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Product listing: RPL11 (D1P5N) Rabbit mAb, UniProt ID P62913 #18163 to HUS1 (D4J9H) Rabbit mAb, UniProt ID O60921 #16416

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Ribosomal protein L11 (RPL11) is a nucleolar protein and component of the 60S ribosomal subunit. Research studies have shown that RPL11 plays a critical role in eukaryotic ribosome biogenesis (1). It has also been suggested that extraribosomal RPL11 functions in an RP-MDM2-p53 network in which RPL11 acts as a sensor of nucleolar stresses that perturb ribosome biogenesis (2). Indeed, RPL11 contributes to enhanced p53 stability and transcriptional activity in response to nucleolar stress and impaired ribosome biogenesis by binding and inhibiting the ubiquitin ligase activity of MDM2 (2-9). In addition to regulating p53 activity, research studies have also shown that RPL11 can inhibit cell cycle progression and ribosome biogenesis in response to nucleolar stress through repression of c-Myc transcriptional activity as well as its mRNA translation (10-12). Mutations in the RPL11 gene have been found in patients with Diamond-Blackfan anemia (13).

$489
96 assays
1 Kit
The PathScan® Total Bmi1 Sandwich ELISA Kit is a solid phase sandwich enzyme-linked immunosorbent assay (ELISA) that detects endogenous levels of Bmi1 protein. A Bmi1 mouse mAb has been coated onto the microwells. After incubation with cell lysates, the Bmi1 proteins are captured by the coated antibody. Following extensive washing, a Bmi1 rabbit detection mAb is added to detect captured Bmi1 proteins. Anti-rabbit, HRP-linked antibody is then used to recognize the bound detection antibody. HRP substrate, TMB, is added to develop color. The magnitude of absorbance for the developed color is proportional to the quantity of Bmi1 protein.Antibodies in the kit are custom formulations specific to the kit.
REACTIVITY
Human, Monkey, Mouse

Background: The polycomb group (PcG) of proteins contributes to the maintenance of cell identity, stem cell self-renewal, cell cycle regulation, and oncogenesis by maintaining the silenced state of genes that promote cell lineage specification, cell death, and cell-cycle arrest (1-4). PcG proteins exist in two complexes that cooperate to maintain long-term gene silencing through epigenetic chromatin modifications. The first complex, EED-EZH2, is recruited to genes by DNA-binding transcription factors and methylates histone H3 on Lys27. This histone methyl-transferase activity requires the Ezh2, Eed, and Suz12 subunits of the complex (5). Histone H3 methylation at Lys27 facilitates the recruitment of the second complex, PRC1, which ubiquitinylates histone H2A on Lys119 (6). Bmi1 is a component of the PRC1 complex, which together with Ring1 strongly enhances the E3 ubiquitin ligase activity of the Ring2 catalytic subunit (7). Bmi1 plays an important role in the regulation of cell proliferation and senescence through repression of the p16 INK4A and p19 ARF genes and is required for maintenance of adult hematopoietic and neural stem cells (3,4,8-10).

The Mutant Ras Antibody Sampler Kit provides an economical means of detecting common mutation in the Ras protein. The kit contains enough primary and secondary antibodies to perform at least two western blot experiments.

Background: The 21 kDa guanine-nucleotide binding proteins (K-Ras, H-Ras, and N-Ras) cycle between active (GTP-bound) and inactive (GDP-bound) forms (1). Receptor tyrosine kinases and G protein-coupled receptors activate Ras, which then stimulates the Raf-MEK-MAPK pathway (2-4). GTPase-activating proteins (GAP) normally facilitate the inactivation of Ras. However, research studies have shown that in 30% of human tumors, point mutations in Ras prevent the GAP-mediated inhibition of this pathway (5). The most common oncogenic Ras mutation found in tumors is Gly12 to Asp12 (G12D), which prevents Ras inactivation, possibly by increasing the overall rigidity of the protein (5,6). Additional oncogenic mutations of Ras have been observed at varying frequencies at codons 12, 13, and 61. The Gly12 to Val12 (G12V) mutation has been detected in a number of different cancers, including colorectal and thyroid cancer (7,8).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometric analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated EOMES (D8D1R) Rabbit mAb #81493.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: The T-box family of transcription factors is named for their shared homology with the DNA binding domain of the mouse brachyury (T) gene product. Members of this family bind DNA and are capable of transcriptional activation. They also have evolutionarily conserved expression patterns and roles in embryonic development, primarily mesoderm development (1). EOMES, or Tbr2 (T-box brain 2), is a master regulator of mesoderm formation that is also essential for trophoblast formation, gastrulation, neurogenesis and the differentiation of certain T cell subsets. Embryos from EOMES knock-out mice die soon after implantation due to their inability to develop a trophoblast (2,3). Conditional neural knock out mice show defects in development of a specific population of neural progenators known as Intermediate Progenator Cells (IPCs) that give rise only to neurons (4,5). These cells are formed from the radial glia in the ventricular and sub-ventricular zones of the cortex. Expression of EOMES increases as cells develop from radial glia to IPCs and then decreases as IPCs progress to neurons. Recent evidence suggests that EOMES and IPCs may also play a role neurogenesis in the adult hippocampal SGZ (5). EOMES is also a key transcription factor for memory T cells and for full effector differentiation of CD8+ T cells (6). Expression of EOMES is induced in CD8+ T cells following viral infection and bacterial infection where sufficient IL-12 has been produced to elicit acute host cell response (7).

PTMScan® Technology employs a proprietary methodology from Cell Signaling Technology (CST) for peptide enrichment by immunoprecipitation using a specific bead-conjugated antibody in conjunction with liquid chromatography (LC) tandem mass spectrometry (MS/MS) for quantitative profiling of post-translational modification (PTM) sites in cellular proteins. These include phosphorylation (PhosphoScan®), ubiquitination (UbiScan®), acetylation (AcetylScan®), and methylation (MethylScan®), among others. PTMScan® Technology enables researchers to isolate, identify, and quantitate large numbers of post-translationally modified cellular peptides with a high degree of specificity and sensitivity, providing a global overview of PTMs in cell and tissue samples without preconceived biases about where these modified sites occur. For more information on PTMScan® Proteomics Services, please visit www.cellsignal.com/services/index.html.

Background: Lysine is subject to a wide array of regulatory post-translational modifications due to its positively charged ε-amino group side chain. The most prevalent of these are ubiquitination and acetylation, which are highly conserved among prokaryotes and eukaryotes (1,2). Acyl group transfer from the metabolic intermediates acetyl-, succinyl-, malonyl-, glutaryl-, butyryl-, propionyl-, and crotonyl-CoA all neutralize lysine’s positive charge and confer structural alterations affecting substrate protein function. Lysine acetylation is catalyzed by histone acetyltransferases, HATs, using acetyl-CoA as a cofactor (3,4). Deacylation is mediated by histone deacetylases, HDACs 1-11, and NAD-dependent Sirtuins 1-7. Some sirtuins have little to no deacetylase activity, suggesting that they are better suited for other acyl lysine substrates (5).

$129
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Calponin 1 is a member of the Calponin family, which consists of Calponins 1, 2, and 3. Calponin 1 is exquisitely expressed in smooth muscle cells of various tissues, where it interacts with filamentous F-actin to regulate smooth muscle contraction (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Complexins are small soluble proteins composed of a central α-helical-structured domain surrounded by amino- and carboxy-terminal unstructured domains (1). These cytosolic proteins bind to t-SNAREs with low affinity and to assembled SNARE complexes with high affinity (1,2). Two isoforms, complexin-1 and complexin-2, are expressed in neuronal cells (3) where they regulate evoked and spontaneous exocytosis (4,5). Altered complexin expression resulting from RNAi-mediated knockdown (6) or gene invalidation (7) leads to alteration in spontaneous fusion events and neurotransmitter release, which reflects functions at both inhibitory and stimulatory synapses.

$121
2 western blots
20 µl
$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to Alexa Fluor® 488 fluorescent dye and tested in-house for direct immunofluorescence analysis in mouse cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated ASC (D2W8U) Rabbit mAb (Mouse Specific) #67824.
APPLICATIONS
REACTIVITY
Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Immunocytochemistry)

Background: TMS1 (target of methylation-induced silencing)/ASC (apoptosis-associated speck-like protein containing a CARD), also referred to as PYCARD and CARD5, is a 22-kDa pro-apoptotic protein containing an N-terminal pyrin domain (PYD) and a C-terminal caspase recruitment domain (CARD) (1-2). The ASC/TMS1 gene was originally found to be aberrantly methylated and silenced in breast cancer cells (2), and has since been found to be silenced in a number of other cancers, including ovarian cancer (3), glioblastoma (4), melanoma (5), gastric cancer (6), lung cancer (7), and prostate cancer (8). Expression of ASC/TMS1 can be induced by pro-apoptotic/inflammatory stimuli (9). During apoptosis ASC/TMS1 is re-distributed from the cytosol to the mitochondria and associates with mitochondrial Bax to trigger cytochrome c release and subsequent apoptosis (10). ASC/TMS1 has also been found to be a critical component of inflammatory signaling where it associates with and activates caspase-1 in response to pro-inflammatory signals (11).

$108
250 PCR reactions
500 µl
SimpleChIP® Mouse USP31 Promoter Primers contain a mix of forward and reverse PCR primers that are specific to a region of the mouse ubiquitin specific peptidase 31 (USP31) promoter. These primers can be used to amplify DNA that has been isolated using chromatin immunoprecipitation (ChIP). Primers have been optimized for use in SYBR® Green quantitative real-time PCR and have been tested in conjunction with SimpleChIP® Enzymatic Chromatin IP Kits #9002 and #9003 and ChIP-validated antibodies from Cell Signaling Technology®.
REACTIVITY
Mouse

Background: The chromatin immunoprecipitation (ChIP) assay is a powerful and versatile technique used for probing protein-DNA interactions within the natural chromatin context of the cell (1,2). This assay can be used to either identify multiple proteins associated with a specific region of the genome or to identify the many regions of the genome bound by a particular protein (3-6). ChIP can be used to determine the specific order of recruitment of various proteins to a gene promoter or to "measure" the relative amount of a particular histone modification across an entire gene locus (3,4). In addition to histone proteins, the ChIP assay can be used to analyze binding of transcription factors and co-factors, DNA replication factors, and DNA repair proteins. When performing the ChIP assay, cells are first fixed with formaldehyde, a reversible protein-DNA cross-linking agent that "preserves" the protein-DNA interactions occurring in the cell (1,2). Cells are lysed and chromatin is harvested and fragmented using either sonication or enzymatic digestion. Fragmented chromatin is then immunoprecipitated with antibodies specific to a particular protein or histone modification. Any DNA sequences that are associated with the protein or histone modification of interest will co-precipitate as part of the cross-linked chromatin complex and the relative amount of that DNA sequence will be enriched by the immunoselection process. After immunoprecipitation, the protein-DNA cross-links are reversed and the DNA is purified. Standard PCR or quantitative real-time PCR are often used to measure the amount of enrichment of a particular DNA sequence by a protein-specific immunoprecipitation (1,2). Alternatively, the ChIP assay can be combined with genomic tiling micro-array (ChIP on chip) techniques, high throughput sequencing (ChIP-Seq), or cloning strategies, all of which allow for genome-wide analysis of protein-DNA interactions and histone modifications (5-8). SimpleChIP® primers have been optimized for amplification of ChIP-isolated DNA using real-time quantitative PCR and provide important positive and negative controls that can be used to confirm a successful ChIP experiment.

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Nectin-4/Poliovirus Receptor-Like 4 (PVRL4) is a type-I transmembrane glycoprotein that belongs to the immunoglobulin superfamily and promotes cell-cell adhesion by serving as a major component of adherens junctions (1-3). The extracellular domain of Nectin-4, which contains an Ig variable-like domain (V) and two Ig constant-like domains (C), mediates binding to the measles virus (4) and to neighboring cells through trans heterophilic interactions with Nectin-1 (5,6). Unlike other nectin family members, which are widely expressed in adult tissues, Nectin-4 expression in humans is largely restricted to the placenta (7). Research studies have demostrated that Nectin-4 is overexpressed in a variety of human solid tumors of the pancreas (8), breast (9,10), lung (11), and ovary (12). Due to its restricted expression pattern in normal human tissues, Nectin-4 may serve as a novel diagnostic and therapeutic target for a variety of human tumors.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: The mammalian Mediator Complex is a multi-subunit protein complex that couples specific transcriptional regulators to RNA polymerase II (Pol II) and the basal transcription machinery. Interactions between distinct Mediator subunits and transcription factors allow for specific gene regulation (reviewed in 1).Mediator complex interactions control various biological processes, including insulin signaling (2), NF-κB-dependent signaling (3), stem cell pluripotency and self renewal (4,5), and proliferation of colon cancer cells (6,7).CDK8/Cyclin C, along with Med12 and Med13, constitute a subcomplex within the Mediator Complex thought to act as a molecular switch, inhibiting Pol II recruitment and transcription initiation (8,9). Expression of CDK8 abrogates E2F-1-dependent inhibition of β-catenin activity in colon cancer cells (9). High levels of CDK8 coincide with high β-catenin-dependent transcription in colon cancer cells, and their proliferation can be inhibited by suppressing CDK8 expression (8).CDK8 can phosphorylate Ser727 on STAT1, which reduces natural killer (NK) cell toxicity (10,11). As such, inhibitors are being pursued as potential therapeutics to enhance NK cell activity and combat a variety of cancer types (12,13).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CYP17A1, also known as cytochrome P450C17, is a steroidogenic enzyme belonging to the P450 cytochrome superfamily of monooxygenases (1, 2). In humans, CYP17A1 expression is abundantly expressed in the adrenal cortex, where it plays a central role in the androgen synthesis pathway (2). CYP17A1 is the primary target of abiraterone, a synthetic steroid used in the treatment of castration-resistant prostate cancer (CRPC) (3, 4). Abiraterone is converted to the more active form D4A, which antagonizes androgen receptor signaling by inhibiting CYP17A1 and other steroidogenic enzymes (3, 4). This suppresses the synthesis of 5α-dihydrotestosterone (DHT), which is a driver of castration-resistant prostate cancer cell growth (3, 4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: CD151 (PETA-3, SFA-1) is a member of the evolutionarily conserved tetraspanin family of multipass glycoproteins (TM4SF), highlighted by four transmembrane domains, two extracellular loops, and N/C-termini that reside within the cytoplasm. Identified as the first member of the tetraspanin family to be implicated in tumorigenesis, research studies have demonstrated that CD151 participates in tumor neovascularization (1), tumor cell cell invasion (2), and cell adhesion (3). Furthermore, a positive correlation exists between CD151 expression levels and poor prognosis for tumors of the lung (4), kidney (5), and prostate (6). CD151 is localized predominantly to the plasma membrane and research studies have demonstrated that CD151 exerts its pro-tumorigenic effects, in part, through the modulation of laminin-binding integrins (7-9) and oncogenic receptor tyrosine kinases, such as c-Met (10,11) and EGFR (12).

The Pro-Survival Bcl-2 Family Antibody Sampler Kit II provides an economical means to examine several members of the Bcl-2 family. The kit contains enough primary antibody to perform two western blot experiments.

Background: The Bcl-2 family consists of a number of evolutionarily conserved proteins containing Bcl-2 homology domains (BH) that regulate apoptosis through control of mitochondrial membrane permeability and release of cytochrome c (1-3). Four BH domains have been identified (BH1-4) that mediate protein interactions. The family can be separated into three groups based upon function and sequence homology: pro-survival members include Bcl-2, Bcl-xL, Mcl-1, A1 and Bcl-w; pro-apoptotic proteins include Bax, Bak and Bok; and "BH3 only" proteins Bad, Bik, Bid, Puma, Bim, Bmf, Noxa and Hrk. Interactions between death-promoting and death-suppressing Bcl-2 family members has led to a rheostat model in which the ratio of pro-apoptotic and anti-apoptotic proteins controls cell fate (4). Thus, pro-survival members exert their behavior by binding to and antagonizing death-promoting members. In general, the "BH3-only members" can bind to and antagonize the pro-survival proteins leading to increased apoptosis (5). While some redundancy of this system likely exists, tissue specificity, transcriptional and post-translational regulation of many of these family members can account for distinct physiological roles.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry, Immunofluorescence (Frozen), Immunofluorescence (Immunocytochemistry), Immunoprecipitation, Western Blotting

Background: Granzymes are a family of serine proteases expressed by cytotoxic T lymphocytes and natural killer (NK) cells and are key components of immune responses to pathogens and transformed cells (1). Granzymes are synthesized as zymogens and are processed into mature enzymes by cleavage of a leader sequence. They are released by exocytosis in lysosome-like granules containing perforin, a membrane pore-forming protein. Granzyme B has the strongest apoptotic activity of all the granzymes as a result of its caspase-like ability to cleave substrates at aspartic acid residues thereby activating procaspases directly and cleaving downstream caspase substrates (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The type 1 insulin-like growth factor receptor (IGF1R) is a transmembrane receptor tyrosine kinase that is widely expressed in many cell types in fetal and postnatal tissues, and which is highly similar in sequence and structure to the insulin receptor (1-4). IGF1R is synthesized as a preproprotein which is proteolytically cleaved into alpha and beta subunits. Receptor assembly involves heterodimerization of two alpha and two beta subunits to generate the heterotetrameric transmembrane receptor. The alpha subunits form the extracellular ligand binding domain; ligand binding by IGF-I or IGF-II initiates autophosphorylation of conserved intracellular residues in the beta subunit kinase domain, leading to kinase activation and subsequent activation of downstream signal transduction pathways (e.g., Akt and MAPK) (4-8). Enhanced mitogenic signaling through the IGF1R is frequently observed in cancer, making the IGF1R an important research target in translational oncology (9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: Receptor type protein tyrosine phosphatase F (PTPRF, LAR) is a transmembrane PTP that helps to regulate insulin signaling, cell proliferation and cell migration. The PTPRF protein is composed of an extracellular segment that contains several Ig-like and fibronectin (Fn-III) domains, a transmembrane region and a pair of cytoplasmic phosphatase domains (1,2). Functional studies reveal that the membrane-associated D1 phosphatase domain is responsible for substrate dephosphorylation, while the D2 domain is important for substrate specificity (3). PTPRF negatively regulates insulin signaling through dephosphorylation of insulin receptor and insulin receptor substrate (4). This phosphatase activates the pro-apoptotic DAPK serine/threonine kinase by removing a phosphate at Tyr491/492, while the kinase Src replaces the phosphate to inactivate DAPK at the same time it down regulates PTPRF expression (5). PTPRF is commonly found at focal adhesions where it interacts with liprin, which localizes the phosphatase to the membrane, and the Rac/Rho family GTPase Trio (6). Localization of PTPRF at adherens junctions results in PTPRF modification of β-catenin, which inhibits cell migration by limiting the amount of available cytosolic β-catenin (7).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells.
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry

Background: Members of the Myc/Max/Mad network function as transcriptional regulators with roles in various aspects of cell behavior including proliferation, differentiation and apoptosis (1). These proteins share a common basic-helix-loop-helix leucine zipper (bHLH-ZIP) motif required for dimerization and DNA-binding. Max was originally discovered based on its ability to associate with c-Myc and found to be required for the ability of Myc to bind DNA and activate transcription (2). Subsequently, Max has been viewed as a central component of the transcriptional network, forming homodimers as well as heterodimers with other members of the Myc and Mad families (1). The association between Max and either Myc or Mad can have opposing effects on transcriptional regulation and cell behavior (1). The Mad family consists of four related proteins; Mad1, Mad2 (Mxi1), Mad3 and Mad4, and the more distantly related members of the bHLH-ZIP family, Mnt and Mga. Like Myc, the Mad proteins are tightly regulated with short half-lives. In general, Mad family members interfere with Myc-mediated processes such as proliferation, transformation and prevention of apoptosis by inhibiting transcription (3,4).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: The coxsackie virus and adenovirus receptor (CXADR, CAR) is a highly conserved, single-transmembrane glycoprotein and the primary receptor to mediate cellular attachment and infection of coxsackie B viruses and most adenoviruses (1,2). The CAR protein contains a pair of Ig-like domains within the amino-terminal extracellular domain and a carboxyl-terminal PDZ motif (1). Research studies indicate that CAR is a tight junction protein that associates with the ZO-1 scaffold protein and promotes both cell adhesion and restriction of solute and ion movement between cells (2). Endogenous CAR is targeted to the basolateral plasma membrane by a tyrosine-based basolateral sorting signal and clathrin adaptors AP-1A and AP-1B (3). CAR binds junctional adhesion molecule L (JAML) on epithelial cells and neutrophils where it activates PI3K and downstream MAPK kinases to stimulate epithelial γδ T cell proliferation and increase production of TNFα and keratinocyte growth factor (4-6). As a result, the CAR protein plays a potentially critical role in adenoviral gene therapy, immunity, wound repair, inflammation, and cancer therapy (4-6). Additional studies demonstrate that CAR is essential in regulating squamous carcinoma cell growth (7).

$269
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Immunoprecipitation, Western Blotting

Background: Sine oculis homeobox (SIX) proteins belong to a family of evolutionarily conserved transcription factors discovered in Drosophila mutant screens for embryonic eye development genes (1-3). The prototypical family member (sine oculis, so) was named for eyeless embryos carrying mutations in a gene highly conserved among vertebrates, including humans (SIX1) (4). A total of six family members (SIX1-6) have been identified in vertebrates. Each SIX protein contains a homeobox nucleic acid recognition domain (HD) with a DNA-binding helix-turn-helix motif and an adjacent SIX domain, which may be involved in regulating protein-protein interactions (5). In addition to their critical functions during embryonic organogenesis, research studies suggest that SIX proteins play additional roles in postnatal cell cycle regulation, with potentially important implications in tumorigenesis (6,7).

$305
100 µl
This Cell Signaling Technology antibody is conjugated to biotin under optimal conditions. The biotinylated antibody is expected to exhibit the same species cross-reactivity as the unconjugated eIF4E (C46H6) Rabbit mAb #2067.
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Western Blotting

Background: Eukaryotic initiation factor 4E (eIF4E) binds to the mRNA cap structure to mediate the initiation of translation (1,2). eIF4E interacts with eIF4G, a scaffold protein that promotes assembly of eIF4E and eIF4A into the eIF4F complex (2). eIF4B is thought to assist the eIF4F complex in translation initiation. Upon activation by mitogenic and/or stress stimuli mediated by Erk and p38 MAPK, Mnk1 phosphorylates eIF4E at Ser209 in vivo (3,4). Two Erk and p38 MAPK phosphorylation sites in mouse Mnk1 (Thr197 and Thr202) are essential for Mnk1 kinase activity (3). The carboxy-terminal region of eIF4G also contains serum-stimulated phosphorylation sites, including Ser1108, Ser1148, and Ser1192 (5). Phosphorylation at these sites is blocked by the PI3 kinase inhibitor LY294002 and by the FRAP/mTOR inhibitor rapamycin.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunofluorescence (Frozen), Immunohistochemistry (Paraffin)

Background: Orexin, also called HCRT or hypocretin, is expressed as a precursor that is processed into two biologically active neuropeptides called orexin-A (HCRT1) and orexin-B (HCRT2) (1). Orexin is expressed in the lateral and posterior hypothalamus and plays a role in feeding behavior (1). The orexin neuropeptides act by stimulating the two orexin receptors that belong to the G Protein-Coupled Receptors family (1). Orexin receptor 1 is mostly found in the hypothalamic region, while orexin receptor 2 is also found in the cerebral cortex and the nucleus accumbent (2). Orexin also plays a role in adipocyte homeostasis and is required for brown adipose tissue development, differentiation, and function (3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: Transient receptor potential (TRP) canonical 6 (TRPC6) belongs to the superfamily of TRP cation channels. The TRPC subfamily (TRPC1-7) is a group of calcium-permeable cation channels that mediates the increase in intracellular [Ca2+] following activation by G-protein-coupled receptors or receptor tyrosine kinases (1). TRPC6 is directly activated by diacylglycerol (DAG) (2). Various tissues express TRPC6, including brain, lung, kidney, ovary and small intestine. TRPC6 exerts a variety of biological functions in various tissues. In brain, TRPC6 plays important roles in synaptic plasticity, spatial cognition (3) and protects neurons from ischemic excitotoxicity (4). In kidney, TRPC6 is expressed in mesangial cells and podocytes of renal glomeruli (5) and regulates glomerular filtration (6). Mutations in TRPC6 gene cause autosomal dominant focal segmental glomerulosclerosis (7). In smooth muscle cells, TRPC6 mediates Na+ influx followed by Ca2+ entry via Na+/Ca2+ -exchanger (NCX) reversal which leads to contraction (8, 9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TKS5 (SH3PXD2A, FISH) is a scaffold protein expressed on invadosomes of both normal and transformed cell lines. Research studies suggest that TKS5 is functionally required for both the formation and invasive behavior of invadosomes (1, 2). TKS5 has an N-terminal PX domain that mediates invadosome initiation and localization of MMP-rich vesicles to the invadosome (3). TKS5 also has five SH3 domains, which recruit ADAM family proteinases to the invadosome to degrade extracellular matrix. These SH3 domains interact with adaptor proteins to facilitate F-actin polymerization during invadosome formation (4-6). Src tyrosine kinase has been shown to phosphorylate TKS5 at Tyr557 and Tyr619, which was shown to be necessary and sufficient for TKS5-mediated invadopia formation and invasion (7). Elevated TKS5 expression is positively associated with invasive behavior of cancer cells, suggesting TKS5 may have prognostic potential in cancer (8, 9).

$305
50 tests
100 µl
This Cell Signaling Technology antibody is conjugated to phycoerythrin (PE) and tested in-house for direct flow cytometry analysis in human cells. This antibody is expected to exhibit the same species cross-reactivity as the unconjugated ERG (A7L1G) Rabbit mAb #97249.
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Flow Cytometry

Background: ETS-related gene (ERG) is a member of the E-26 transformation-specific (ETS) family of sequence-specific DNA-binding transcription factors (1). ERG plays important and highly conserved roles in vertebrate development. Early in embryonic development, ERG is highly expressed in the embryonic mesoderm and endothelium, where it plays a critical role in the formation of the vascular system, urogenital tract and bone development (2,3). Later in embryonic development, ERG functions to regulate the pluripotency of hematopoietic stem cells, endothelial cell homeostasis and angiogenesis (2,4-7). ERG expression is not restricted to development. In adult mouse, ERG is normally expressed in endothelial tissues, including adrenal, cartilage, heart, spleen, lymphatic endothelial and eosinophil cells (8). However, deregulation of ERG activity, often resulting from chromosomal rearrangements, has been implicated and linked to poor prognosis in a number of different cancers. Chromosomal translocations generating EWS/ERG chimeric proteins comprised of the amino-terminal transactivation domain of Ewing’s sarcoma breakpoint region 1 (EWS) and the carboxy-terminal ETS domain of ERG have been identified in 5-10% of Ewing’s sarcoma, an aggressive bone and soft tissue tumor (9). Chromosomal translocations between ERG and TLS/FUS or ERG and ELF4 have been implicated in acute myeloid leukemia (10, 11). Over-expression of ERG, resulting from gene fusion with the androgen-driven promoter of the TMPRSS2 gene, has been identified as a key driver of metastasis and marker for poor prognosis in prostate cancer (12).

$303
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunofluorescence (Immunocytochemistry), Immunohistochemistry (Paraffin), Western Blotting

Background: Mucins represent a family of glycoproteins characterized by repeat domains and dense O-glycosylation (1). MUC1 (or mucin 1) is aberrantly overexpressed in most human carcinomas. Increased expression of MUC1 in carcinomas reduces cell-cell and cell-ECM interactions. MUC1 is cleaved proteolytically, and the large ectodomain can remain associated with the small 25 kDa carboxy-terminal domain that contains a transmembrane segment and a 72-residue cytoplasmic tail (1). MUC1 interacts with ErbB family receptors and potentiates ERK1/2 activation (2). MUC1 also interacts with β-catenin, which is regulated by GSK-3β, PKCγ, and Src through phosphorylation at Ser44, Thr41, and Tyr46 of the MUC1 cytoplasmic tail (3-5). Overexpression of MUC1 potentiates transformation (6) and attenuates stress-induced apoptosis through the Akt or p53 pathways (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: ROR1 and ROR2 are orphan receptor tyrosine kinases that are most closely related to MuSK and the Trk family of neurotrophin receptors. They are characterized by the presence of extracellular frizzled-like cysteine-rich domains and membrane-proximal kringle domains, both of which are assumed to mediate protein-protein interactions (1-3). The ROR family RTKs are evolutionarily conserved among Caenorhabditis elegans, Drosophila, mice, and humans (1,4). Although the functions of ROR kinases are unknown, similarities between ROR and MuSK and Trk kinases have led to speculation that ROR kinases regulate synaptic development. CAM-1, a C. elegans ortholog of the ROR family RTKs, plays several important roles in regulating cellular migration, polarity of asymmetric cell divisions, and axonal outgrowth of neurons during nematode development (4). mROR1 and mROR2 may play differential roles during the development of the nervous system (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: DNA damage resulting from genotoxic stress activates cellular checkpoints that prevent or delay cell division until damaged DNA is repaired or the cell follows an apoptotic pathway. The Rad9 homolog A (Rad9A, Rad9) protein is part of a checkpoint protein complex that acts as an early sensor of DNA damage. Together with the HUS1 and Rad1 checkpoint proteins, Rad9 forms a heterotrimeric 9-1-1 complex with a ring structure similar to the processivity factor PCNA. The 9-1-1 complex induces multiple signaling pathways, including the ATM- and ATR-activated DNA repair pathways (1,2). A functional 9-1-1 complex is required for ATR-dependent S phase checkpoint signaling (3).The 9-1-1 complex interacts with DNA topoisomerase 2-binding protein 1 (TopBP1) in response to DNA damage, activating ATR and causing signal amplification through further recruitment of TopBP1 (4). The 9-1-1 complex interacts with DNA mismatch repair proteins MSH2, MSH3, and MSH6 to play a role in mismatch repair (5). During an error-free DNA damage tolerance process, the 9-1-1 complex cooperates with polyubiquitinated PCNA and Exo1 nuclease to support switching of the replicative polymerase to the undamaged template (6).