41259 Results for: "Butyraldehyde+dibutyl+acetal&pageNo=67"

Supplier: Bioss

Representing about 2% of human DNA, chromosome 20 consists of approximately 63 million bases and 600 genes. Chromosome 20 contains a region with numerous genes expressed in the epididymis, which are thought important for seminal production, and some viewed as potential targets for male contraception. The PRNP gene encoding the prion protein associated with spongiform encephalopathies, like Creutzfeldt-Jakob disease, is found on chromosome 20. Amyotrophic lateral sclerosis, spinal muscular atrophy, ring chromosome 20 epilepsy syndrome and Alagille syndrome are also associated with chromosome 20. The C20orf112 gene product has been provisionally designated C20orf112 pending further characterization.

Supplier: Bioss

Tissue specificity: Liver, skeletal and heart muscle, mammary cells. Very low levels in brain, lung, placenta and kidney. Strongly overexpressed in many pancreas and colorectal cancers. Increased gene copy numbers are detected in 3 of 12 tumor cell lines and 2 of 12 primary pancreatic carcinomas. Overexpresseed in 80% of colorectal cancers.

Supplier: Bioss

CCDC146

Supplier: Bioss

Induces cardiac myocyte hypertrophy in vitro. Binds to and activates the ILST/gp13 receptor.

Supplier: Bioss

The DnaJ family is one of the largest of all the chaperone families and has evolved with diverse cellular localization and functions. The presence of the J domain defines a protein as a member of the DnaJ family. DnaJ heat shock induced proteins are from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. The DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. The proteins contain cysteine rich regions that are composed of zinc fingers that form a peptide binding domain responsible for the chaperone function. DnaJ proteins are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB2 (DnaJ homolog subfamily B member 2), also known as HSJ1 or HSPF3, is expressed almost exclusively in the brain, with the highest levels in the frontal cortex and hippocampus. Two isoforms are produced due to alternative splicing.

Supplier: Bioss

HSPC300 (hematopoietic stem cell protein 300) is also known as probable protein BRICK1 or C3orf10 (chromosome 3 open reading frame 10) and is a 75 amino acid protein that is expressed as two isoforms and localizes to both the cytoplasm and the cytoskeleton. HSPC300 is thought to regulate cytoskeletal organization and Actin polymerization. Free HSPC300 exists as homotrimers prior to its incorporation into the WAVE complex. The WAVE complex includes five proteins, one of which is HSPC300, that regulate the ARC (Arp2/3 complex) which is responsible for Actin nucleation and is Rac 1-dependent. Because HSPC300 is a highly conserved subunit of the WAVE complex across many species, it is thought to have the same or similar functions in many different organisms. In Drosophila, the WAVE/ARC pathway may affect the development of the nervous system. HSPC300 is thought to localize to axons of the central nervous system of Drosophila embryos and thus may also be involved in axonogenesis. In addition, HSPC300 is thought to be necessary for synaptic morphogenesis by motoneurons. In mice, the knockout of the WAVE complex leads to learning and memory defects, and it is therefore hypothesized that HSPC300 may also be involved in cognitive functions. Genetic depletion of HSPC300 results in cytoskeletal abnormalities and prevents cytokinesis of cells, suggesting that decreased levels of HSPC300 may be associated with tumor suppression.

Supplier: Bioss

Phocein is a 225 amino acid protein encoded by the human gene MOBKL3. Phocein belongs to the MOB1/phocein family and is phosphorylated on serine residues. Phocein is a widely expressed, highly conserved intracellular protein. The sequence of Phocein has limited homology to the sigma subunits from Clathrin adaptor complexes and contains an additional stretch bearing a putative SH3-binding domain. Phocein is usually associated with membranes but can be present in the cytosol, where it behaves as a protein complex. Phocein is the major partner of the striatin family members, which are scaffolding proteins involved in signaling and trafficking. Due to its association with Dynamin via direct interactions with nucleotide diphosphate kinase (NDPK) and Eps15, Phocein has been implicated in vesicular trafficking, acting in particular in the endocytic process.

Supplier: Bioss

The synaptogyrin family of proteins are integral membrane proteins containing four transmembrane regions. Synaptogyrins are tyrosine-phosphorylated proteins with two neuronal (Synaptogyrin-1 and -3) and one ubiquitous (Synaptogyrin-2) isoform. Synaptophysin and synaptogyrin represent the major constituents of synaptic vesicles. Synaptogyrin-1 is associated with presynaptic vesicles in neuronal cells. Synaptogyrin-2, also known as cellugyrin, has a tyrosine phosphorylated C-terminal cytoplasmic tail and is involved in the regulation of membrane traffic in non-neuronal cells. Synaptogyrin-3 is expressed mainly in brain and placenta.

Supplier: Bioss

Chromosome 7 has been linked to Osteogenesis imperfecta, Pendred syndrome, Lissencephaly, Citrullinemia and Shwachman-Diamond syndrome. The deletion of a portion of the q arm of chromosome 7 is associated with Williams-Beuren syndrome, a condition characterised by mild mental retardation, an unusual comfort and friendliness with strangers and an elfin appearance. Deletions of portions of the q arm of chromosome 7 are also seen in a number of myeloid disorders including cases of acute myelogenous leukemia and myelodysplasia. The C7orf25 gene product has been provisionally designated C7orf25 pending further characterisation.

Supplier: Bioss

Troponin T is the tropomyosin-binding subunit of troponin, the thin filament regulatory complex which confers calcium-sensitivity to striated muscle actomyosin ATPase activity.

Supplier: Bioss

This gene encodes a highly glycosylated transmembrane protein with a high content of threonine and serine residues in its extracellular domain, similar to a broadly defined category of proteins termed mucins. Exposure of some cell types to anti PORIMIN (pro oncosis receptor inducing membrane injury) antibody, crosslinks this protein on the cell surface and induces a type of cell death termed oncosis. Oncosis is distinct from apoptosis and is characterized by a loss of cell membrane integrity without DNA fragmentation. This gene product is proposed to function as a cell surface receptor that mediates cell death.

Supplier: Bioss

Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes. Also involved in the deacetylation of cohesin complex protein SMC3 regulating release of cohesin complexes from chromatin. May play a role in smooth muscle cell contractility.

Supplier: Bioss

Emx1 and Emx2 are human homologs to the Drosophila developmental genes empty spiracles expressed in anterior body regions during early Drosophila embryogenesis. Emx1 and Emx2 are homeobox proteins expressed in the developing vertebrate brain. Emx2 is expressed in the dorsal telencephalon and small diencephalic regions, while Emx1 expression is exclusively confined to pyramidal neurons of the dorsal telencephalon. In the embryonic brain, Emx1 is expressed in both proliferating and differentiating neurons while Emx2 is expressed only in proliferating neurons. OTX1 and OTX2 are human homologs of the Drosophila developmental genes orthodenticle. In development, the sequence of expression begins with OTX2 at day ten post coitum followed by OTX1, Emx2 and finally Emx1. The genes encoding human Emx1 and Emx2 map to chromosomes 2p13.2 and 10q26.11, respectively.

Supplier: Bioss

Making up nearly 6% of the human genome, chromosome 6 contains around 1,200 genes within 170 million base pairs of sequence. Deletion of a portion of the q arm of chromosome 6 is associated with early onset intestinal cancer suggesting the presence of a cancer susceptibility locus. Porphyria cutanea tarda is associated with chromosome 6 through the HFE gene which, when mutated, predisposes an individual to developing this porphyria. Notably, the PARK2 gene, which is associated with Parkinson's disease, and the genes encoding the major histocompatiblity complex proteins, which are key molecular components of the immune system and determine predisposition to rheumatic diseases, are also located on chromosome 6. Stickler syndrome, 21-hydroxylase deficiency and maple syrup urine disease are also associated with genes on chromosome 6. A bipolar disorder susceptibility locus has been identified on the q arm of chromosome 6. The C6orf174 gene product has been provisionally designated C6orf174 pending further characterization.

Supplier: Bioss

Defects in NOD2 are the cause of sarcoidosis early-onset (EOS) . EOS is a form of sarcoidosis manifesting in children younger than 4 years of age. Sarcoidosis is an idiopathic, systemic, inflammatory disease characterized by the formation of immune granulomas in involved organs. Granulomas predominantly invade the lungs and the lymphatic system, but also skin, liver, spleen, eyes and other organs may be involved. Early-onset sarcoidosis is quite rare and has a distinct triad of skin, joint and eye disorders, without apparent pulmonary involvement. Compared with an asymptomatic and sometimes naturally disappearing course of the disease in older children, early-onset sarcoidosis is progressive and in many cases causes severe complications, such as blindness, joint destruction and visceral involvement.

Supplier: Bioss

GTPase activator for the Rho-type GTPases by converting them to an inactive GDP-bound state.

Supplier: Bioss

This gene is a member of the UBA domain family, whose members include proteins having connections to ubiquitin and the ubiquitination pathway. The ubiquitin associated domain is thought to be a non-covalent ubiquitin binding domain consisting of a compact three helix bundle. This particular protein originates from a gene locus in a refined region on chromosome 9 undergoing loss of heterozygosity in nasopharyngeal carcinoma (NPC). Taking into account its cytogenetic location, this UBA domain family member is being studied as a putative target for mutation in nasopharyngeal carcinomas. Multiple alternatively spliced transcript variants encoding different isoforms have been found for this gene.

Supplier: Bioss

ZNRF4 contains 1 PA (protease associated) domain and 1 RING-type zinc finger.

Supplier: Bioss

Members of the class-III pyridoxal-phosphate-dependent aminotransferase family, such as AGXT2, catalyze the conversion of glyoxylate to glycine using L-alanine as the amino donor. AGXT2 protects from asymmetric dimethylarginine (ADMA)-induced inhibition in nitric oxide (NO) production. Elevated blood concentrations of ADMA, a methyl derivate of the amino acid arginine and an endogenous inhibitor of nitric oxide (NO) synthase, is produced by the physiological degradation of methylated proteins and is found in association with diabetes, hypertension, congestive heart failure and atherosclerosis. AGXT2L2 (alanine-glyoxylate aminotransferase 2-like 2) is a 450 amino acid pyridoxal phosphate that exists as a homotetramer. Belonging to the class-III pyridoxal-phosphate-dependent aminotransferase family, AGXT2L2 localizes to the mitochondria and exists as three alternatively spliced isoforms. Encoded by a gene located on human chromosome 5q35.3, AGXT2L2 may have similar functions as AGXT2.

Supplier: Bioss

Mediates the uptake of glutamate into synaptic vesicles at presynaptic nerve terminals of excitatory neural cells. May also mediate the transport of inorganic phosphate.

Supplier: Bioss

The endophilins comprise a family of three SH3 domain-containing proteins designated Endophilin I, II and III, or alternatively known as SH3P4, SH3P8 and SH3P13, respectively. These proteins associate with Amphiphysin, Synaptojanin and Dynamin and are implicated in presynaptic vesicle trafficking at nerve terminals. The expression patterns of the endophilins are consistent with their cellular functions at the neuronal synapse, as Endophilin I is ex- pressed only in the brain. Both Endophilin II and Endophilin III are detected in a variety of tissues. Endophilin I is also implicated in modulating G protein-coupled receptor signaling by functioning as an adapter protein and directing 1 adrenergic receptors to the endocytic machinery.

Supplier: Bioss

FRAT1 and FRAT2 were originally characterized as proteins frequently rearranged in advanced T cell lymphoma, and they have since been identified as proto-oncogenes involved in tumorigenesis. These proteins share significant homology with the Xenopus glycogen synthase kinase-3 (xGSK-3) binding protein, which is designated GBP and is essential for the formation of the dorsal-ventral axis during embryonic development. Establishment of these embryonic axes is mediated by the Wnt intracellular signaling pathway. Wnt signaling is regulated in part by the activity of GSK-3, which phosphorylates and thereby facilitates the degradation of ?catenin. GBP binds to GSK-3 and inhibits this phosphorylation, resulting in the accumulation of ?catenin and the subsequent transcription of Wnt target genes. Like GBP, FRAT2 has been shown to bind xGSK-3, suggesting that FRAT1 and FRAT2 may be GSK-3 regulatory proteins.

Supplier: Bioss

May be involved in regulating transcriptional activation of cardiac genes during the aging process. May play a role in biosynthesis and/or processing of SLC2A4 in adipose cells.

Supplier: Bioss

MOZ (monocytic leukemia zinc finger protein) is a chromatin-associated histone acetyltransferase (HAT) that regulates chromatin remodeling and transcription. The MOZ gene was initially isolated as a consequence of two variant translocations that were identified in a distinct subtype of acute myeloid leukemias and resulted in the formation of MOZ fusion proteins. These fusions involve the HAT domain of MOZ with the activation domain of either transcriptional coactivator protein TIF2/GRIP1 or CBP, and lead to enhanced transcriptional activation by a mechanism involving aberrant histone acetylation. Additional MOZ related proteins, including MORF (MOZ related factor) and TIP60 (TAT interacting proteins 60), share significant similarities with MOZ including the putuative HAT domain. MORF also contains a strong transcriptional repression domain at its N terminus and a highly potent activation domain at the C terminus, suggesting that MORF has both HAT activity and contributes to the regulation of transcriptional activation. TIP60 was originally identified as a coactivator for the HIV TAT protein and also functions as a nuclear hormone receptor coactivator that enhances ligand dependent steroid receptor-mediated transactivation involving the androgen, estrogen and progesterone receptors.

Supplier: Bioss

In the process of endocytosis, essential rate-limiting regulator of a fast recycling pathway back to the plasma membrane. During cytokinesis, required for the postfurrowing terminal steps, namely for intercellular bridge stability and abscission, possibly by controlling phosphatidylinositol 4,5-bis phosphate (PIP2) and SEPT2 localization at the intercellular bridge.

Supplier: Bioss

Non-receptor tyrosine-protein kinase that plays an essential role in the selection and maturation of developing T-cells in the thymus and in the function of mature T-cells. Plays a key role in T-cell antigen receptor (TCR)-linked signal transduction pathways. Constitutively associated with the cytoplasmic portions of the CD4 and CD8 surface receptors. Association of the TCR with a peptide antigen-bound MHC complex facilitates the interaction of CD4 and CD8 with MHC class II and class I molecules, respectively, thereby recruiting the associated LCK protein to the vicinity of the TCR/CD3 complex. LCK then phosphorylates tyrosines residues within the immunoreceptor tyrosine-based activation motifs (ITAM) of the cytoplasmic tails of the TCR-gamma chains and CD3 subunits, initiating the TCR/CD3 signaling pathway. Once stimulated, the TCR recruits the tyrosine kinase ZAP7, that becomes phosphorylated and activated by LCK. Following this, a large number of signaling molecules are recruited, ultimately leading to lymphokine production. LCK also contributes to signaling by other receptor molecules. Associates directly with the cytoplasmic tail of CD2, which leads to hyperphosphorylation and activation of LCK. Also plays a role in the IL2 receptor-linked signaling pathway that controls the T-cell proliferative response. Binding of IL2 to its receptor results in increased activity of LCK. Is expressed at all stages of thymocyte development and is required for the regulation of maturation events that are governed by both pre-TCR and mature alpha beta TCR. Phosphorylates other substrates including RUNX3, PTK2B/PYK2, the microtubule-associated protein MAPT, RHOH or TYROBP.

Supplier: Bioss

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

This gene is a member of the Period family of genes and is expressed in a circadian pattern in the suprachiasmatic nucleus, the primary circadian pacemaker in the mammalian brain. Genes in this family encode components of the circadian rhythms of locomotor activity, metabolism, and behavior. This gene is upregulated by CLOCK/ARNTL heterodimers but then represses this upregulation in a feedback loop using PER/CRY heterodimers to interact with CLOCK/ARNTL. Polymorphisms in this gene may increase the risk of getting certain cancers and have been linked to sleep disorders. [provided by RefSeq, Jan 2014]

Supplier: Bioss

Zinc-finger proteins bind nucleic acids and play important roles in various cellular functions, including cell proliferation, differentiation, and apoptosis. This protein and Grb10-interacting GYF protein 2 have been identified as a components of the mammalian 4EHP (m4EHP) complex. The complex is thought to function as a translation repressor in embryonic development. [provided by RefSeq, Oct 2012].

Supplier: Bioss

Involved in global genome nucleotide excision repair (GG-NER) by acting as damage sensing and DNA-binding factor component of the XPC complex. Has only a low DNA repair activity by itself which is stimulated by RAD23B and RAD23A. Has a preference to bind DNA containing a short single-stranded segment but not to damaged oligonucleotides. This feature is proposed to be related to a dynamic sensor function: XPC can rapidly screen duplex DNA for non-hydrogen-bonded bases by forming a transient nucleoprotein intermediate complex which matures into a stable recognition complex through an intrinsic single-stranded DNA-binding activity. The XPC complex is proposed to represent the first factor bound at the sites of DNA damage and together with other core recognition factors, XPA, RPA and the TFIIH complex, is part of the pre-incision (or initial recognition) complex. The XPC complex recognizes a wide spectrum of damaged DNA characterized by distortions of the DNA helix such as single-stranded loops, mismatched bubbles or single-stranded overhangs. The orientation of XPC complex binding appears to be crucial for inducing a productive NER. XPC complex is proposed to recognize and to interact with unpaired bases on the undamaged DNA strand which is followed by recruitment of the TFIIH complex and subsequent scanning for lesions in the opposite strand in a 5'-to-3' direction by the NER machinery. Cyclobutane pyrimidine dimers (CPDs) which are formed upon UV-induced DNA damage esacpe detection by the XPC complex due to a low degree of structural perurbation. Instead they are detected by the UV-DDB complex which in turn recruits and cooperates with the XPC complex in the respective DNA repair. In vitro, the XPC:RAD23B dimer is sufficient to initiate NER; it preferentially binds to cisplatin and UV-damaged double-stranded DNA and also binds to a variety of chemically and structurally diverse DNA adducts.