"Prosci"

Supplier: Prosci

DR4 Antibody: Apoptosis, or programmed cell death, occurs during normal cellular differentiation and development of multicellular organisms. Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors, TNFR1 and Fas. A novel death domain containing receptor was recently identified and designated DR4 (for death receptor 4). The ligand for this novel death receptor has been identified and termed TRAIL, which is a new member in the TNF family. DR4 is also called TRAIL receptor-1 (TRAIL-R1). DR4 is expressed in most of human tissues including spleen, peripheral blood leukocytes, small intestine and thymus. Like TNFR1, Fas and DR3, DR4 mediates apoptosis and NF-kappa B activation in many tissues and cells.

Supplier: Prosci

Bonzo Antibody: Human immunodeficiency virus (HIV) and simian immunodeficiency virus (SIV) require coreceptors, in addition to CD4, to infect target cells. Some G protein-coupled receptors including CCR5, CXCR4, CCR3, and CCR2b in the chemokine receptor family have been identified as HIV coreceptors. An orphan G protein-coupled receptor was recently cloned and designated Bonzo, STRL33 and TYMSTR, and identified as HIV and SIV coreceptor. Bonzo/STRL33 is used by SIV, HIV-2 and HIV-1. The messenger RNA of Bonzo/STRL33 is expressed in lymphoid tissues and activated peripheral blood lymphocytes.

Supplier: Prosci

ICAD Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A human DNA fragmentation factor (DFF) was identified recently which is cleaved by caspase-3 during apoptosis. Mouse homologue of human DFF was identified as a DNase inhibitor designated ICAD, for inhibitor of caspase-activated DNase. Upon cleavage of DFF/ICAD, a caspase activated deoxyribonuclease (CAD) is released and activated and eventually causes the degradation of DNA in the nuclei. Therefore, the cleavage of CAD inhibitor molecule DFF/ICAD, which causes DNase activation and DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

ICAD Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A human DNA fragmentation factor (DFF) was identified recently which was cleaved by caspase-3 during apoptosis. Mouse homologue of human DFF was identified as a DNase inhibitor designated ICAD, for inhibitor of caspase-activated DNase. Upon cleavage of DFF/ICAD, a caspase activated deoxyribonuclease (CAD) is released and activated and eventually causes the degradation of DNA in the nuclei. Therefore, the cleavage of CAD inhibitor molecule DFF/ICAD, which causes DNase activation and DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

CAD Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD (for caspase activated deoxyribonuclease). The human homologue of mouse CAD was more recently identified by two groups independently and termed CPAN and DFF40. Human DFF45 and its mouse homologue ICAD are the inhibitors of CPAN/DFF40 and CAD, respectively. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually causes the degradation of DNA in the nuclei. Activation of CAD/DFF40, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

CAD Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. A mouse DNase that causes DNA fragmentation was identified recently and designated CAD (for caspase activated deoxyribonuclease). The human homologue of mouse CAD was more recently identified by two groups independently and termed CPAN and DFF40. Human DFF45 and its mouse homologue ICAD are the inhibitors of CPAN/DFF40 and CAD, respectively. Upon cleavage of DFF45/ICAD by activated caspase, DFF40/CAD is released and activated and eventually causes the degradation of DNA in the nuclei. Activation of CAD/DFF40, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

Apaf1 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homologues of the key cell death gene CED-4 in C. elegans has been identified recently from human and mouse and designated Apaf1 (for apoptosis protease-activating factor 1). Apaf1 binds to cytochrome c (Apaf-2) and caspase-9 (Apaf-3), which leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 is ubiquitously expressed in human tissues.

Supplier: Prosci

Apaf1 Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. The mammalian homologous of the key cell death gene CED-4 in C. elegans was identified recently from human and mouse and designated Apaf1 for apoptosis protease-activating factor 1. Apaf1 binds to cytochrome c (Apaf2) and caspase-9 (Apaf3), which leads to caspase-9 activation. Activated caspase-9 in turn cleaves and activates caspase-3 that is one of the key proteases, being responsible for the proteolytic cleavage of many key proteins in apoptosis. Apaf1 can also associate with caspase-4 and caspase-8. Apaf1 transcript is ubiquitously expressed in human tissues.

Supplier: Prosci

DR5 Antibody: Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. TRAIL/Apo2L is a new member of the TNF family. DR4 was recently identified as the receptor for TRAIL. A novel death domain containing receptor for TRAIL was more recently identified and designated DR5, Apo2, TRAIL-R2, TRICK2, or KILLER by several groups independently. Like DR4, DR5 transcript is widely expressed in normal tissues and in many types of tumor cells. DR5 binds to TRAIL and mediates TRAIL induced cell death. Overexpression of DR5 induces apoptosis and activates NF-kappa B.

Supplier: Prosci

DcR2 Antibody: Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. TRAIL/Apo2L is a new member of the TNF family and induces apoptosis of a variety of tumor cell lines. DR4 and DR5 are the recently identified functional receptors for TRAIL, and DcR1/TRID is a decoy receptor. Another member of the TRAIL receptor family was more recently identified and designated DcR2, TRAIL-R4, or TRUNDD. DcR2 has an extracellular TRAIL-binding domain but lacks intracellular death domain and does not induce apoptosis. Like DR4 and DR5, DcR2 transcript is widely expressed in normal human tissues. Overexpression of DcR2 attenuated TRAIL-induced apoptosis.

Supplier: Prosci

IKK alpha Antibody: Nuclear factor kappa B (NF-kappa B) is a ubiquitous transcription factor and an essential mediator of gene expression during activation of immune and inflammatory responses. NF-kappa B mediates the expression of a great variety of genes in response to extracellular stimuli including IL-1, TNFa, and bacteria product LPS. NF-kappa B is associated with I kappa B proteins in the cell cytoplasm, which inhibit NF-kappa B activity. The long-sought I kappa B kinase (IKK), which phosphorylates I kappa B, and mediates I kappa B degradation and NF-kappa B activation, was recently identified by several laboratories. IKK is a serine protein kinase, and the IKK complex contains alpha and beta subunits (IKK alpha and IKK beta ). IKK alpha and IKK beta interact with each other and both are essential for the NF-kappa B activation. IKK alpha specifically phosphorylates IkB-alpha. IKK alpha is expressed in variety of human tissues.

Supplier: Prosci

ADAM10 Antibody: Proinflammatory cytokine tumor necrosis factor-alpha (TNF-alpha ) contributes to a variety of inflammatory responses and programmed cell death. Notch receptor and its ligand participate in cell fate decisions during vertebrate development and are associated with several human disorders, including a T-cell lymphoma. TNF-alpha , notch and its ligand delta are all membrane-bond molecules, which are cleaved by proteases to release mature proteins or functional receptor. ADAM10, a metalloprotease-disintegrin in the family of mammalian ADAM (for a disintegrin and metalloprotease), was recently identified to cleave TNF-alpha , notch and its ligand delta. The genes encoding human, mouse, and bovine ADAM10 were recently cloned and designated ADAM 10, kuzbanian (KUZ), and MADM, respectively. ADAM10 mRNA is expressed in a variety of human and bovine tissues.

Supplier: Prosci

FLIP Antibody: Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain (DD)-containing adapter molecules and members of the ICE/CED-3 protease family. Caspases-8 (FLICE) and -10 (FLICE2) are two pivotal members in the ICE/CED-3 protease family. FLICE-inhibitory proteins were identified in virus and human and designated v-FLIPs and c-FLIPs, respectively. The human FLIPs were also cloned by several labs independently and termed Casper, I-FLICE, FLAME-1, CASH, CLARP and usurpin. FLIP contains two death effector domains (DEDs) and a caspase-like domain. FLIP interacts with adapter protein FADD and caspase-8 and 10, and potently inhibits apoptosis induced by all known death receptors CD95, DR3, TRAIL-R and TNFR1. Four splice variants of c-FLIPs have been identified and termed FLIPalpha, beta, gamma, and delta, respectively.

Supplier: Prosci

KLHL1 Antibody: The mammalian Kelch-like 1 (KLHL1) was initially discovered as a homolog to the Drosophila Kelch gene that is highly expressed in several brain tissues. The predicted protein domain structure of KLHL1 is characteristic of a number of proteins that bind actin, form dimers, and often act as actin-organizing proteins. Based on the presence of anti-sense RNA that spans the transcription and translation start sites as well as the first splice site of KLHL1 in brain tissue of individuals suffering from the neurodegenerative disorder spinocerebellar ataxia type 8 (SCA8), it has been suggested that KLHL1 is involved this disease and that regulation of KLHL1 protein may be affected by antisense RNA expression.

Supplier: Prosci

ILP-2 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 including IAP, XIAP/ILP-1/MIHA, and Livin/KIAP that bind to and inhibits specific proteases. A novel member in the IAP protein family was recently identified and designated ILP-2 for IAP-like protein-2. ILP-2 has high homology to ILP-1, but is encoded by a distinct gene that is solely expressed in testis of tested normal human tissues. ILP-2, unlike ILP-1, has no inhibitory effect on Fas and TNF induced apoptosis, but potently inhibits apoptosis induced by overexpression of Bax or by coexpression of caspase-9 with Apaf-1. ILP-2 interacts with the processed caspase-9. These results suggest that ILP-2 is a novel IAP family member with restricted specificity for caspase-9.

Supplier: Prosci

Bcl-rambo 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. Members of the Bcl-2 family are known to be critical regulators of this process. These proteins are characterized by the presence of several conserved motifs termed Bcl-2 homology (BH) domains. A novel, widely expressed member termed Bcl-rambo was recently identified. This protein is localized to mitochondria in mammalian cells and its overexpression induces apoptosis which could be blocked by co-expression of inhibitor of apoptosis proteins (IAPs) such as XIAP, cIAP1, and cIAP2. Bcl-rambo shows overall homology to the anti-apoptotic members containing BH motifs, but unlike Bcl-2, the C-terminal membrane anchor of Bcl-rambo is preceded by a unique 250 amino acid insertion. This region by itself can induce apoptosis more efficiently than the Bcl-2 homology regions, suggesting that Bcl-rambo may be important other pro-apoptotic pathways.