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Product listing: ETO Antibody, UniProt ID Q06455 #4498 to COBRA1 (D6K9A) Rabbit mAb, UniProt ID Q8WX92 #14894

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

Application Methods: Western Blotting

Background: ETO belongs to a family of evolutionarily conserved nuclear factors. Although it has no DNA binding domains it is reported to act as a transcriptional corepressor (1). It is best characterized as the fusion partner of AML1 in acute myeloid leukemia with the t(8;21) translocation which gives rise to the AML-ETO fusion protein (2). AML1 is a transcription factor that is involved in the differentiation of all hematopoietic lineages. The fusion protein lacks the activation domain of AML1 and behaves as a dominant negative AML1, repressing AML1 target genes. AML-ETO also causes activation of other genes through a mechanism that involves Bcl-2 and enhanced expression of p21 waf1/cip1 (3,4). The AML-ETO fusion protein is thought to cause the expansion of a hematopoietic stem cell population that has limited lineage commitment and genomic instability (5). Recent evidence derived from chromatin immunoprecipitation (ChIP) experiments has demonstrated that ETO may play a role in the regulation of Notch target genes, and AML-ETO has been shown to disrupt repression of Notch target genes (6). Therefore, both AML and Notch target genes are deregulated by AML-ETO. Epigenetic silencing of the microRNA-223 gene has also been attributed to activities of AML-ETO, contributing to the differentiation block in t(8;21) leukemia (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Angiotensinogen (AGT) is the primary precursor of angiotensins, peptide hormones that play a central role in the renin-angiotensin system (RAS) (1-3). AGT is a secreted protein synthesized primarily by the liver and secreted into circulation. Upon binding to renin, the amino terminal fragment of AGT is cleaved and released as a decapeptide hormone termed angiotensin 1 (Ang I). Ang I is subsequently processed by angiotensin converting enzyme (ACE) to generate angiotensin II (Ang II), which acts on AT1 and AT2 receptors in the central nervous system to increase production of anti-diuretic hormone (ADH), while promoting vasoconstriction in the peripheral circulation (4). Aberrant upregulation of Ang II has been associated with numerous clinical conditions, including hypertension, atherosclerosis, myocardial hypertrophy, and obesity (5-7). Alternative cleavage products of Ang I (e.g., Ang 1-7) can also be generated by ACE2 cleavage, some of which display biological functions that are distinct from Ang II (8). Treatments that target the RAS (e.g., ACE inhibitors) are consequently of significant importance in the treatment of hypertensive and hypertensive-related disorders(5-8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunohistochemistry (Paraffin), Western Blotting

Background: Complement Regulatory Protein; Membrane Cofactor Protein (CD46) is a type 1 membrane protein that plays an important inhibitory role in the complement system (1). CD46 exhibits a cofactor activity that promotes inactivation of C3b and C4b by serum factor 1, thereby protecting host (self) cells from complement-dependent cytotoxicity (1,2). The importance of CD46 to complement regulation is underscored by the observation that genetic loss of CD46 leads to development of atypical hemolytic-uremic syndrome (aHUS), a disease characterized by uncontrolled complement activation (2,3). In addition to its role in complement inactivation, CD46 can function as a receptor for selected bacteria and viruses (4), and is reportedly required for proper fusion of spermatozoa to the oocyte membrane during fertilization (5). CD46 is implicated in the development and/or progression of selected cancer types. For example, research studies show elevated CD46 expression in medulloblastoma tumor samples (6), while CD46 expression has been linked with poor prognosis in breast cancer (7). It has been suggested that upregulation of CD46 may serve to protect cancer cells from complement-dependent cytotoxicity, thereby evading destruction by the immune system (8,9).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: CTP:phosphocholine cytidylyltransferase (CCT) is a critical enzyme that regulates the CDP-choline pathway for the biosynthesis of phosphatidylcholine. Three distinct CCT isoforms are found in mammals, including CCTα, CCTβ2, and CCTβ3 (1,2). CCTα is the major isoform that is expressed in most tissues (3). CCTα is essential in the synthesis and secretion of surfactant by alveolar epithelial cells and is important in maintaining the phosphatidylcholine level that regulates lipoprotein assembly and secretion in hepatocytes (4,5). CCTα is a major component in membrane biogenesis during cytokine secretion by stimulated macrophages (6). Monoubiquitination of CCTα prevents it from entering the nucleus and leads to its degradation by lysosome (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: TNIK (Traf2 and Nck-Interacting Kinase) is a member of the germinal center kinase (GCK) family (1). TNIK phosphorylates TCF4 and is an essential activator for Wnt signaling (2). Animal knockout model and kinase inhibition studies have reported that TNIK can stimulate both cancer cell growth and epithelial-mesenchymal transition (EMT) (3-5). TNIK has also been shown to promote F-actin disruption through its interactions with Rap2 (6). In neuronal cells, TNIK is enriched in the postsynaptic density (PSD), where it is reported to modulate neuronal receptor surface expression, dendrite complexity and signaling (7-9).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: Mer tyrosine kinase belongs to a receptor tyrosine kinase family with Axl and Tyro3. This family is characterized by a common NCAM (neural adhesion molecule)-related extracellular domain and a common ligand, GAS6 (growth arrest-specific protein 6). Mer protein has an apparent molecular weight of 170-210 kDa due to different glycosylation patterns generated in different cell types. Mer can be activated by dimerization and autophosphorylation through ligand binding or homophilic cell-cell interaction mediated by its NCAM-like motif (1). The downstream signaling components of activated Mer include PI3 kinase, PLCγ, and MAP kinase (2). Family members are prone to transcriptional regulation and carry out diverse functions including the regulation of cell adhesion, migration, phagocytosis, and survival (3). Mer regulates macrophage activation, promotes apoptotic cell engulfment, and supports platelet aggregation and clot stability in vivo (4). Investigators have found that overexpression of Mer may play a cooperative role in leukemogenesis and may be an effective target for biologically based leukemia/lymphoma therapy (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: Platelet derived growth factor (PDGF) family proteins exist as several disulphide-bonded, dimeric isoforms (PDGF AA, PDGF AB, PDGF BB, PDGF CC, and PDGF DD) that bind in a specific pattern to two closely related receptor tyrosine kinases, PDGF receptor α (PDGFRα) and PDGF receptor β (PDGFRβ). PDGFRα and PDGFRβ share 75% to 85% sequence homology between their two intracellular kinase domains, while the kinase insert and carboxy-terminal tail regions display a lower level (27% to 28%) of homology (1). PDGFRα homodimers bind all PDGF isoforms except those containing PDGF D. PDGFRβ homodimers bind PDGF BB and DD isoforms, as well as the PDGF AB heterodimer. The heteromeric PDGF receptor α/β binds PDGF B, C, and D homodimers, as well as the PDGF AB heterodimer (2). PDGFRα and PDGFRβ can each form heterodimers with EGFR, which is also activated by PDGF (3). Various cells differ in the total number of receptors present and in the receptor subunit composition, which may account for responsive differences among cell types to PDGF binding (4). Ligand binding induces receptor dimerization and autophosphorylation, followed by binding and activation of cytoplasmic SH2 domain-containing signal transduction molecules, such as GRB2, Src, GAP, PI3 kinase, PLCγ, and NCK. A number of different signaling pathways are initiated by activated PDGF receptors and lead to control of cell growth, actin reorganization, migration, and differentiation (5). Tyr751 in the kinase-insert region of PDGFRβ is the docking site for PI3 kinase (6). Phosphorylated pentapeptides derived from Tyr751 of PDGFRβ (pTyr751-Val-Pro-Met-Leu) inhibit the association of the carboxy-terminal SH2 domain of the p85 subunit of PI3 kinase with PDGFRβ (7). Tyr740 is also required for PDGFRβ-mediated PI3 kinase activation (8).

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

Application Methods: Western Blotting

Background: Translation is the process where amino acid residues are assembled into polypeptides on ribosomes. This process is generally divided into three stages: initiation, elongation and termination. During elongation, mRNA and tRNA pair at the two active sites (A and P sites) on the ribosome. A number of eukaryotic elongation factors (eEFs) are involved in this process in mammalian cells (1). eEF1A, also called elongation factor Tu (EF-Tu), binds GTP and interacts with amino acyl-tRNAs to promote recruitment of amino acyl-tRNAs to the A-site of the ribosome (1). After GTP hydrolysis, GDP-eEF1A leaves the ribosome and is later converted back to the GTP-eEF1A by eEF1B (1). Studies have shown that eEF1A is phosphorylated under certain conditions, indicating that its activity is regulated at the post-translational level (2,3).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: PKCν, also known as PKD3, is a member of the protein kinase C (PKC) family of serine/threonine kinases that play critical roles in the regulation of cellular differentiation and proliferation. PKCν is composed of 890 amino acid residues and has 77.3% similarity to human PKCμ (PKCμ) and 77. 4% similarity to mouse PKD (the mouse homolog of PKCμ) (1). The PKCν mRNA is ubiquitously expressed in various tissues. PKCν has two putative diacylglycerol binding C1 domains, suggesting that it may participate in a novel diacylglycerol-mediated signaling pathway (2). PKCν is translocated to the plasma membrane and activated by the diacylglycerol mimic phorbol 12-myristate 13-acetate. PKCν is an important physiologic target of the B-cell receptor (BCR) and exhibits robust activation after BCR engagement (2). GPCR agonists induce a rapid activation of PKCν by a protein kinase C (PKC)-dependent pathway that leads to the phosphorylation of the activation loop of PKCν. PKCν is present both in the nucleus and cytoplasm and this distribution of PKCν results from its continuous shuttling between both compartments by a mechanism that requires a nuclear import receptor and a competent CRM1-nuclear export pathway (3). Cell stimulation with the GPCR agonist neurotensin induces a rapid and reversible plasma membrane translocation of PKCν that is PKC-dependent.

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Chromatin IP, Western Blotting

Background: The most well characterized nuclear receptor corepressors are NCoR1 (nuclear receptor corepressor) and its close paralog NCoR2, also know as SMRT (silencing mediator for retinoic acid and thyroid hormone receptors) (1,2). NCoR1 and SMRT function to transcriptionally silence various unliganded, DNA bound non-steroidal nuclear receptors by serving as a large molecular scaffold that bridges the receptors with multiple chromatin remodeling factors that repress nuclear receptor-mediated gene transcription, in part, through deacetylation of core histones surrounding target promoters. Indeed, the N-terminal portion of NCoR1 and SMRT possess multiple distinct transcriptional repression domains (RDs) responsible for the recruitment of additional components of the corepressor complex such as HDACs, mSin3, GPS2, and TBL1/TBLR1. In between the RDs lies a pair of potent repressor motifs known as SANT motifs (SWI3, ADA2, N-CoR, and TFIIIB), which recruit HDAC3 and histones to the repressor complex in order to enhance HDAC3 activity (3). The C-terminal portion of NCoR1 and SMRT contain multiple nuclear receptor interaction domains (NDs), each of which contains a conserved CoRNR box (or L/I-X-X-I/V-I) motif that allow for binding to various unliganded nuclear hormone receptors such as thyroid hormone (THR) and retinoic acid (RAR) receptors (4,5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Immunoprecipitation, Western Blotting

Background: HS1 (HCLS1, LckBP1, p75) is a protein kinase substrate that is expressed only in tissues and cells of hematopoietic origin (1,2). HS1 contains four cortactin repeats and a single SH3 domain (2). This intracellular protein is phosphorylated following immune receptor activation, which promotes recruitment of HS1 to the immune synapse (3-5). Phosphorylation of HS1 is required to regulate actin dynamics and provide docking sites for many other signaling molecules, such as Vav1 and PLCγ1 (6). HS1 also plays an important role in platelet activation (7).

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

Application Methods: Western Blotting

Background: Erk5 (Mitogen-activated protein kinase 7, Big mitogen-activated protein kinase 1) is a member of the MAPK superfamily implicated in the regulation numerous cellular processes including proliferation, differentiation, and survival (1-4). Like other MAPK family members, Erk5 contains a canonical activation loop TEY motif (Thr218/Tyr220) that is specifically phosphorylated by MAP2K5 (MEK5) in a growth-factor-dependent, Ras-independent mechanism (5-7). For example, EGF stimulation promotes Erk5 phosphorylation that induces its translocation to the nucleus where it phosphorylates MEF2C and other transcriptional targets (5,6). Erk5 is also activated in response to granulocyte colony-stimulating factor (G-CSF) in hematopoietic progenitor cells where it promotes survival and proliferation (7). In neuronal cells, Erk5 is required for NGF-induced neurite outgrowth, neuronal homeostasis, and survival (8,9). Erk5 is thought to play a role in blood vessel integrity via maintenance of endothelial cell migration and barrier function (10-12). Although broadly expressed, research studies have shown that mice lacking erk5 display numerous cardiac defects, suggesting Erk5 plays a critical role in vascular development and homeostasis (1,2).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

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

Background: There are three members of the steroid receptor co-activator (SRC) family of proteins: SRC-1 (NCoA-1), SRC-2 (TIF2/GRIP1/NCoA-2), and SRC-3 (ACTR/pCIP/RAC3/TRAM-1/AIB1). All SRC family members share significant structural homology and function to stimulate transcription mediated by nuclear hormone receptors and other transcriptional activators such as Stat3, NF-κB, E2F1, and p53 (1-4). Two SRC proteins, SRC-1 and SRC-3, function as histone acetyltransferases (5,6). In addition, all three family members can recruit other histone acetyltransferases (CBP/p300, PCAF) and histone methyltransferases (PRMT1, CARM1) to target promoters and cooperate to enhance expression of many genes (5-8). The SRC proteins play important roles in multiple physiological processes including cell proliferation, cell survival, somatic cell growth, mammary gland development, female reproductive function, and vasoprotection (9). SRC-1 and SRC-3 are conduits for kinase-mediated growth factor signaling to the estrogen receptor and other transcriptional activators. Seven SRC-1 phosphorylation sites and six SRC-3 phosphorylation sites have been identified, which are induced by steroids, cytokines, and growth factors and involve multiple kinase signaling pathways (9-11). Research has shown that all three SRC family members are associated with increased activity of nuclear receptors in breast, prostate, and ovarian carcinomas. According to the literature, SRC-3 is frequently amplified or overexpressed in a number of cancers (12), and SRC-1/PAX3 and SRC-2/MYST3 translocations are found associated with rhabdomyosarcoma and acute myeloid leukemia, respectively (13,14).

$260
100 µl
APPLICATIONS
REACTIVITY
Mouse, Rat

Application Methods: Western Blotting

Background: Myosin is composed of six polypeptide chains: two identical heavy chains and two pairs of light chains. Myosin light chain 2 (MLC2), also known as myosin regulatory light chain (MRLC), RLC, or LC20, has many isoforms with varying tissue distribution. Smooth muscle MLC2 is phosphorylated at Thr18 and Ser19 by myosin light chain kinase (MLCK) in a Ca2+/calmodulin-dependent manner (1). These phosphorylation events are correlated with myosin ATPase activity and smooth muscle contraction (2). Striated muscle contraction is regulated by the troponin-tropomyosin complex in thin actin filaments and by binding of Ca2+ to troponin C (3). Two types of myosin light chain are expressed in the heart, with myosin light chain 2v (MYL2, MLC-2v) expression restricted to the ventricles and myosin light chain 2a (MYL7, MLC-2a) found specific to the atria. Mutations in the corresponding MYL2 gene are found in patients diagnosed with a form of hypertrophic cardiomyopathy characterized by thickening of the mid-left ventricle.

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

Application Methods: Western Blotting

Background: Ubiquitinating enzymes (UBEs) catalyze protein ubiquitination, a reversible process countered by deubiquitinating enzyme (DUB) action (1,2). Five DUB subfamilies are recognized, including the USP, UCH, OTU, MJD, and JAMM enzymes. USP4 was originally identified during a survey of murine genes near the Mpv20 retroviral insertion site and intially referred to as Ubiquitous Nuclear Protein (UNP). Analysis of the mouse cDNA originally identified Usp4/Unp as a proto-oncogene related to the human tre-2/tre-17/USP6 proto-oncogene (3,4). Usp4/Unp was subsequently observed to contain the conserved Cys and His boxes of the UBP family (5,6) as well as DUB activity (7,8). In a study of primary lung tumor tissue, it was observed that the human homolog of Usp4, USP4/UNPH, had elevated gene expression levels in small cell tumors and adenocarcinomas of the lung, suggesting a causative role for USP4 in neoplasia (6). Another recent study demonstrated overexpression of USP4 in several types of human cancer and that USP4 positively contributes to cell transformation by negatively regulating p53 levels (9). Both murine and human USP4 have been shown to interact with the Rb family of tumor suppressor proteins, providing additional mechanistic evidence of a role for USP4 in cellular transformation (10, 11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: CYLD is a cytoplasmic deubiquitinating enzyme encoded by a tumor suppressor gene altered in individuals diagnosed with cylindromatosis, a genetic condition characterized by benign tumors of skin appendages (1,2). Functional CYLD deubiquitinase regulates inflammation and cell proliferation by down regulating NF-κB signaling through removal of ubiquitin chains from several NF-κB pathway proteins (3,4). CYLD is a negative regulator of proximal events in Wnt/β-catenin signaling and is a critical regulator of natural killer T cell development (5,6). The transcription factor Snail can inhibit CYLD expression, resulting in melanoma cell proliferation (7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: The ZFX (X-linked zinc finger protein) gene is expressed from the inactive X chromosome and is structurally similar to its homologue on the Y chromosome, ZFY (1). Transcripts of ZFX and ZFY encode proteins composed of a highly acidic amino-terminal domain and a carboxy-terminal zinc-finger motif that is commonly associated with nucleic acid-binding proteins (2). Both ZFY and ZFX are probable transcriptional activators and may function in sex determination (3). Multiple alternatively spliced transcript variants of ZFX, encoding different isoforms, have been identified and may be functionally distinct (2). Conditional gene targeting studies in mouse have suggested ZFX is also required for self-renewal of embryonic and hematopoietic stem cells (4). ZFX has also been suggested to play a role in proliferation and expansion of B cells, and could contribute to lymphocyte homeostasis (5).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Mouse, Rat

Application Methods: Western Blotting

Background: The serine/threonine PI3 kinase regulatory subunit 4 (PIK3R4, Vps15) is the mammalian homologue of the yeast vacuolar protein sorting 15 (1). PIK3R4 regulates the kinase activity of PI3K class III and anchors the kinase to cellular membranes through myristoylation (2,3). Recruitment of PI3K class III to the site of early endosome fusion and docking is directly mediated by PIK3R4 binding to the small GTPase Rab5 through its HEAT and WD-40 domains (4,5). The PIK3R4/PI3K class III plays a role in late endosome function through PIK3R4 binding to the Rab7 GTPase (6). In addition to its role in trafficking, the PIK3R4/PI3K class III complex interacts with beclin-1 to play a role during several stages of autophagy. Autophagosome formation is stimulated when Atg14 complexes with PIK3R4, PI3K class III, and beclin-1. The UVRAG protein competes with Atg14 for beclin-1 binding, forming a mutually exclusive complex with PIK3R4, PI3K class III, and beclin-1 that regulates autophagosome maturation. Autophagosome maturation is impaired in the presence of the beclin-1-binding protein Rubicon (7,8). Co-expression of PIK3R4 is required for PI3K class III activation and regulation by both beclin-1/UVRAG and by nutrients (9). Overexpression of PIK3R4 protein has been associated with decreased survival in patients with ovarian tumors, while mutations of the corresponding PIK3R4 gene are associated with metastatic melanoma, suggesting that PIK3R4 functions in cancer (10,11).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Acetylation of the histone tail causes chromatin to adopt an "open" conformation, allowing increased accessibility of transcription factors to DNA. The identification of histone acetyltransferases (HATs) and their large multiprotein complexes has yielded important insights into how these enzymes regulate transcription (1,2). HAT complexes interact with sequence-specific activator proteins to target specific genes. In addition to histones, HATs can acetylate nonhistone proteins, suggesting multiple roles for these enzymes (3). In contrast, histone deacetylation promotes a "closed" chromatin conformation and typically leads to repression of gene activity (4). Mammalian histone deacetylases can be divided into three classes on the basis of their similarity to various yeast deacetylases (5). Class I proteins (HDACs 1, 2, 3, and 8) are related to the yeast Rpd3-like proteins, those in class II (HDACs 4, 5, 6, 7, 9, and 10) are related to yeast Hda1-like proteins, and class III proteins are related to the yeast protein Sir2. Inhibitors of HDAC activity are now being explored as potential therapeutic cancer agents (6,7).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey

Application Methods: Immunoprecipitation, Western Blotting

Background: The tumor necrosis factor receptor family, which includes TNF-RI, Fas, DR3, DR4, DR5, and DR6, plays an important role in the regulation of apoptosis in various physiological systems (1,2). The receptors are activated by a family of cytokines that include TNF, FasL, and TRAIL. They are characterized by a highly conserved extracellular region containing cysteine-rich repeats and a conserved intracellular region of about 80 amino acids termed the death domain (DD). The DD is important for transducing the death signal by recruiting other DD containing adaptor proteins (FADD, TRADD, RIP) to the death-inducing signaling complex (DISC), resulting in activation of caspases.

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

Application Methods: Western Blotting

Background: The 90 kDa ribosomal S6 kinases (RSK1-4) are a family of widely expressed Ser/Thr kinases characterized by two nonidentical, functional kinase domains (1) and a carboxy-terminal docking site for extracellular signal-regulated kinases (ERKs) (2). Several sites both within and outside of the RSK kinase domain, including Ser380, Thr359, Ser363, and Thr573, are important for kinase activation (3). RSK1-3 are activated via coordinated phosphorylation by MAPKs, autophosphorylation, and phosphoinositide-3-OH kinase (PI3K) in response to many growth factors, polypeptide hormones, and neurotransmitters (3).

$122
20 µl
$303
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse, Rat

Application Methods: Immunoprecipitation, Western Blotting

Background: PTEN (phosphatase and tensin homologue deleted on chromosome ten), also referred to as MMAC (mutated in multiple advanced cancers) phosphatase, is a tumor suppressor implicated in a wide variety of human cancers (1). PTEN encodes a 403 amino acid polypeptide originally described as a dual-specificity protein phosphatase (2). The main substrates of PTEN are inositol phospholipids generated by the activation of the phosphoinositide 3-kinase (PI3K) (3). PTEN is a major negative regulator of the PI3K/Akt signaling pathway (1,4,5). PTEN possesses a carboxy-terminal, noncatalytic regulatory domain with three phosphorylation sites (Ser380, Thr382, and Thr383) that regulate PTEN stability and may affect its biological activity (6,7). PTEN regulates p53 protein levels and activity (8) and is involved in G protein-coupled signaling during chemotaxis (9,10).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: The evolutionarily conserved CCR4-NOT (CNOT) complex regulates mRNA metabolism in eukaryotic cells (1). This regulation occurs at different levels of mRNA synthesis and degradation, including transcription initiation, elongation, deadenylation, and degradation (1). Multiple components, including CNOT1, CNOT2, CNOT3, CNOT4, CNOT6, CNOT6L, CNOT7, CNOT8, CNOT9, and CNOT10 have been identified in this complex (2). In addition, subunit composition of this complex has been shown to vary among different tissues (3).

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

Application Methods: Chromatin IP, Immunoprecipitation, Western Blotting

Background: Methyltransferase-like protein 3 (METTL3) and methytransferase-like protein 14 (METTL14) are the two catalytic subunits of an N6-methyltransferase complex that methylates adenosine residues in RNA (1). Methylation of adenosine residues regulates mRNA splicing, processing, translation efficiency, editing and stability, in addition to regulating primary miRNA processing, and is critical for proper regulation of the circadian clock, embryonic stem cell self-renewal, immune tolerance, response to various stimuli, meiosis and mouse fertility (2,3). In this complex, METTL3 functions as the catalytic methyltransferase subunit and METTL14 functions as the target recognition subunit by binding to RNA (4). In addition, the Wilms tumor 1-associated protein (WTAP) functions as a regulatory subunit and is required for accumulation of the complex to nuclear speckles, which are sites of RNA processing (5). Several studies suggest a role for this complex in cancer. METTL3 expression is elevated in lung adenocarcinoma where it promotes growth, survival and invasion of human lung cancer cells (6). In addition, WTAP is over-expressed in a number of different cancers and positively regulates cell migration and invasion in glioblastoma and cholangiocarcinoma (7,8).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Western Blotting

Background: B-cell CLL/lymphoma 9 protein (BCL9) is a widely conserved adaptor protein that functions as a transcriptional co-activator in the canonical Wnt signaling pathway (1,2). BCL9 is a core component of a nuclear protein complex (BCL9, LEF/TCF, β-catenin and PYGO) that regulates the transcription of Wnt-dependent target genes (3). Research studies show that disrupting the interaction between BCL9 and β-catenin suppresses oncogenic Wnt signaling, suggesting a potential avenue for therapeutic intervention in Wnt-mediated cancers (4). BCL9 promotes association of PYGO with the tail of histone H3 that has been methylated at lysine 4 (H3K4me), suggesting a specific chromatin remodeling function for BCL9 in the Wnt signaling pathway (5). Research studies in colon epithelium and adenocarcinomas suggest that BCL9 is required to mediate Wnt-dependent stem cell behaviors, such as epithelial-mesenchymal transition (6). Crystallography studies revealed that BCL9 contains a β-catenin binding site that is distinct from the majority of known β-catenin binding partners, making it an attractive target for therapeutic drug development (7).

The Phospho-HER2/ErbB2 Antibody Sampler Kit provides an economical means to evaluate the activation status of HER2/ErbB2, including the phosphorylation of Tyr1248 and Tyr1221/1222. The control HER2/ErbB2 antibody is also included. The kit contains enough primary antibodies to perform two Western blot experiments per primary antibody.

Background: The ErbB2 (HER2) proto-oncogene encodes a 185 kDa transmembrane, receptor-like glycoprotein with intrinsic tyrosine kinase activity (1). While ErbB2 lacks an identified ligand, ErbB2 kinase activity can be activated in the absence of a ligand when overexpressed and through heteromeric associations with other ErbB family members (2). Amplification of the ErbB2 gene and overexpression of its product are detected in almost 40% of human breast cancers (3). Binding of the c-Cbl ubiquitin ligase to ErbB2 at Tyr1112 leads to ErbB2 poly-ubiquitination and enhances degradation of this kinase (4). ErbB2 is a key therapeutic target in the treatment of breast cancer and other carcinomas and targeting the regulation of ErbB2 degradation by the c-Cbl-regulated proteolytic pathway is one potential therapeutic strategy. Phosphorylation of the kinase domain residue Tyr877 of ErbB2 (homologous to Tyr416 of pp60c-Src) may be involved in regulating ErbB2 biological activity. The major autophosphorylation sites in ErbB2 are Tyr1248 and Tyr1221/1222; phosphorylation of these sites couples ErbB2 to the Ras-Raf-MAP kinase signal transduction pathway (1,5).

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

Application Methods: Immunoprecipitation, Western Blotting

Background: Protein ubiquitination requires the concerted action of the E1, E2, and E3 ubiquitin-conjugating enzymes. Ubiquitin is first activated through ATP-dependent formation of a thiol ester with ubiquitin-activating enzyme E1. The activated ubiquitin is then transferred to a thiol group of ubiquitin-carrier enzyme E2. The final step is the transfer of ubiquitin from E2 to an ε-amino group of the target protein lysine residue, which is mediated by ubiquitin-ligase enzyme E3 (1).

$260
100 µl
APPLICATIONS
REACTIVITY
Human, Monkey, Mouse

Application Methods: Immunoprecipitation, Western Blotting

Background: Import and export through the nuclear envelope (NE) via facilitated translocation is important for many cellular processes including protein synthesis and miRNA biogenesis (1). Exportin 5 (XPO5) is a member of the importin β family of proteins (2) and functions in tRNA export in a sequence dependent fashion. More recently, it has been shown to export pre-miRNA by a RanGTPase-driven process from the nucleus to the cytoplasm, where pre-miRNA processing occurs to produce mature miRNAs (1,3). Study of the miRNA biosynthesis pathway is essential toward understanding the process of oncogenesis as global downregulation of miRNAs and the resulting alterations in expression of tumor suppressor and oncogenic proteins is a common phenotype of cancers cells (3,4). Research studies have shown that disruption of exportin 5 functions in many types of cancers including breast and lung, where pre-miRNA accumulates in the nucleus and miRNA maturation is impaired (2,3).

$260
100 µl
APPLICATIONS
REACTIVITY
Human

Application Methods: Flow Cytometry, Immunoprecipitation, Western Blotting

Background: Dectin-1 is a C-type lectin receptor expressed by macrophages, monocytes, dendrtic cells, neutrophils, and a subset of γδ T cells (1,2). Dectin-1 is a glycoprotein with eight different isoforms, generated through alternative splicing (3-5). It plays an important role in anti-fungal immunity by acting as a pattern recognition receptor for β-glucans found on the cell wall of fungi and some bacteria (5,6). Dectin-1 is composed of a short amino-terminal cytoplasmic domain containing an ITAM-like motif, a transmembrane domain, and an extracellular carboxy-terminal C-type lectin domain (5). Dectin-1 recognizes β-glucans through its C-type lectin domain and transduces signals through its ITAM-like motif by recruiting and activating Syk (7,8). Dendritic cells activated through Dectin-1 promote differentiation of Th17 cells by producing IL-6 and IL-23 (9).

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

Application Methods: Chromatin IP, Chromatin IP-seq, Immunoprecipitation, Western Blotting

Background: Negative Elongation Factor (NELF) consists of four subunits: WHSC2 (NELF-A), COBRA-1 (NELF-B), TH1L (NELF-C/D), and NELF-E (1). NELF, together with DRB-sensitivity inducing factor (DSIF), inhibits RNA Polymerase II (RNAPII) elongation resulting in RNAPII promoter proximal pausing, where it waits additional signaling to resume transcription (2,3). The release of RNAPII from promoter proximal pausing is a critical regulatory point during transcription and is signaled by positive transcription elongation factor (p-TEF-b) phosphorylation of both NELF and the carboxy-terminal domain (CTD) within the largest subunit of RNAPII (3,4). WHSC2 is thought to connect the NELF complex to RNAPII machinery, while NELF-E contains an RNA binding motif that is necessary for NELF function (1,5,6). TH1L, together with COBRA-1, are integral subunits that bring WHSC2 and NELF-E together in the NELF complex (1).