139173 Results for: "Propoxyacetic+acid"

Supplier: Prosci

POLR3F Antibody: The human POLR3F is a component of RNA III polymerase. RNA polymerase III transcribes many essential, small, noncoding RNAs, including the 5S rRNAs and tRNAs. While most pol III-transcribed genes are found scattered throughout the linear chromosome maps or in multiple linear clusters, there is increasing evidence that many of these genes prefer to be spatially clustered, often at or near the nucleolus. This association could create an environment that fosters the coregulation of transcription by pol III with transcription of the large ribosomal RNA repeats by RNA polymerase I (pol I) within the nucleolus. Given the high number of pol III-transcribed genes in all eukaryotic genomes, the spatial organization of these genes is likely to affect a large portion of the other genes in a genome. POLR3F has also been recently identified as an HIV dependency factor (HDF), suggesting that POLR3F may be an important drug target in HIV treatment. At least two isoforms of POLR3F are known to exist.

Supplier: Prosci

MED28 Antibody: The mediator complex is a multi-protein transcriptional co-activator that is expressed ubiquitously in eukaryotes from yeast to mammals and is required for induction of RNA polymerase II (pol II) transcription by DNA binding transcription factor. One of the proteins in this complex is MED28, also known as Magicin. MED28 is expressed in many cell lines and tissues. It has been shown that a down-regulation of MED28 expression in NIH3T3 cells results in a significant induction of several genes associated with smooth muscle cell differentiation and conversely its over-expression represses expression of SMC genes. MED28 can also form a ternary complex with Grb2 and Merlin, the neurofibromatosis 2 tumor suppressor protein, indicating that MED28 may play a role in Merlin's tumor suppressive activity. MED28 has also been recently identified as an HIV dependency factor (HDF), suggesting that MED28 may be an important drug target in HIV treatment. At least two isoforms of MED28 are known to exist.

Supplier: Prosci

UEV1A Antibody: Ubiquitin-conjugating enzyme E2 (UEV1) was initially discovered as a protein similar in sequence and structure to the E2 ubiquitin-conjugating enzymes but lacking their enzymatic activity. There are at least two variants and multiple isoforms of UEV1. In particular, UEV1A (Ubiquitin-conjugating enzyme E2 variant 1 isoform A) has recently been shown to be an important component of the Toll-like receptor and IL-1R signaling pathway. Signals from these pathways are relayed by a number of downstream molecules such as MyD88 and tumor necrosis factor receptor associated factor (TRAF6), ultimately activating various kinases and transcription factors. UEV1A is part of a dimeric ubiquitin-conjugating enzyme complex also containing Ubc13 (ubiquitin-conjugating enzyme 13) that together with TRAF6 activates TAK1, a member of the mitogen-activated protein kinase kinase kinase family. The Ubc13-UEV1A complex also mediates the Lys-63 ubiquitination of TRAF-6, and this ubiquitination is essential for TAK1 activation.

Supplier: Prosci

TSC1 Antibody: Tuberous sclerosis complex (TSC) is an autosomal dominant tumor syndrome caused by mutations in either of the TSC1 or TSC2 tumor suppressor genes. The products of these genes form a protein complex that indirectly decreases the signaling of the mammalian Target of Rapamycin (TOR), an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. TOR activity is stimulated by Rheb, a member of the Ras superfamily of G-proteins, when the GTP/GDP ratio bound to Rheb is high. Immunoprecipitated TSC1/TSC2 has been shown to stimulate Rheb GTPase activity in vitro, suggesting that the TSC1/TSC2 decreases the ability of Rheb to stimulate TOR activity. This is supported by experiments showing overexpression of TSC1 and TSC2 results in a significant decrease in the GTP/GDP ratio bound to Rheb and the inhibition of cell growth. A shorter 40 kDa isoform of TSC1 has been shown to exist but its function is unknown.

Supplier: Rockland Immunochemical

Members in the Bcl-2 family are critical regulators of apoptosis by either inhibiting or promoting cell death. Bcl-2 homology 3 (BH3) domain is a potent death domain. BH3 domain containing pro-apoptotic proteins, including Bad, Bax, Bid, Bik, and Hrk, form a growing subclass of the Bcl-2 family. A novel BH3 domain containing protein was recently identified and designated Bcl-G. The mRNA of Bcl-G encodes 2 isoforms, Bcl-GL, which is widely expressed in multiple tissues, and Bcl-GS, which is only found in testis. The Bcl-GS protein is predominantly localized to cytoplasmic organelles whereas Bcl-GL was distributed throughout the cytosol. Overexpression of either protein induced apoptosis, although Bcl-GS was far more potent than Bcl-GS. Apoptosis induction was dependent on the BH3 domain and could be suppressed by co-expression with the anti-apoptotic Bcl-XL protein.

Supplier: Rockland Immunochemical

Rkhd2, also known as MEX3C is a member of a novel family of four homologous human MEX3 proteins each containing two heterogeneous nuclear ribonucleoprotein K homology (KH) domains and one carboxy-terminal RING finger module. MEX3 proteins, including Rkhd2, are phosphoproteins that bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1 export pathway. These proteins are a novel family of evolutionarily conserved RNA-binding proteins, differentially recruited to P bodies and potentially involved in post-transcriptional regulatory mechanisms. It has been suggested that genetic variations in Rkhd2 may be associated with susceptibility to essential hypertension type 8. Rkhd3 and Rkhd4, but not Rkhd2, co-localize with both the hDcp1a decapping factor and Argonaute (Ago) proteins in processing bodies (P bodies), recently characterized as centers of mRNA turnover.

Supplier: Rockland Immunochemical

Rkhd3, also known as MEX3B is a member of a novel family of four homologous human MEX3 proteins each containing two heterogeneous nuclear ribonucleoprotein K homology (KH) domains and one carboxy-terminal RING finger module. MEX3 proteins, including Rkhd3, are phosphoproteins that bind RNA through their KH domains and shuttle between the nucleus and the cytoplasm via the CRM1 export pathway. These proteins are a novel family of evolutionarily conserved RNA-binding proteins, differentially recruited to P bodies and potentially involved in post-transcriptional regulatory mechanisms. Rkhd3 is thought to act as a mechanism to fine-tune mRNA regulation in early Xenopus development, and with Rkhd4, but not Rkhd1, will co-localize with both the hDcp1a decapping factor and Argonaute (Ago) proteins in processing bodies (P bodies), recently characterized as centers of mRNA turnover.

Supplier: Rockland Immunochemical

Bora (Protein aurora borealis) is a key activator of Aurora Related Protein Kinase A (ARK-1), which is a centrosome-associated serine/threonine kinase that regulates centrosome maturation, bipolar spindle assembly and chromosome segregation during mitosis. Bora is localized to the nucleus until mitosis is initiated, then translocates to the cytoplasm in a Cdc2 dependent manner. Activation of Cdc2 initiates the release of Bora into the cytoplasm where it can bind and activate ARK-1. PLK1 (polo-like kinase-1) interacts with Bora to control the accessibility of its activation loop for phosphorylation and activation by ARK-1. Bora and ARK-1 cooperatively activate PLK1 and control mitotic entry. Bora mutants result in multipolar spindles in mitosis identical to those observed when ARK-1 function is blocked. Thus, the ARK1-Bora-PLK1 regulatory circuit in mammalian cells elucidates a key mechanism in cell cycle regulation. At least three isoforms of Bora are known to exist.

Supplier: Prosci

CIDE-B 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. DFF45/ICAD has been identified as inhibitor of caspase activated DNase DFF40/CAD. DFF45 related proteins CIDE-A and CIDE-B (for cell death-inducing DFF-like effector A and B) were recently identified. CIDE contains a new type of domain termed CIDE-N, which has high homology with the regulatory domains of DFF45/ICAD and DFF40/CAD. Expression of CIDE-B induces apoptosis, which is inhibited by DFF45. CIDE-B is a DFF45-inhibitable effector that promotes cell death and DNA fragmentation. CIDE-B is expressed mainly in liver and at lower levels in spleen, kidney, peripheral blood lymphocytes and bone marrow.

Supplier: Prosci

GOLPH1 Antibody: GOLPH1, also known as GCP60, was initially identified as a Golgi protein that can interact with the integral membrane protein giantin and is thought to be involved in the maintenance of the Golgi structure. GOLPH1 has also been shown to interact with other Golgi proteins such as Golgin-160, a Golgi protein that can be cleaved by caspases-2, -3, and -7, leading to the nuclear localization of Golgin-160. GOLPH1 interaction with the Golgin-160 fragments is stronger than that with the intact Golgin-160, with its interaction regulated by the oxidation state of Cys-463 within GOLPH1, suggesting that the nuclear localization of the caspase-cleaved Golgin-160 fragments is a highly coordinated event. GOLPH1 has also been found to interact with Numb, a cytosolic signaling protein that mediates asymetric cell division of neural progenitor cells to a daughter progenitor cell and a neuron, suggesting that Golgi fragmentation and reconstitution during the cell cycle differentially regulate Numb signaling through changes in GOLPH1 subcellular distribution and may couple cell fate with cell cycle progression.

Supplier: Prosci

IRGC Antibody: Immunity-related GTPases (IRG) (also known as p47 GTPases) are a family of GTPase proteins found in vertebrates, which play critical roles in mediating innate resistance to intracellular pathogens. IRG genes have been found in a number of mammals and lower species including mice, rats, zebrafish and humans. Most of the mouse genes contain interferon-stimulated response elements which mediate transcriptional activation by IFNs. In humans, only two IRG genes have been found: human IRGC encodes a full-length IRG protein that, like the mouse homologue, is constitutively expressed in testis, while human IRGM encodes a considerably truncated protein that is constitutively expressed in cultured cells including some macrophage cell lines. As the two human genes IRGC and IRGM are not subject to IFN control, it has been suggested that the host resistance mechanism supported by IRG proteins in the mouse is lacking in humans.

Supplier: Rockland Immunochemical

Autophagy, the process of bulk degradation of cellular proteins through an autophagosomic-lysosomal pathway is important for normal growth control and may be defective in tumor cells. It is involved in the preservation of cellular nutrients under starvation conditions as well as the normal turnover of cytosolic components. This process is negatively regulated by TOR (Target of rapamycin) through phosphorylation of autophagy protein APG1. ATG16, another member of the autophagy protein family, forms a complex with the ATG5-ATG12 conjugate. This multimeric protein has been shown to be essential for autophagosome formation in both yeast and mammals and targets the ATG5-ATG12 complex to the autophagic isolation membrane during the formation of the autophagosome. Because mammalian ATG16 has seven WD-repeats in its C-terminal domain, it has been suggested that these may form a platform for further protein-protein interactions. Multiple isoforms of ATG16 are known to exist.

Supplier: Rockland Immunochemical

GbetaL (G protein beta protein subunit-like) is a member of a signaling pathway that regulates mammalian cell growth in response to the presence of nutrients and growth factors. It binds to the kinase domain of TOR (Target of rapamycin, also known as mTOR), an evolutionarily conserved serine/threonine kinase that regulates cell growth and cell cycle through its ability to integrate signals from nutrient levels and growth factors. Rapamycin inhibits TOR resulting in reduced cell growth and reduced rates of cell cycle and cell proliferation. TOR is normally associated with GbetaL and an additional regulatory protein RAPTOR, allowing TOR to control protein biosynthesis. The binding of GbetaL to TOR stimulates TOR's kinase activity towards downstream proteins such as RPS6K (ribosomal protein S6 kinase) and the translation factor 4E-BP1 which leads to increased protein translation and cell growth.

Supplier: Prosci

IL-16 Antibody: IL-16 was initially identified as a chemotactic cytokine, but is now known to possess a wide range of activities. Later studies have more fully characterized IL-16 as an immunomodulatory cytokine that contributes to the regulatory process of CD4+ T cell recruitment and activation at sites of inflammation in association with asthma and several autoimmune diseases. The precursor of IL-16 (pro-IL-16) is thought to be cleaved towards the C-terminal region by Caspase-3, releasing a 20 kDa active form that binds to and signals through CD4. Besides acting as a chemotactic cytokine, IL-16 is thought to also be involved in the regulation of T cell proliferation and multiple infectious, immune-mediated, and autoimmune inflammatory disorders including irritable bowel syndrome, systemic lupus erythematosus, and neurodegenerative disorders. At least two isoforms of IL-16 are known to exist; the longer isoform (also known as NIL-16) is detected only in neurons of the cerebellum and hippocampus.

Supplier: Prosci

Dact3 Antibody: The Wnt signaling cascade is a conserved process in multicellular animals that plays important roles during development and can contribute to cancer and other diseases. Many members of this pathway are also expressed in the postnatal tissues such as brain. One such protein is Dact3, a member of the Dact protein family that was initially identified through binding to Disheveled (Dvl), a cytoplasmic protein essential to Wnt signaling. Dact3 is expressed in the ventral region of maturing somites, limb bud and branchial arch mesenchyme, embryonic CNS, and the adult brain. Recent evidence shows that Dact3 acts as a negative regulator Wnt/beta-catenin signaling that is repressed at the transcriptional level in colorectal cancer and this repression is associated with bivalent histone modifications. This repression can be reversed by pharmacological agents that targets both histone methylation and deacetylation, suggesting that Dact3 may be a potential target for therapeutic treatment of this cancer. At least three isoforms of Dact3 are known to exist.

Supplier: Prosci

Stk39 Antibody: The serine/threonine kinase Stk39 belongs to the STE20 family, a group of kinases that are known to interact with inflammation-related kinases (such as p38, JNK, NKCC1, PKC-theta, WNK and MLCK), and with transcription factor AP-1. The STE 20 family is involved in diverse biological phenomena, including cell differentiation, cell transformation/ proliferation, cytoskeleton rearrangement, and the regulation of ion transporters. STK39 contains an N-terminal series of proline and alanine repeats (PAPA box), followed by a serine/threonine kinase catalytic domain and is abundantly expressed in the brain. STK39 is activated in response to hypotonic stress, leading to phosphorylation of several cation-chloride-coupled co-transporters. The catalytically active kinase specifically activates the p38 MAP kinase pathway, and its interaction with p38 decreases upon cellular stress, suggesting that this kinase may serve as an intermediate in the response to cellular stress. Recent studies show that STK39 tend to be a novel candidate gene for autism and hypertension.

Supplier: Prosci

Bora Antibody: Bora (Protein aurora borealis) is a key activator of Aurora Related Protein Kinase A (ARK-1), which is a centrosome-associated serine/threonine kinase that regulates centrosome maturation, bipolar spindle assembly and chromosome segregation during mitosis. Bora is localized to the nucleus until mitosis is initiated, then translocates to the cytoplasm in a Cdc2 dependent manner. Activation of Cdc2 initiates the release of Bora into the cytoplasm where it can bind and activate ARK-1. PLK1 (polo-like kinase-1) interacts with Bora to control the accessibility of its activation loop for phosphorylation and activation by ARK-1. Bora and ARK-1 cooperatively activate PLK1 and control mitotic entry. Bora mutants result in multipolar spindles in mitosis identical to those observed when ARK-1 function is blocked. Thus, the ARK1-Bora-PLK1 regulatory circuit in mammalian cells elucidates a key mechanism in cell cycle regulation. At least three isoforms of Bora are known to exist.

Supplier: Prosci

Avian Influenza Hemagglutinin 4 Antibody: Influenza A virus is a major public health threat, killing more than 30, 000 people per year in the USA. Novel influenza virus strains caused by genetic drift and viral recombination emerge periodically to which humans have little or no immunity, resulting in devastating pandemics. Influenza A can exist in a variety of animals; however it is in birds that all subtypes can be found. These subtypes are classified based on the combination of the virus coat glycoproteins hemagglutinin (HA) and neuraminidase (NA) subtypes. During 1997, an H5N1 avian influenza virus was determined to be the cause of death in 6 of 18 infected patients in Hong Kong. There was some evidence of human to human spread of this virus, but it is thought that the transmission efficiency was fairly low. HA interacts with cell surface proteins containing oligosaccharides with terminal sialyl residues. Virus isolated from a human infected with the H5N1 strain in 1997 could bind to oligosaccharides from human as well as avian sources, indicating its species-jumping ability.

Supplier: Prosci

JPH2 Antibody: Junctional complexes between the plasma membrane (PM) and endoplasmic/sarcoplasmic reticulum (ER/SR) are a common feature of all excitable cell types and mediate cross talk between cell surface and intracellular ion channels. Junctophilins (JPs) are important components of the junctional complexes. JPs are composed of a carboxy-terminal hydrophobic segment spanning the ER/SR membrane and a remaining cytoplasmic domain that shows specific affinity for the PM. Four JPs have been identified as tissue-specific subtypes derived from different genes: JPH1 is expressed in skeletal muscle, JPH2 is detected throughout all muscle cell types, and JPH3 and JPH4 are predominantly expressed in the brain and contribute to the subsurface cistern formation in neurons. JPH2-null mice died of embryonic cardiac arrest and human patients with mutations in the JPH2 gene showed hypertrophic cardiomyopathy, demonstrating the importance of this protein. Multiple isoforms of JPH2 are known to exist.

Supplier: Prosci

Adiponectin Antibody: Adipose tissue of an organism plays a major role in regulating physiologic and pathologic processes such as metabolism and immunity by producing and secreting a variety of bioactive molecules termed adipokines. One highly conserved family of adipokines is adiponectin/ACRP30 and its structural and functional paralogs, the C1q/tumor necrosis factor-alpha-related proteins (CTRPs) 1-7. Unlike the CTRPs, which are expressed in a wide variety of tissues, adiponectin is reported to be expressed exclusively by differentiated adipocytes. These proteins are thought to act mainly on liver and muscle tissue to control glucose and lipid metabolism. An analysis of the crystal structure of adiponectin revealed a structural and evolutionary link between TNF and C1q-containing proteins, suggesting that these proteins arose from a common ancestral innate immunity gene. It is present in high levels in normal human plasma, but is reduced in obese subjects and often in those with increased insulin resistance and type 2 diabetes, suggesting that adiponectin may be a useful pharmacological target in various metabolic diseases.

Supplier: Prosci

Bit1 Antibody: Adhesion to extracellular matrix regulates cell survival through both integrin engagement and appropriate cell spreading. Anoikis is the molecular mechanism of apoptosis induced by integrin detachment. Bit1 (Bcl-2 inhibitor of transcription 1) was recently identified as being involved in this process. Bit1 is a mitochondrial protein that is released into the cytoplasm upon onset of apoptosis where it forms a complex with AES, a small Groucho/transducin-like enhancer of split (TLE) protein and induces caspase-independent apoptosis. Both AES and TLE proteins are transcriptional co-repressors that play important roles in neurogenesis, segmentation, and sex determination. It has been suggested that Bit1-AES complexes turn off a survival-promoting gene transcription program controlled by TLE. Interestingly, apoptosis of cells transfected with Bit1 and AES could be inhibited if the cells were allowed to attach to fibronectin through the alpha5beta1 integrin suggesting that the Bit1-AES pathway contributing to anoikis is regulated by integrins, and in particular, the alpha5beta1 integrin.

Supplier: Biotium

TIMP3 (tissue inhibitor of metalloproteinases 3), along with family members TIMP1, TIMP2, and TIMP4, are inhibitors of the matrix metalloproteinases (MMPs), a group of peptidases involved in degradation of the extracellular matrix (ECM). An imbalance between MMPs and the associated TIMPs may play a significant role in the invasive phenotype of malignant tumors. TIMP s inhibit the proteolytic invasiveness of tumor cells and normal placental trophoblast cells. TIMP-3 may be involved in regulating trophoblastic invasion of the uterus as well as in regulating remodeling of the extracellular matrix during the folding of epithelia, and in the formation, branching and expansion of epithelial tubes.

CF® dyes are Biotium's next-generation fluorescent dyes. CF®488A is a green fluorescent dye (Ex/Em 490/515 nm) with excellent brightness and photostability. The dye is minimally charged for less non-specific binding. CF®488A also is compatible with super-resolution imaging by TIRF.

Supplier: Rockland Immunochemical

Interferons (IFNs) are involved in a multitude of immune interactions during viral infections and play a major role in both the induction and regulation of innate and adaptive antiviral mechanisms. During infection, host-virus interactions signal downstream molecules such as transcription factors such as IFN regulatory factor-3 (IRF3) which can act to stimulate transcription of IFN-alpha/beta genes. IRF7 has been shown to play a role in the transcriptional activation of virus-inducible cellular genes, including interferon beta chain genes. IRF7 play a major role in the innate immune pathway, interacting with the Toll-like receptor (TLR) adaptor proteins MyD88 and Tirp/TRAM and functioning as an intermediate TLR4 and TLR9 signaling. There are at least four differentially spliced isoforms of IRF7, although their function has not been clearly established.

Supplier: Rockland Immunochemical

SIGIRR is a member of the Toll-like receptor-interleukin 1 receptor superfamily. Members of this family are defined by the presence of an intracellular Toll-IL-1R (TIR) domain. The Toll-like receptors (TLRs) are signaling molecules that recognize different microbial products during infection and serve as an important link between the innate and adaptive immune responses. SIGIRR was originally identified through database analysis and was shown to have only one Ig domain as opposed to the normal three Ig folds seen in the TIR family. Similar to ST2, another TIR family member, it has been shown to negatively regulate IL-1 receptor and Toll-like receptor signaling. However, SIGIRR inhibits TLR-IL-1R signaling by dimerizing with TLR4, TLR5, TLR9, and IL-1R. It also associates with the down-stream TLR signaling proteins IRAK and TRAF6 in an IL-1-dependent fashion.

Supplier: Rockland Immunochemical

Apoptosis is mediated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and a caspase family of proteases. DD-containing serine/threonine kinase RIP regulates Fas-induced apoptosis. A novel CARD-containing serine/threonine kinase was recently identified and designated RICK/RIP2/CARDIAK for RIP-like interacting CLARP kinase, receptor interacting protein-2, and CARD-containing ICE associated kinase, respectively. RICK contains an N-terminal kinase catalytic domain and a C-terminal CARD domain. Overexpression of RICK induced apoptosis and activation of NF-kB and JNK. RICK interacts with members of the TRAF family, CLARP and caspase-1. Thus, RICK represents a novel kinase that regulates TNF and Fas induced-apoptosis and that is involved in the generation of proinflammatory cytokine IL-1b. The messenger RNA of RICK is expressed in multiple human tissues.

Supplier: Rockland Immunochemical

Two distinct signaling pathways activate the host innate immunity against viral infection. One pathway is reliant on members of the Toll-like receptor (TLR) family while the other uses the RNA helicase RIG-I as a receptor for intracellular viral double-stranded RNA as a trigger for the immune response. VISA is a mitochondrial membrane protein that was identified as a critical component in the IFN-b signaling pathways that recruits IRF-3 to RIG-I, leading to its activation and that of NF-kB. VISA is also thought to interact with other components of the innate immune pathway such as the TLR adapter protein TRIF, TRAF2 and TRAF6. VISA also interacts with the IKKa, IKKb and IKKe kinases through its C-terminal region. Cleavage of this region by the Hepatitis C virus (HCV) protease allows HCV to escape the host immune system. At least three isoforms of VISA are known to exist.

Supplier: Rockland Immunochemical

TMP21 is a ubiquitously expressed protein that is involved in vesicular targeting and protein transport. More recent experiments have shown that it is also a component in the presenilin complex and modulates the gamma-secretase but not the epsilon-secretase cleavage activity of the amyloid precursor protein. The presenilin complex is composed of the proteins APH1, nicastrin, and PEN2 in addition to presenilin-1. Together, these proteins cleave the amyloid precursor protein at what is known as the gamma- and epsilon-sites and can lead to the accumulation of the Abeta cleavage product that is associated with Alzheimer's disease. Co-immunoprecipitation experiments using antibodies against these proteins also yielded TMP21 indicating that TMP21 may play a role in the regulation of this complex. Suppression of TMP21 expression by siRNA in transfected cells caused increased gamma-secretase activity but not epsilon-secretase activity, and increased Abeta; production, demonstrating that TMP21 can modulate gamma-secretase activity.

Supplier: MP Biomedicals

DL-Dithiothreitol is also known as Clelands reagent; Protective agent for sulfhydryl groups (-SH). Quantitatively reduces disulfides (-S-S- to -SH). In this reaction the DTT is oxidized to the cyclic disulfide which ensures the reduction of other disulfides in solution. Disulfide reduction occurs quickly at pH 8.

DTT has been used:

Supplier: Rockland Immunochemical

Apoptosis, also known as programmed cell death, plays major roles in development and normal tissue turnover in addition to tumor formation. Apoptosis is regulated by death domain (DD) and/or caspase recruitment domain (CARD) containing molecules and the caspase family of proteases. CARD domain containing cell death regulators include RAIDD, Apaf-1, caspase-9, and caspase-2. A novel CARD domain containing protein was recently identified and designated ARC for apoptosis repressor with CARD. An alternate splicing isoform of ARC was identified as Nop30. While ARC interacts with caspase-2 and -8 and suppresses apoptosis induced by cell death adapters FADD and TRADD and by cell death receptors Fas, TNFR-1 and DR3, Nop30 multimerizes and binds to the splicing factor SRp30c and may act to influence alternative splice site selection in vivo. The Nop30 antibody will not detect ARC protein.

Supplier: Rockland Immunochemical

NogoA is a member of a family of integral membrane proteins termed reticulons that are thought to be involved in numerous disorders including neurodegenerative diseases. Reticulon proteins are known to regulate many cellular processes and interact with multiple proteins and receptors such as BACE. NogoA was initially identified as a myelin-associated neurite outgrowth inhibitor. It is highly expressed in oligodendrocytes in the white matter of the CNS; blocking its activity with antibodies or other factors results in improved axon regrowth and functional recovery in experimental CNS lesion models. NogoA has also been suggested to play a role in neurodegenerative diseases such as Amyotrophic lateral sclerosis, in which case NogoA is found at elevated levels in postmortem muscular samples, and multiple sclerosis (MS), in which case autoantibodies to NogoA have been found in serum and cerebrospinal fluid in MS patients.