54781 Results for: "Carbenicillin+disodium+salt&pageNo=48"

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Voltage-gated K+ channels in the plasma membrane control the repolarization and the frequency of action potentials in neurons, muscles, and other excitable cells. The KV gene family encodes more than 30 genes that comprise the subunits of the K+ channels, and they vary in their gating and permeation properties, subcellular distribution, and expression patterns. Functional KV channels assemble as tetramers consisting of pore-forming alpha-subunits (KV alpha), which include the KV1, KV2, KV3, and KV4 proteins, and accessory or KV beta subunits that modify the gating properties of the coexpressed KV alpha subunits. Differences exist in the patterns of trafficking, biosynthetic processing and surface expression of the major KV1 subunits (KV1.1, KV1.2, KV1.4, KV1.5 and KV1.6) expressed in rat and human brain, suggesting that the individual protein subunits are highly regulated to control for the assembly and formation of functional neuronal channels.

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Tyrosine protein phosphatase which functions as a dosage-dependent inducer of mitotic progression. Directly dephosphorylates CDK1 and stimulates its kinase activity. Also dephosphorylates CDK2 in complex with cyclin E, in vitro.

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GCF (GC-rich sequence DNA-binding factor), also known as C2orf3 (chromosome 2 open reading frame 3), transcription factor 9 (TCF-9) or DNABF, is a 781 amino acid nuclear protein that belongs to the GCF family. Widely expressed, GCF binds the GC-rich sequences of _-Actin, EGFR and calcium-dependent protease (CANP) promoters. GCF contains multiple phosphoserine and phosphothreonine residues, and two GCF isoforms are produced due to alternative splicing events. GCF is considered a candidate for susceptibility to dyslexia (DYX3) as both genes reside in close proximity on human chromosome 2. Chromosome 2 is the second largest human chromosome and consists of 237 million bases, encodes over 1,400 genes and makes up approximately 8% of the human genome.

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The isthmic organizer signals at the mid/hindbrain boundary (MHB) regulate the development and differentiation of the vertebrate caudal midbrain and the anterior hindbrain. The MHB forms at the boundary of expression between homeobox genes Gbx2 and Otx2. Gbx2 and Otx2 play distinct, essential roles in MHB positioning and development. During development, the GBX2 gene is expressed in the anterior hindbrain. Specifically, Gbx2 negatively regulates Otx2 expression along the anterior-posterior axis; Gbx2(-) mutants demonstrate an expanded Otx2 domain. During development, the GBX2 gene is expressed in the anterior hindbrain. Gbx2 is expressed in the adult brain, spleen and female genital tract. The GBX2 gene is over-expressed in human prostate cancer cell lines (TSU-prl, PC3, DU145 and LNCaP). Furthermore, downregulation of Gbx2 expression restricts tumorigenicity in human prostate cancer cell lines, which suggests that Gbx2 expression may be required for growth of malignant prostate cells.

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spindle microtubules. The checkpoint works by inhibiting the activity of the anaphase promoting complex, thereby preventing the degradation of several cell cycle regulators. Like other spindle checkpoint mutants, MAD1 loss-of-function mutants are sensitive to benomyl and cannot delay cell division in response to spindle depolymerization. Mad1p becomes hyperphosphorylated upon spindle depolymerization.

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BEGAIN is a 593 amino acid protein that localizes to cytoplasm and membrane. BEGAIN interacts with PSD-95 and SAPAP1 and forms a ternary complex and may sustain the structure of the postsynaptic density (PSD). BEGAIN is a novel PSD component associated with the core complex of PSD-95 and SAPAP. Because BEGAIN and SAPAP interact with the same region of PSD-95, BEGAIN and SAPAP may compete for the binding to PSD-95 and cannot interact with PSD-95 simultaneously. The C-terminal region of BEGAIN is involved in the interaction with PSD-95 whereas the N-terminal region has a coiled-coil structure that may interact with other molecules. BEGAIN is specifically expressed in brain and enriched in the PSD fraction. BEGAIN is also expressed in neurons and enriched at synaptic junctions, and is likely involved in the organization of synaptic junction components.

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KNDC1 is a 1,749 amino acid protein that contains two KIND domains and an N-terminal Ras-GEF domain. Expressed in the cerebral cortex, KNDC1 is a likely guanine nucleotide exchange factor (GEF). Existing as six alternatively spliced isoforms, the gene encoding KNDC1 maps to human chromosome 10q26.3 and mouse chromosome 7 F4. Spanning nearly 135 million base pairs, chromosome 10 makes up approximately 4.5% of total DNA in cells and encodes nearly 1,200 genes. 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 some of the 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.

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Acts as a tumor suppressor in many tumor types; induces growth arrest or apoptosis depending on the physiological circumstances and cell type. Involved in cell cycle regulation as a trans-activator that acts to negatively regulate cell division by controlling a set of genes required for this process. One of the activated genes is an inhibitor of cyclin-dependent kinases. Apoptosis induction seems to be mediated either by stimulation of BAX and FAS antigen expression, or by repression of Bcl-2 expression. In cooperation with mitochondrial PPIF is involved in activating oxidative stress-induced necrosis; the function is largely independent of transcription. Induces the transcription of long intergenic non-coding RNA p21 (lincRNA-p21) and lincRNA-Mkln1. LincRNA-p21 participates in TP53-dependent transcriptional repression leading to apoptosis and seem to have to effect on cell-cycle regulation. Implicated in Notch signaling cross-over. Prevents CDK7 kinase activity when associated to CAK complex in response to DNA damage, thus stopping cell cycle progression. Isoform 2 enhances the transactivation activity of isoform 1 from some but not all TP53-inducible promoters. Isoform 4 suppresses transactivation activity and impairs growth suppression mediated by isoform 1. Isoform 7 inhibits isoform 1-mediated apoptosis.

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ACLP2 (acid phosphatase-like 2), also known as UNQ370 or PRO706, is a 480 amino acid secreted protein that functions to catalyze the H2O-dependent conversion of a phosphate monoester to an alcohol and a phosphate. Expressed as two alternatively spliced isoforms, ACPL2 is encoded by a gene that maps to chromosome 3, which houses over 1,100 genes, including a chemokine receptor (CKR) gene cluster and a variety of human cancer-related gene loci. Key tumor suppressing genes on chromosome 3 include those that encode the apoptosis mediator RASSF1, the cell migration regulator HYAL1 and the angiogenesis suppressor SEMA3B. Marfan Syndrome, porphyria, von Hippel-Lindau syndrome, osteogenesis imperfecta and Charcot-Marie-Tooth Disease are a few of the numerous genetic diseases associated with chromosome 3.

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Junctophilins are components of the junctional complexes between plasma membranes and endoplasmic or sarcoplasmic reticulums present in all excitable cells. Junctophilins contain a cytoplasmic domain which binds to the plasma membrane, as well as an ER/SR membrane spanning hydrophobic C-terminal segment. The three subtypes in this family are Junctophilin-1, -2 and -3. Junctophilin-1 is predominantly expressed in skeletal muscle, but is also expressed at low levels in heart. Junctophilin-2 is expressed in heart and skeletal muscle. Mutant mice lacking the Jph2 gene exhibit embryonic lethality and possess cardiac myocytes that express abnormal calcium transients. Junctophilin-3 is expressed in brain. The JPH3 alternatively spliced exon 2A has been suggested as a site for CTG repeat expansion leading to a Huntington disease-like autosomal dominant disorder.

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This gene encodes a tumor suppressor protein containing transcriptional activation, DNA binding, and oligomerization domains. The encoded protein responds to diverse cellular stresses to regulate expression of target genes, thereby inducing cell cycle arrest, apoptosis, senescence, DNA repair, or changes in metabolism. Mutations in this gene are associated with a variety of human cancers, including hereditary cancers such as Li-Fraumeni syndrome. Alternative splicing of this gene and the use of alternate promoters result in multiple transcript variants and isoforms. Additional isoforms have also been shown to result from the use of alternate translation initiation codons (PMIDs: 12032546, 20937277). [provided by RefSeq, Feb 2013].

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This gene encodes a ubiquitous nuclear protein that stimulates both cell proliferation and differentiation. It is a member of the MADS (MCM1, Agamous, Deficiens, and SRF) box superfamily of transcription factors. This protein binds to the serum response element (SRE) in the promoter region of target genes. This protein regulates the activity of many immediate-early genes, for example c-fos, and thereby participates in cell cycle regulation, apoptosis, cell growth, and cell differentiation. This gene is the downstream target of many pathways; for example, the mitogen-activated protein kinase pathway (MAPK) that acts through the ternary complex factors (TCFs). [provided by RefSeq, Jul 2008].

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HEMK2 is a 214 amino acid protein that belongs to the methyltransferase superfamily and exists as multiple alternatively spliced isoforms. The gene encoding HEMK2 maps to human chromosome 21, which houses approximately 300 genes and comprises nearly 1,5% of the human genome. Chromosome 21-associated disorders include Alzheimer's disease, amyotrophic lateral sclerosis and, most notably, Down syndrome (also known as trisomy 21).

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Cell adhesion molecules influence cell growth, differentiation, embryogenesis, immune response and cancer metastasis by networking information from the extracellular matrix to the cell. Sidekick-1 (SDK1) is a 2,213 amino acid single-pass membrane protein that functions as a cell adhesion molecule by guiding axonal terminals to specific synapses in developing neurons. Existing as three alternatively spliced isoforms, Sidekick-1 is expressed in retinal neurons and contains thirteen fibronectin type-III domains and six Ig-like C2-type (immunoglobulin-like) domains. Sidekick-1 expression is upregulated in glomeruli of patients with HIV-associated nephropathy, where it leads to podocyte dysfunction. The gene encoding Sidekick-1 maps to human chromosome 7p22.2 and murine chromosome 5 G2.

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The exosome is a multisubunit complex composed of several highly conserved subunits, some of which are 3’ to 5’ exoribonucleases. The complex is involved in a variety of cellular processes and is responsible for degrading unstable mRNAs that contain AU-rich (ARE) elements in their untranslated 3’ region. DIS3L2 (DIS3-like exonuclease 2) is an 885 amino acid protein that is thought to function as an exonuclease and may be required for the 3’ processing of pre-mRNA into mature mRNA. Defects or chromosomal translocations involving the gene encoding DIS3L2 may be associated with Marfanoid habitus, a genetic disorder characterized by abnormalities in the skeleton, eyes and cardiovascular system. DIS3L2 is expressed as five isoforms due to alternative splicing events.

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This gene is a member of the Tyr protein kinase family and the epidermal growth factor receptor subfamily. It encodes a single-pass type I membrane protein with multiple cysteine rich domains, a transmembrane domain, a tyrosine kinase domain, a phosphotidylinositol-3 kinase binding site and a PDZ domain binding motif. The protein binds to and is activated by neuregulins and other factors and induces a variety of cellular responses including mitogenesis and differentiation. Multiple proteolytic events allow for the release of a cytoplasmic fragment and an extracellular fragment. Mutations in this gene have been associated with cancer. Alternatively spliced variants which encode different protein isoforms have been described; however, not all variants have been fully characterized. [provided by RefSeq, Jul 2008].

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This gene expresses a paternally imprinted antisense transcript of the insulin-like growth factor 2 gene. The transcript is overexpressed in Wilms' tumor. This gene is predicted to be non-coding because the predicted protein is not conserved in any other species and the majority of transcripts would be candidates for non-sense mediated decay (NMD) if a protein were expressed. Alternative splicing results in multiple transcript variants.

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IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors.

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The bromodomain-containing proteins include BRD2, BRD3, BRD4 and BRDT. BRD2 (RING3 protein) is a mitogen-activated nuclear protein whose gene is located in the human MHC II region, suggesting its relation to HLA-associated diseases. The gene encoding BRD3 (RING3-like protein) contains two bromodomains and maps to chromosome 9q34. BRD4 (HUNK1 protein) is a nuclear protein involved in the regulation of chromosomal dynamics during mitosis. The testis-specific bromodomain protein BRDT contains a PEST sequence, indicating that it undergoes rapid intracellular degradation. The bromodomain-containing proteins are ubiquitously expressed.

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Catalase is the classical marker for peroxisomes and is the most abundant protein within peroxisomes. It is found in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide.

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PTOV1 belongs to the Mediator complex subunit 25 family, PTOV1 subfamily. It may activate transcription and is required for nuclear translocation of FLOT1. PTOV1 promotes cell proliferation. There are three named isoforms.

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Chromosome 1 is the largest human chromosome spanning about 260 million base pairs and making up 8% of the human genome. There are about 3,000 genes on chromosome 1, and considering the great number of genes there are also a large number of diseases associated with chromosome 1. Notably, the rare aging disease Hutchinson-Gilford progeria is associated with the LMNA gene which encodes lamin A. When defective, the LMNA gene product can build up in the nucleus and cause characteristic nuclear blebs. The mechanism of rapidly enhanced aging is unclear and is a topic of continuing exploration. The MUTYH gene is located on chromosome 1 and is partially responsible for familial adenomatous polyposis. Stickler syndrome, Parkinsons, Gaucher disease and Usher syndrome are also associated with chromosome 1. A breakpoint has been identified in 1q which disrupts the DISC1 gene and is linked to schizophrenia. Aberrations in chromosome 1 are found in a variety of cancers including head and neck cancer, malignant melanoma and multiple myeloma.

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Fibulin-1 and Fibulin-2 associate with Fibronectin and other extracellular matrix proteins. In bone marrow, Fibulin-1 and Fibulin-2 bind to Fibronectin in the adherent layer. Fibulin-1 expression is stimulated by estrogen in ovarian cancer cell lines and has been suggested as both an agent of metastasis in ovarian cancer cells and as an indicator for predicting cancer risk or aggressiveness in ovarian carcinomas. The mobility of cancer cells may be inhibited with increasing exposure to Fibulin-1. Fibulin-2 binds to the lectin domains of extracellular matrix proteins aggrecan, versican and brevican. Fibulin-2 is abundantly expressed in heart, placenta and ovarian tissue, where it localizes to basement membranes and connective tissue compartments. In mice, differential Fibulin-2 gene expression correlates with the early phase of diabetic kidneys and glomerulosclerosis. The gene encoding human Fibulin-2 maps to chromosome 3p25.1.

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Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal. Signal activation necessitate an association with IL6ST. Activation may lead to the regulation of the immune response, acute-phase reactions and hematopoiesis.

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G protein-coupled receptors (GPRs) are a protein family of transmembrane receptors that transmit an extracellular signal (ligand binding) into an intracellular signal (G protein activation). GPR signaling is an evolutionarily ancient mechanism used by all eukaryotes to sense environmental stimuli and mediate cell-cell communication. All of the receptors have seven membrane-spanning domains and the extracellular parts of the receptor can be glycosylated. These extracellular loops also contain two highly conserved cysteine residues which create disulfide bonds to stabilize the receptor structure. GPR103 is a 455-amino acid protein with highest expression in the brain, retina, trigeminal ganglion, hypothalamus and vestibular nucleus. In peripheral tissues, GPR103 is expressed only in the heart, kidney and testis. GPR103 may regulate adrenal function. A hypothalamic neuropeptide of the RFamide family (26RFa) acts as an endogenous ligand for GPR103.

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Binds the telomeric double-stranded 5'-TTAGGG-3' repeat and plays a central role in telomere maintenance and protection against end-to-end fusion of chromosomes. In addition to its telomeric DNA-binding role, required to recruit a number of factors and enzymes required for telomere protection, including the shelterin complex, TERF2IP/RAP1 and DCLRE1B/Apollo. Component of the shelterin complex (telosome) that is involved in the regulation of telomere length and protection. Shelterin associates with arrays of double-stranded 5'-TTAGGG-3' repeats added by telomerase and protects chromosome ends; without its protective activity, telomeres are no longer hidden from the DNA damage surveillance and chromosome ends are inappropriately processed by DNA repair pathways. Together with DCLRE1B/Apollo, plays a key role in telomeric loop (T loop) formation by generating 3' single-stranded overhang at the leading end telomeres: T loops have been proposed to protect chromosome ends from degradation and repair. Required both to recruit DCLRE1B/Apollo to telomeres and activate the exonuclease activity of DCLRE1B/Apollo. Preferentially binds to positive supercoiled DNA. Together with DCLRE1B/Apollo, required to control the amount of DNA topoisomerase (TOP1, TOP2A and TOP2B) needed for telomere replication during fork passage and prevent aberrant telomere topology. Recruits TERF2IP/RAP1 to telomeres, thereby participating in to repressing homology-directed repair (HDR), which can affect telomere length.

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This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B.

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Dipeptidyl peptidases (DPPs) mediate regulatory activity of their substrates and have been linked to a variety of diseases including type 2 diabetes, obesity and cancer. DPPs have post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. DPPs can bind specific voltage-gated potassium channels and alter their expression and biophysical properties and may also influence T cells. DPP proteins include DPRP1, DPRP2, DPP3, DPP7, DPP10, DPPX and CD26. DPP3 (dipeptidyl-peptidase 3), also known as DPPIII, is a zinc-exopeptidase that belongs to the peptidase M49 family. DPP3 localizes to the cytoplasm and is involved in intracellular protein catabolism. More specifically, DPP3 is an important enzyme involved in the degradation of enkephalins. An increase in the activity of DPP3 is implicated in ovarian and endometrial cancers.

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Orphan receptor. Displays a significant level of constitutive activity. Its effect is mediated by G(s)-alpha protein that stimulate adenylate cyclase, resulting in an elevation of intracellular cAMP.

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Glucose Oxidase is a dimeric enzyme that binds to β-D-glucose and aids in its oxidation into D-glucono-1,5-lactone which then hydrolyzes to gluconic acid. Flavin adenine dinucleotide (FAD) is a cofactor to Glucose Oxidase that acts as the initial electron acceptor and is required for this oxidation to occur. Glucose Oxidase is a natural preservative found in honey, where it reduces atmospheric oxygen into hydrogen peroxide which acts as an antibacterial barrier. Glucose Oxidase is also commonly used in biosensors in which it conveys levels of glucose by keeping track of the number of electrons passed through the enzyme. In this application, Glucose Oxidase is connected to an electrode and the resulting charge is measured.