interacts with second mitochondria-derived activator of caspase (Smac). Co-expression of NADE and Smac promotes TRAIL-induced apoptosis and inhibits XIAP-mediated Smac ubiquitization. It has been suggested that it is this interaction between NADE and Smac that allows apoptosis to proceed. Finally, although initially discovered as an mRNA expressed in ovarian granulosa cells, NADE has been suggested to play a role in the neuronal death seen in epileptic brain damage.