192260 Results for: "Comparator+Kits&pageNo=50&view=easy"

Supplier: Bioss

Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes can lead to severe genetic diseases, such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD13B (ankyrin repeat domain 13B) is a 626 amino acid protein that contains two ANK repeats and three ubiquitin-interacting motif (UIM) repeats. Conserved in dog, cow, mouse and rat, ANKRD13B exists as two alternatively spliced isoforms. The gene that encodes ANKRD13B maps to human chromosome 17, which makes up over 2.5% of the human genome, with about 81 million bases encoding over 1,200 genes. Two key tumor suppressor genes are associated with chromosome 17, namely, p53 and BRCA1. Malfunction or loss of p53 expression is associated with malignant cell growth and Li-Fraumeni syndrome. BRCA1 is recognized as a genetic determinant of early onset breast cancer. Chromosome 17 is also linked to neurofibromatosis, dysregulated Schwann cell growth, Alexander disease, Birt-Hogg-Dube syndrome and Canavan disease.

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Ankyrins are a family of proteins that link the integral membrane proteins to the underlying spectrin-actin cytoskeleton and play key roles in activities such as cell motility, activation, proliferation, contact and the maintenance of specialized membrane domains. Multiple isoforms of ankyrin with different affinities for various target proteins are expressed in a tissue-specific, developmentally regulated manner. Most ankyrins are typically composed of three structural domains: an amino-terminal domain containing multiple ankyrin repeats; a central region with a highly conserved spectrin binding domain; and a carboxy-terminal regulatory domain which is the least conserved and subject to variation. Ankyrin 1, the prototype of this family, was first discovered in the erythrocytes, but since has also been found in brain and muscles. Mutations in erythrocytic ankyrin 1 have been associated in approximately half of all patients with hereditary spherocytosis. Complex patterns of alternative splicing in the regulatory domain, giving rise to different isoforms of ankyrin 1 have been described. Truncated muscle-specific isoforms of ankyrin1 resulting from usage of an alternate promoter have also been identified. [provided by RefSeq, Dec 2008].

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Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

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Composed of more than ten subunits, the anaphase-promoting complex (APC) acts in a cell-cycle dependent manner to promote the separation of sister chromatids during the transition between metaphase and anaphase in mitosis. APC, or cyclosome, accomplishes this progression through the ubiquitination of mitotic cyclins and other regulatory proteins that are targeted for destruction during cell division. APC is phosphorylated, and thus activated, by protein kinases Cdk1/cyclin B and polo-like kinase (Plk). APC is under tight control by a number of regulatory factors, including CDC20, CDH1 and MAD2. Specifically, CDC20 and CDH1 directly bind to and activate the cyclin-ubiquitination activity of APCs. In contrast, MAD2 inhibits APC by forming a ternary complex with CDC20 and APC, thus preventing APC activation. APC10 contains a Doc1 homology domain, which is a beta-sandwich structure common to many other putative E3 ubiquitin ligases. APC10 binds to core APC subunits throughout the cell cycle. Specifically, APC10 binds to the C-terminus of CDC27/APC3. During mitosis, APC10 is localized in centrosomes and mitotic spindles. APC10 also localizes to kinetochores from prophase to anaphase, and to the midbody in telophase and cytokinesis.

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P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.

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ATP-binding cassette (ABC) transporters are an evolutionarily conserved family of widely-expressed proteins that use ATP hydrolysis to catalyze the transport of various molecules across extracellular and intracellular membranes. Eukaryotic ABC transporters are largely responsible for trafficking hydrophobic compounds either within the cell as part of a metabolic process, outside the cell for transport to other organs, or for secretion from the body. The cholesterol-responsive transporter, ABCA7, maps to human chromosome 19 and mouse chromosome 10 and has been reported as a candidate regulator of ceramide transport in epidermal lipid reorganization. High expression levels of ABCA7 have been reported in myelolymphatic tissues, reticuloendothelial cells, peripheral leukocytes, thymus, spleen and bone marrow. This expression pattern of the two alternatively-spliced isoforms also indicates an involvement in lipid homeostasis in cells of the immune system, though the complete role of ABCA7 is not yet known. Full-length type I ABCA7 has shown plasma membrane localization, while the type II splicing variant has shown expression predominantly in the endoplasmic reticulum.

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Mediates interactions of advanced glycosylation end products (AGE). These are nonenzymatically glycosylated proteins which accumulate in vascular tissue in aging and at an accelerated rate in diabetes. Acts as a mediator of both acute and chronic vascular inflammation in conditions such as atherosclerosis and in particular as a complication of diabetes. AGE/RAGE signaling plays an important role in regulating the production/expression of TNF-alpha, oxidative stress, and endothelial dysfunction in type 2 diabetes. Interaction with S1A12 on endothelium, mononuclear phagocytes, and lymphocytes triggers cellular activation, with generation of key proinflammatory mediators. Receptor for amyloid beta peptide. Contributes to the translocation of amyloid-beta peptide (ABPP) across the cell membrane from the extracellular to the intracellular space in cortical neurons. ABPP-initiated RAGE signaling, especially stimulation of p38 mitogen-activated protein kinase (MAPK), has the capacity to drive a transport system delivering ABPP as a complex with RAGE to the intraneuronal space. Can also bind oligonucleotides (By similarity). Interaction with S1B after myocardial infarction may play a role in myocyte apoptosis by activating ERK1/2 and p53/TP53 signaling.

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c-Jun NH2-terminal kinases (JNKs) are distant members of the MAP kinase family (1). JNK1 is activated by dual phosphorylation at a Thr-Pro-Tyr motif in response to ultraviolet (UV) light, and it functions to phosphorylate c-Jun at amino terminal serine regulatory sites, Ser-63 and Ser-73, resulting in transcriptional activation (2-5). Two additional JNK family members have been identified as JNK2 and JNK3 (3). JIP-1 (for JNK interacting protein-1) has been identified as a cytoplasmic inhibitor of JNK that retains JNK in the cytoplasm, thereby inhibiting JNK-regulated gene expression. Evidence suggests that JNK1 and JNK2 bind to JIP-1 with greater affinity than to ATF-2 and c-Jun, which are targets of the JNK signaling pathway. JIP-1 contains an amino terminal JNK binding domain and a carboxy terminal SH3 domain. ATF-2 and c-Jun also contain the JNK binding domain and are thought to compete with JIP-1 for JNK binding (6). Multiple splice variants if JIP-1, including JIP-1b, JIP-1c (also designated islet-brain 1 or IB-1), JIP-2a, JIP-2b and JIP-3, have been identified in brain (7).

Supplier: Bioss

JNK1(MAPK8) is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha induced apoptosis. This kinase is also involved in UV radiation induced apoptosis, which is thought to be related to cytochrome c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.JNK1 is activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. The JNK pathway is critically involved in diabetes and levels are abnormally elevated in obesity. The cell-permeable JNK inhibitory peptide may have promise as a therapeutic agent for diabetes.

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Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing receptor) or chemokine-scavenging receptor or chemokine decoy receptor. Acts as a receptor for chemokines CXCL11 and CXCL12/SDF1. Chemokine binding does not activate G-protein-mediated signal transduction but instead induces beta-arrestin recruitment, leading to ligand internalization and activation of MAPK signaling pathway. Required for regulation of CXCR4 protein levels in migrating interneurons, thereby adapting their chemokine responsiveness. In glioma cells, transduces signals via MEK/ERK pathway, mediating resistance to apoptosis. Promotes cell growth and survival. Not involved in cell migration, adhesion or proliferation of normal hematopoietic progenitors but activated by CXCL11 in malignant hemapoietic cells, leading to phosphorylation of ERK1/2 (MAPK3/MAPK1) and enhanced cell adhesion and migration. Plays a regulatory role in CXCR4-mediated activation of cell surface integrins by CXCL12. Required for heart valve development. Acts as coreceptor with CXCR4 for a restricted number of HIV isolates.

Supplier: Bioss

The sense of taste provides animals with valuable information about the quality and nutritional value of food. A family of G protein-coupled receptors are involved in taste perception and include T1R, which is involved in sweet and umami taste perception, and T2R, which is involved in bitter taste perception. Both types of taste receptors couple to various G proteins to initiate signal transduction cascades. Single taste receptor cells express a variety of T2Rs, suggesting that each cell is capable of recognizing multiple tastants. T2R6 (also designatedT2R30, mt2r42, STC 7-4 or taste receptor, type 2, member 130) is an integral membrane receptor protein in mice that may play a role in the perception of bitterness and in sensing the chemical composition of the gastrointestinal content. The activity of this receptor may stimulate Alpha-gustducin, mediate PLC-Beta-2 activation and lead to the gating of TRPM5. T2R6 is expressed in subsets of taste receptor cells of the tongue and palate epithelium and exclusively in gustducin-positive cells. The human homolog of T2R6, designated T2R7 (TAS2R7, TRB4 or taste receptor, type 2, member 7) is a G protein-coupled receptor expressed in taste receptor cells of the tongue and palate epithelia.

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C2CD3 (C2 domain-containing protein 3), also known as FLJ34770, is a 2,353 amino acid protein that contains two C2 domains. C2 domains are regions of about 130 amino acid residues that are found in proteins that bind phospholipids. It is thought that calcium binding to the C2 domain induces an electrostatic potential change that enhances phospholipid binding, which suggests a role for the domain as an electrostatic switch. C2CD3 is expressed as five isoforms produced by alternative splicing events. The gene that encodes C2CD3 maps to human chromosome 11, which makes up around 4% of human genomic DNA. The chromosome 11 encoded Atm gene is important for regulation of cell cycle arrest and apoptosis following double strand DNA breaks. Atm mutation leads to the disorder known as ataxia-telangiectasia. The blood disorders Sickle cell anemia and β thalassemia are caused by HBB gene mutations. Wilms' tumors, WAGR syndrome and Denys-Drash syndrome are associated with mutations of the WT1 gene. Jervell and Lange-Nielsen syndrome, Jacobsen syndrome, Niemann-Pick disease, hereditary angioedema and Smith-Lemli-Opitz syndrome are also associated with defects in chromosome 11.

Supplier: Bioss

Key regulator of entry into cell division that acts as a tumor suppressor. Promotes G-G1 transition when phosphorylated by CDK3/cyclin-C. Acts as a transcription repressor of E2F1 target genes. The underphosphorylated, active form of RB1 interacts with E2F1 and represses its transcription activity, leading to cell cycle arrest. Directly involved in heterochromatin formation by maintaining overall chromatin structure and, in particular, that of constitutive heterochromatin by stabilizing histone methylation. Recruits and targets histone methyltransferases SUV39H1, SUV42H1 and SUV42H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-2' trimethylation. Inhibits the intrinsic kinase activity of TAF1. Mediates transcriptional repression by SMARCA4/BRG1 by recruiting a histone deacetylase (HDAC) complex to the c-FOS promoter. In resting neurons, transcription of the c-FOS promoter is inhibited by BRG1-dependent recruitment of a phospho-RB1-HDAC1 repressor complex. Upon calcium influx, RB1 is dephosphorylated by calcineurin, which leads to release of the repressor complex (By similarity). In case of viral infections, interactions with SV4 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

Supplier: Bioss

Ankyrins are membrane adaptor molecules that play important roles in coupling integral membrane proteins to the spectrin-based cytoskeleton network. Mutations of ankyrin genes lead to severe genetic diseases, such as fatal cardiac arrhythmias and hereditary spherocytosis. ANKRD22 (ankyrin repeat domain 22) is a 191 amino acid protein that contains four ANK repeats. Conserved in chimpanzee, dog, cow, mouse, rat, chicken and zebrafish, ANKRD22 is encoded by a gene that maps to human chromosome 10. Chromosome 10 encodes nearly 1,200 genes within 135 million bases, making up approximately 4.5% of the human genome. Several protein-coding genes, including those that encode for chemokines, cadherins, excision repair proteins, early growth response factors (Egrs) and fibroblast growth receptors (FGFRs), are located on chromosome 10. Defects in genes that map to chromosome 10 are associated with Charcot-Marie Tooth disease, Jackson-Weiss syndrome, Usher syndrome, nonsyndromatic deafness, Wolman’s syndrome, Cowden syndrome, multiple endocrine neoplasia type 2 and porphyria.

Supplier: Bioss

Converts sphingomyelin to ceramide. Also has phospholipase C activities toward 1,2-diacylglycerolphosphocholine and 1,2-diacylglycerolphosphoglycerol. Isoform 2 and isoform 3 have lost catalytic activity.Involvement in disease: Defects in SMPD1 are the cause of Niemann-Pick disease type A (NPDA) ; also known as Niemann-Pick disease classical infantile form. It is an early-onset lysosomal storage disorder caused by failure to hydrolyze sphingomyelin to ceramide. It results in the accumulation of sphingomyelin and other metabolically related lipids in reticuloendothelial and other cell types throughout the body, leading to cell death. Niemann-Pick disease type A is a primarily neurodegenerative disorder characterized by onset within the first year of life, mental retardation, digestive disorders, failure to thrive, major hepatosplenomegaly, and severe neurologic symptoms. The severe neurological disorders and pulmonary infections lead to an early death, often around the age of four. Clinical features are variable. A phenotypic continuum exists between type A (basic neurovisceral) and type B (purely visceral) forms of Niemann-Pick disease, and the intermediate types encompass a cluster of variants combining clinical features of both types A and B.

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The LIM-only (LMO) proteins, LMO1 and LMO2, are nuclear factors that are characterized by a conserved LIM domain. The LIM domain consists of a cysteine-rich zinc-binding motif that is present in a variety of transcription factors, including the LIM homeobox (LHX) proteins expressed in the central nervous system and involved in cell differentiation. LMO1 and LMO2 are expressed in the adult CNS in a cell type-specific manner, where they are differentially regulated by neuronal activity and are involved in regulating the cellular differentiated phenotype of neurons. LMO2 lacks a specific DNA-binding homeobox domain but rather assembles into transcriptional regulatory complexes to mediate gene expression by interacting with the widely expressed nuclear LIM interactor (NLI). NLI, known also as CLIM-1, and the related protein CLIM-2, facilitate the formation of heteromeric LIM complexes and also enhance the nuclear retention of LIM proteins. LMO2 and the related protein LMO4 are expressed in thymic precursor cells. LMO4 is also expressed in mature T cells, cranial neural crest cells, somite, dorsal limb bud mesenchyme, motor neurons, and Schwann cell progenitors.

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Neurexins comprise a family of neuronal cell surface proteins, which include neurexin I (NRXN1), neurexin II (NRXN2), neurexin III (NRXN3) and Caspr (neurexin IV). Neurexins I-III are expressed as a and b isoforms. The a isoforms are made of three cassettes, which contain two LNS (Laminin A, Neurexins, Sex hormone-binding)-domains separated by EGF domains, followed by a transmembrane region and a 55 amino acid cytoplasmic C-terminal. The a isoforms bind to neurexophilins at the second LNS site and to the excitatory neurotoxin a-latrotoxin. The b isoforms have only one LNS-domain, bind to neuroligins, and play a role in the formation and remodeling of synapes. Caspr (for Contactin-Associated Protein 1, also designated Paranodin in mouse), contains an extracellular domain similar to the other three neurexins, and binds to the surface glycoprotein Contactin. Caspr and the closely related Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), demarcate distinct subdomains in myelinated axons. Specifically, Caspr exists at the paranodal junctions, while Caspr2 colocalizes with Shaker-like K+ channels in the juxtaparanodal region. Caspr may play a role in the communication of glial cells and neurons during development.

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PDZRN3 contains a RING-finger motif in its N-terminal region, two PDZ domains in its central region and a consensus-binding motif for PDZ domains at its C-terminus. It was identified in silico as a homolog of the protein known as LNX1 or SEMCAP1, which possesses ubiquitin ligase activity and binds the membrane protein Semaphorin 4C. However, PDZRN3 itself has not previously been characterized. We have now evaluated the properties and functions of PDZRN3. The PDZRN3 gene was shown to be expressed in various human tissues including the heart, skeletal muscle and liver and its expression in mouse skeletal muscle was developmentally regulated. Both the differentiation of C2C12 mouse skeletal myoblasts into myotubes and injury-induced muscle regeneration in vivo were found to be accompanied by up-regulation of PDZRN3. The differentiation-associated increase in the expression of PDZRN3 in C2C12 cells follows that of myogenin and precedes that of myosin heavy chain. Depletion of PDZRN3 by RNA interference inhibited the formation of myotubes as well as the associated up-regulation of myosin heavy chain in C2C12 cells. Our data suggest that PDZRN3 plays an essential role in the differentiation of myoblasts into myotubes by acting either downstream or independently of myogenin.

Supplier: Bioss

Serine/threonine-protein kinase that plays a critical role in initiating innate immune response against foreign pathogens. Involved in Toll-like receptor (TLR) and IL-1R signaling pathways. Is rapidly recruited by MYD88 to the receptor-signaling complex upon TLR activation. Association with MYD88 leads to IRAK1 phosphorylation by IRAK4 and subsequent autophosphorylation and kinase activation. Phosphorylates E3 ubiquitin ligases Pellino proteins (PELI1, PELI2 and PELI3) to promote pellino-mediated polyubiquitination of IRAK1. Then, the ubiquitin-binding domain of IKBKG/NEMO binds to polyubiquitinated IRAK1 bringing together the IRAK1-MAP3K7/TAK1-TRAF6 complex and the NEMO-IKKA-IKKB complex. In turn, MAP3K7/TAK1 activates IKKs (CHUK/IKKA and IKBKB/IKKB) leading to NF-kappa-B nuclear translocation and activation. Alternatively, phosphorylates TIRAP to promote its ubiquitination and subsequent degradation. Phosphorylates the interferon regulatory factor 7 (IRF7) to induce its activation and translocation to the nucleus, resulting in transcriptional activation of type I IFN genes, which drive the cell in an antiviral state. When sumoylated, translocates to the nucleus and phosphorylates STAT3.

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The Drosophila hairy and Enhancer of split genes encode basic helix-loop-helix (bHLH) transcriptional repressors that function in the Notch signaling pathway and control segmentation and neural development during embryogenesis. The mammalian homologues of Drosophila hairy and Enhancer of split are the HES gene family members, HES1-6, which also encode bHLH transcriptional repressors that regulate myogenesis and neurogenesis. The HES family members form a complex with TLE, the mammalian homologue of Groucho, and this interaction is mediated by the carboxy terminal WRPW motif of the HES proteins. The HES/TLE complex functions by directly binding to DNA, instead of interfering with activator proteins. Most HES family members, including HES1 and HES5, preferentially bind to the N box (CACNAG) as opposed to the E box (CANNTG). HES2 binds to both N and E box sites, while HES6 does not bind DNA. Rather, HES6 inhibits HES1 activity, thereby promoting transcription. HES1 and HES2 are expressed in a variety of adult and embryonic tissues. HES3 is expressed exclusively in cerebellar Purkinje cells, and HES5 is found solely in the nervous system. HES6 is produced in brain as well as in the limb buds of developing embryos.

Supplier: Bioss

The Drosophila hairy and Enhancer of split genes encode basic helix-loop-helix (bHLH) transcriptional repressors that function in the Notch signaling pathway and control segmentation and neural development during embryogenesis. The mammalian homologues of Drosophila hairy and Enhancer of split are the HES gene family members, HES1-6, which also encode bHLH transcriptional repressors that regulate myogenesis and neurogenesis. The HES family members form a complex with TLE, the mammalian homologue of Groucho, and this interaction is mediated by the carboxy terminal WRPW motif of the HES proteins. The HES/TLE complex functions by directly binding to DNA, instead of interfering with activator proteins. Most HES family members, including HES1 and HES5, preferentially bind to the N box (CACNAG) as opposed to the E box (CANNTG). HES2 binds to both N and E box sites, while HES6 does not bind DNA. Rather, HES6 inhibits HES1 activity, thereby promoting transcription. HES1 and HES2 are expressed in a variety of adult and embryonic tissues. HES3 is expressed exclusively in cerebellar Purkinje cells, and HES5 is found solely in the nervous system. HES6 is produced in brain as well as in the limb buds of developing embryos.

Supplier: Bioss

P19ARF Capable of inducing cell cycle arrest in G1 and G2 phases. Acts as a tumor suppressor. Binds to MDM2 and blocks its nucleocytoplasmic shuttling by sequestering it in the nucleolus. This inhibits the oncogenic action of MDM2 by blocking MDM2-induced degradation of p53 and enhancing p53-dependent transactivation and apoptosis. Also induces G2 arrest and apoptosis in a p53-independent manner by preventing the activation of cyclin B1/CDC2 complexes. Binds to BCL6 and down-regulates BCL6-induced transcriptional repression. Binds to E2F1 and MYC and blocks their transcriptional activator activity but has no effect on MYC transcriptional repression. Binds to TOP1/TOPOI and stimulates its activity. This complex binds to rRNA gene promoters and may play a role in rRNA transcription and/or maturation. Interacts with NPM1/B23 and promotes its polyubiquitination and degradation, thus inhibiting rRNA processing. Interacts with UBE2I/UBC9 and enhances sumoylation of a number of its binding partners including MDM2 and E2F1. Binds to HUWE1 and represses its ubiquitin ligase activity. May play a role in controlling cell proliferation and apoptosis during mammary gland development.

Supplier: Biotium

Near-infrared CF™ dye antibodies are affinity-purified antibodies labeled with near-infrared fluorescent CF™750 or CF™770, two members of the novel CF™ dye series developed by Biotium for labeling proteins and other biomolecules. CF™ dyes are designed to offer advantages in brightness, photostability, and/or specificity compared to other commercial dyes, and are available in colors spanning the visible, far-red, and near-infrared spectra.

Supplier: Bioss

The mitotic checkpoint ensures that chromosomes are divided equally between daughter cells and is a primary mechanism preventing the chromosome instability often seen in aneuploid human tumors. This gene encodes a protein that is one of many involved in mechanisms to ensure proper chromosome segregation during cell division. The encoded protein binds to centromeres during the prophase, metaphase, and early anaphase cell division stages and to kinetochore microtubules during metaphase. It is part of the MIS12 complex, which may be fundamental for kinetochore formation and proper chromosome segregation during mitosis. In mitotic human cells ZW10 resides in a complex with Rod and Zwilch, whereas another ZW10 partner, Zwint-1, is part of a separate complex of structural kinetochore components including Mis12 and Ndc80-Hec1. Zwint-1 is critical for recruiting ZW10 to unattached kinetochores. Depletion from human cells demonstrates that the ZW10 complex is essential for stable binding of a Mad1-Mad2 complex to unattached kinetochores. Thus, ZW10 functions as a linker between the core structural elements of the outer kinetochore and components that catalyze generation of the mitotic checkpoint-derived "stop anaphase" inhibitor.

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Microtubule-associated proteins (MAPs) regulate microtubule stability and play critical roles in neuronal development and in maintaining the balance between neuronal plasticity and rigidity. MAP-light chain 3 beta (MAP-LC3 Beta) and MAP-light chain 3 alpha (MAP-LC3 alpha) are subunits of both MAP1A and MAP1B. MAP-LC3M Beta, a homolog of Apg8p, is essential for autophagy and associated to the autophagosome membranes after processing. Two forms of LC3 Beta, the cytosolic LC3-I and the membrane-bound LC3-II, are produced post-translationally. LC3-I is formed by the removal of the C-terminal 22 amino acids from newly synthesized LC3∫, followed by the conversion of a fraction of LC3-I into LC3-II. LC3 enhances fibronectin mRNA translation in ductus arteriosus cells through association with 60S ribosomes and binding to an AU-rich element in the 3’ untranslated region of fibronectin mRNA. This facilitates sorting of fibronectin mRNA onto rough endoplasmic reticulum and translation. MAP LC3 Beta may also be involved in formation of autophagosomal vacuoles. It is expressed primarily in heart, testis, brain and skeletal muscle.

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The Notch signaling pathway controls cellular interactions important for the specification of a variety of fates in both invertebrates and vertebrates. Key players in the Notch pathway are the TLE genes (for transducin-like enhancer of split, also designated ESG for enhancer of split groucho), which are human homologs of the Drosophila groucho gene. Groucho is a transcriptional repressor that plays a key role in neurogenesis, segmentation and sex determination. TLEs associate with chromatin in live cells and specifically with Histone H3, but not with other core histones. Expression of the TLE genes, TLE1, TLE2, TLE3 and TLE4, correlate with immature epithelial cells that are progressing toward a terminally differentiated state, suggesting a role during epithelial differentiation. TLE1, TLE2 and TLE3 have elevated expression in cervical squamous metaplasias and carcinomas, while TLE4 is most highly expressed in the brain, particularly in the caudate nucleus. TLE1 and TLE4 contain SP and WD40 domains, through which TLE1 binds AML1 to inhibit AML1-induced transactivation of the CSF1 receptor. In early stages of cell differentiation, TLE1 is upregulated, and TLE2 and TLE4 are downregulated. In later stages, TLE2 and TLE4 are upregulated, and expression of TLE1 decreases.

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APOBEC proteins inhibit retroviruses by deaminating cytosine residues of viral RNA and DNA. The seven APOBEC3 genes or pseudogenes are found in a cluster thought to result from gene duplication on chromosome 22. Like APOBEC3G, APOBEC3F deaminates deoxycytosine to deoxyuracil in the minus strand of HIV-1 DNA, resulting in G to A hypermutation in the plus strand of DNA. Thus, APOBEC3G and APOBEC3F provide a mechanism for innate immunity to retroviruses, and are also likely contribute to sequence variation observed in many viruses. Viral infectivity factor (Vif) imparts APOBEC3G and APOBEC3F resistance to HIV through impaired translation of their mRNA and accelerated posttranslational degradation of the APOBEC3 proteins by the 26S proteasome. Interestingly, HIV-1 Vif cannot form a complex with APOBEC3G or APOBEC3F of mouse origin as it does with the human protein, and thus mouse APOBEC3G and APOBEC3F function as a potent inhibitors of wildtype HIV-1 replication, where human APOBEC3G and APOBEC3F are only able to inhibit Vif-deficient HIV-1 replication. This implies that induction of APOBEC3G and APOBEC3F activity or a method of blocking their interaction with Vif may provide a method for therapeutic intervention.

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Chk2 is a serine/threonine kinase involved in the control of cell cycle checkpoints, and may also participate in transduction of the DNA damage and replicational stress signals. Chk2 is the mammalian ortholog of the budding yeast Rad53 and fission yeast Cds1 checkpoint kinases. The amino-terminal domain of Chk2 contains a series of seven serine and threonine residues (Ser19, Thr26, Ser28, Ser33, Ser35, Ser50 and Thr68) followed by glutamine (SQ or TQ motif). These are known to be preferred sites for phosphorylation by ATM/ATR kinases. Indeed, after DNA damage by ionizing radiation (IR), UV irradiation or hydroxyurea treatment, Thr68 and other sites in this region become phosphorylated by ATM/ATR. The SQ/TQ cluster domain, therefore, seems to have a regulatory function. Phosphorylation at Thr68 is a prerequisite for the subsequent activation step, which is attributable to autophosphorylation of Chk2 on residues Thr383 and Thr387 in the activation loop of the kinase domain. Chk2 inhibits CDC25C phosphatase by phosphorylating it on Ser-216, preventing the entry into mitosis. This kinase may have a role in meiosis as well. Kinase activity is up regulated by autophosphorylation and the protein is rapidly phosphorylated in response to DNA damage and to replication block.

Supplier: Bioss

Dual specificity protein kinase which acts as an essential component of the MAP kinase signal transduction pathway. Essential component of the stress-activated protein kinase/c-Jun N-terminal kinase (SAP/JNK) signaling pathway. With MAP2K4/MKK4, is the one of the only known kinase to directly activate the stress-activated protein kinase/c-Jun N-terminal kinases MAPK8/JNK1, MAPK9/JNK2 and MAPK10/JNK3. MAP2K4/MKK4 and MAP2K7/MKK7 both activate the JNKs by phosphorylation, but they differ in their preference for the phosphorylation site in the Thr-Pro-Tyr motif. MAP2K4/MKK4 shows preference for phosphorylation of the Tyr residue and MAP2K7/MKK7 for the Thr residue. The monophosphorylation of JNKs on the Thr residue is sufficient to increase JNK activity indicating that MAP2K7/MKK7 is important to trigger JNK activity, while the additional phosphorylation of the Tyr residue by MAP2K4/MKK4 ensures optimal JNK activation. Has a specific role in JNK signal transduction pathway activated by proinflammatory cytokines. The MKK/JNK signaling pathway is also involved in mitochondrial death signaling pathway, including the release cytochrome c, leading to apoptosis.

Supplier: Bioss

JNK1(MAPK8) is a member of the MAP kinase family. MAP kinases act as an integration point for multiple biochemical signals, and are involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation and development. This kinase is activated by various cell stimuli, and targets specific transcription factors, and thus mediates immediate-early gene expression in response to cell stimuli. The activation of this kinase by tumor-necrosis factor alpha (TNF-alpha) is found to be required for TNF-alpha induced apoptosis. This kinase is also involved in UV radiation induced apoptosis, which is thought to be related to cytochrome c-mediated cell death pathway. Studies of the mouse counterpart of this gene suggested that this kinase play a key role in T cell proliferation, apoptosis and differentiation. Four alternatively spliced transcript variants encoding distinct isoforms have been reported.JNK1 is activated by threonine and tyrosine phosphorylation by either of two dual specificity kinases, MAP2K4 and MAP2K7. The JNK pathway is critically involved in diabetes and levels are abnormally elevated in obesity. The cell-permeable JNK inhibitory peptide may have promise as a therapeutic agent for diabetes.