"Prosci"

Supplier: Prosci

IKK beta 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, TNF alpha , 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 NF-kappa B activation. IKK beta phosphorylates both I kappa B-alpha and I kappa B-beta. IKK beta is expressed in variety of human tissues.

Supplier: Prosci

IRAK-2 Antibody: The pro-inflammatory cytokine IL-1 induces cellular response through two subunits of its receptor, IL-1 receptor I (IL-1RI) and IL-1 receptor accessory protein (IL-1RAcP). IL-1 receptor-associated kinase (IRAK) mediates activation of NF-kappa B, which is a pivotal transcription factor mediating inflammatory and immune response. A novel member in the IRAK/Pelle family was recently identified and designated IRAK2. Both IRAK and IRAK2 recruit to the subunits of the IL-1R complex after IL-1 binding and lead to NF-kappa B activation. IRAKs also associate with Toll like receptor (TLR) and the dominant negative mutants of IRAKs inhibit LPS-induced NF-kappa B activation. Members in IRAK/Pelle family play a central role in IL-1R and TLR mediated inflammatory response. IRAK2 is expressed in a variety of human tissues.

Supplier: Prosci

MYD88 Antibody: The pro-inflammatory cytokine IL-1 induced cellular response requires IL-1 receptor complex including IL-1RI and IL-1RAcP. Recently, MyD88 was identified as an adapter molecule in the IL-1 signaling pathway. MyD88 associates with and recruits IRAK to the IL-1 receptor complex in response to IL-1 treatment and dominant negative form of MyD88 attenuates IL-1R-mediated NF-kappa B activation. MyD88 is also employed as a regulator molecule by IL-18 receptor and human Toll receptor, which are members in the Toll/IL-1R family of receptors. Targeted disruption of the MyD88 gene results in lose of cellular responses to IL-1 and IL-18, and MyD88-deficient mice lack responses to bacterial product LPS that employs Toll-like receptors 2 and 4 (TLR2 and TLR4) as the signaling receptors. MyD88 is a general adapter protein for the Toll/IL-1R family of receptors and plays an important role in the inflammatory response induced by cytokines IL-1 and IL-18 and endotoxin. MyD88 gene is expressed in many tissues.

Supplier: Prosci

MYD88 Antibody: The pro-inflammatory cytokine IL-1 induced cellular response requires IL-1 receptor complex including IL-1RI and IL-1RAcP. Recently, MyD88 was identified as an adapter molecule in the IL-1 signaling pathway. MyD88 associates with and recruits IRAK to the IL-1 receptor complex in response to IL-1 treatment and dominant negative form of MyD88 attenuates IL-1R-mediated NF-kappa B activation. MyD88 is also employed as a regulator molecule by IL-18 receptor and human Toll receptor, which are members in the Toll/IL-1R family of receptors. Targeted disruption of the MyD88 gene results in lose of cellular responses to IL-1 and IL-18, and MyD88-deficient mice lack responses to bacterial product LPS that employs Toll-like receptors 2 and 4 (TLR2 and TLR4) as the signaling receptors. MyD88 is a general adapter protein for the Toll/IL-1R family of receptors and plays an important role in the inflammatory response induced by cytokines IL-1 and IL-18 and endotoxin. MyD88 gene is expressed in many tissues.

Supplier: Prosci

IL-1RAcP Antibody: The pro-inflammatory cytokine IL-1 induced cellular response requires two subunits of its receptor, IL-1 receptor I (IL-1RI) and IL-1 receptor accessory protein (IL-1RAcP). IL-1RAcP forms a complex with IL-1RI in response to IL-1 treatment. The IL-1 receptor-associated kinase (IRAK), which mediates activation of NF-kappa B inducing kinae (NIK) and of NF-kappa B, recruits to the IL-1R complex through IL-1RAcP. IL-1 activation of stress-activated protein kinase and of acid sphingomyelinase also requires IL-1RAcP. Like IL-1RI, IL-1RAcP subunit is essential for IL-1 mediated cellular response. IL-1RAcP is expressed in many tissues.

Supplier: Prosci

IL-1RAcP Antibody: The pro-inflammatory cytokine IL-1 induced cellular response requires two subunits of its receptor, IL-1 receptor I(IL-1RI) and IL-1 receptor accessory protein (IL-1RAcP). IL-1 RAcP forms a complex with IL-1RI in response to IL-1 treatment. The IL-1 receptor-associated kinase (IRAK), which mediates activation of NF-kappa B inducing kinae (NIK) and of NF-kappa B, recruites to the IL-1R complex through IL-1 RAcP. IL-1 activation of stress-activated protein kinase and of acid sphingomyelinase also requires IL-1RAcP. Like IL-1RI, IL-1RAcP subunit is essential for IL-1 mediated cellular response. IL-1RAcP is expressed in many tissues.

Supplier: Prosci

APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the brains of all suffers of Alzheimer's disease.

Supplier: Prosci

APP Antibody: Accumulation of the amyloid-beta peptide (Abeta) in the cerebral cortex is a critical event in the pathogenesis of Alzheimer's disease. The beta-amyloid protein precursor (APP) is cleaved by beta-secretase, producing a soluble derivative of the protein and a membrane anchored 99-amino acid carboxy-terminal fragment (C99). The C99 fragment serves as substrate for gamma-secretase to generate the 4 kDa amyloid-beta peptide (Abeta), which is deposited in the brains of all suffers of Alzheimer's disease.

Supplier: Prosci

DcR3 Antibody: Apoptosis is induced by certain cytokines including TNF and Fas ligand in the TNF family through their death domain containing receptors. Several novel members in the TNFR family including DR3, DR4, DR5, and DR6 were recently discovered and function as cell death receptors. Two decoy receptors, DcR1 and DcR2, were recently identified to compete with DR4 and DR5 for their ligand TRAIL binding. A novel decoy receptor was more recently discovered and designated DcR3 and TR6, respectively,. Unlike DcR1 and DcR2, DcR3 is a soluble rather than a membrane associated molecule. DcR3 binds to FasL and LIGHT and inhibits FasL and LIGHT induced apoptosis. DcR3 transcript is expressed in a number of lung and colon carcinomas and in some normal tissues.

Supplier: Prosci

SODD Antibody: Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNF family through their death domain containing receptors, TNF-R1 and Fas. Several novel death receptors including DR3, DR4, DR5, and DR6 were recently identified. Cell death signal is transduced by death domain containing adapter molecules through the interaction with death domain of these death receptors. A novel TNF-R1 interacting protein was recently identified and designated SODD for silencer of death domains. SODD associates with the death domain of TNF-R1 and prevents constitutive activation of TNF-R1 signaling. TNF treatment releases SODD and permits adapter molecules such as TRADD recruiting to the active TNF-R1 complex, which activates TNF signaling pathways. SODD also interacts with DR3. SODD is ubiquitously expressed in human tissues and cell lines.

Supplier: Prosci

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.

Supplier: Prosci

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.

Supplier: Prosci

DFF40 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 three groups independently and termed CPAN, DFF40, and human CAD, respectively. DFF45/ICAD is the inhibitory protein of DFF40/CAD and forms complex with DFF40/CAD. 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 DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

DFF40 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 three groups independently and termed CPAN, DFF40, and human CAD, respectively. DFF45/ICAD is the inhibitory protein of DFF40/CAD and forms complex with DFF40/CAD. 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 DFF40/CAD, which causes DNA degradation, is the hallmark of apoptotic cell death.

Supplier: Prosci

DR6 Antibody: Apoptosis is induced by certain cytokines including TNF and Fas ligand of the TNF family through their death domain containing receptors, TNF-R1 and Fas. Several novel death receptors including DR3, DR4, and DR5 were recently identified. A new death domain containing receptor in the TNFR family was cloned recently and termed DR6 for death receptor-6. Like TNF-R1, DR6 interacts with death domain containing adapter molecule TRADD. Overexpression of DR6 induces apoptosis and activates NF-kappa B and JNK. DR6 is widely expressed in human tissues and cell lines. The ligand for DR6 has not been identified.

Supplier: Prosci

Bcl-10 Antibody: Apoptosis is related to many diseases including cancer. Cell death signals are transduced by death domain (DD) and caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. CARD containing cell death regulators include ARC, RAIDD, Apaf-1, caspase-9, and caspase-2. A novel CARD containing protein was recently identified by several groups and designated Bcl10, CIPER, mE10, CARMEN, CLAP. Bcl10 is a cellular homolog of the equine herpesvirus-2 E-10 gene. Overexpression of Bcl10 induces JNK, p38, and NF-kappa B activation. Bcl10 interacts with caspase-9 and enhances pro-caspase-9 processing and induces apoptosis through caspase-9 activation. Bcl10 exhibits a variety of mutations in MALT lymphomas and in B and T cell lineage lymphomas indicating that it may be commonly involved in the pathogenesis of human malignancy. Bcl10 is expressed in many human and murine tissues and cell lines.