127964 Results for: "Bioss"

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Heterotrimeric G protein-mediated signal transduction is a dynamically regulated process with the intensity of signal decreasing over time despite the continued presence of the agonist (1,2). G protein-coupled receptor kinases (GRKs) are activated by activated G protein-coupled receptors, and they function to phosphorylate and inactivate cell surface receptors in the heterotrimeric G protein signaling cascade (3,4). GIT1 (for GRK-interactor 1) and GIT2 are GTPase-activating proteins (GAP) for members of the ADP ribosylation factor (ARF) family of small GTP-binding proteins, which are involved in vesicular trafficking (5,6). GIT1 overexpression results in reduced internalization and resensitization of b2-adrenergic receptor, thus reducing b2-adrenergic receptor signaling (5).

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This gene encodes a transmembrane signaling polypeptide which contains an immunoreceptor tyrosine-based activation motif (ITAM) in its cytoplasmic domain. The encoded protein may associate with the killer-cell inhibitory receptor (KIR) family of membrane glycoproteins and may act as an activating signal transduction element. This protein may bind zeta-chain (TCR) associated protein kinase 70kDa (ZAP-70) and spleen tyrosine kinase (SYK) and play a role in signal transduction, bone modeling, brain myelination, and inflammation. Mutations within this gene have been associated with polycystic lipomembranous osteodysplasia with sclerosing leukoencephalopathy (PLOSL), also known as Nasu-Hakola disease. Its putative receptor, triggering receptor expressed on myeloid cells 2 (TREM2), also causes PLOSL. Multiple alternative transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq, Mar 2010]

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Steroid receptors are ligand-dependent, intracellular proteins that stimulate transcription of specific genes by binding to specific DNA sequences following activation by the appropriate hormone. Glucocorticoids are a family of steroids necessary for the regulation of energy metabolism and the immune and inflammatory responses. These compounds exert their effect through their interaction with the glucocoticoid receptor (GR) and that complex's subsequent association with DNA. All normal mammalian tissues examined to date have been shown to contain glucocorticoid receptor.

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ADRM1 is a 407 amino acid protein that localizes to both the nucleus and the cytoplasm and is thought to be involved in protein recruitment and cell adhesion. An integral membrane protein, ADRM1 functions to recruit UCH-L5, a deubiquitinating enzyme, to the 26S proteasome, and once at the proteasome it promotes the activity of UCH-L5. Additionally, ADRM1 is thought to mediate lymphocyte adhesion in endothelial cells and may thus play a role in lymphocyte homing. ADRM1 expression is induced by IFN-g in some cancer cell lines and its expression is upregulated in other metastatic cells, suggesting a role in carcinogenesis. Two isoforms of ADRM1 exist due to alternative splicing events.

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GLT25D1 is a 622 amino acid protein that localizes to the lumen of the endoplasmic reticulum. Ubiquitously expressed with higher levels in placenta, heart, lung and spleen, GLT25D1 is a member of the glycosyltransferase 25 family. The beta-galactosyltransferase activity of GLT25D1 allows the transfer of beta-galactose to hydroxylysine residues of collagen. GLT25D1 is considered an important target for investigating the biological significance of collagen glycosylation and the importance of posttranslational modification in the etiology of connective tissue disorders. The gene encoding GLT25D1 is located on human chromosome 19, which consists of over 63 million bases, houses approximately 1,400 genes and is recognized for having the greatest gene density of the human chromosomes.

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Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'-linked polyubiquitination. Mediates the selective degradation of short-lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and auto-ubiquitination of CHIP, TRAF6 and TRIM63/MURF1. Ubiquitinates CHIP-associated HSP90AB1 in vitro. Lacks inherent specificity for any particular lysine residue of ubiquitin. Essential for viral activation of IRF3. Mediates polyubiquitination of CYP3A4.

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The protein encoded by this gene is a member of the transmembrane 4 superfamily, also known as the tetraspanin family. Most of these members are cell-surface proteins that are characterized by the presence of four hydrophobic domains. The proteins mediate signal transduction events that play a role in the regulation of cell development, activation, growth and motility.

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Hexamethylene bis-acetamide inducible 1 (HEXIM1) and Hexamethylene bis-acetamide inducible 2 (HEXIM2) comprise a family of proteins which inhibit positive transcription elongation factor b (P-TEFb) through association with 7SK. P-TEFb is composed of a catalytic subunit, Cdk9, and either Cyclin T1 or T2 as a regulatory subunit. This complex regulates eukaryotic gene expression at the level of elongation. The C-terminal domains of HEXIM proteins interact directly with each other. Via these domains, HEXIM1 and HEXIM2 form stable homo- and hetero-oligomers, which may aid in the formation of the 7SK small nuclear ribonucleic acid particle. Despite their similar functions, HEXIM1 and HEXIM2 exhibit distinct expression patterns in various established cell lines and human tissues.

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Myt1 is a zinc finger protein that is known to interact with the co-repressor Sin3B and also HDAC1 and HDAC2. The Myt1 family, including Myt1 and Myt1L, exemplifies a class of neural sequence specific transcription factors that actively recruit HDACs to selected genes during CNS development.

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Mre11 is a component of the MRN complex, which plays a critical role in double-strand break repair (DSB), DNA recombination, maintenance of telomere integrity, and meiosis. Mre11 has both single-strand endonuclease and double strand-specific 3'-5' exonuclease activities. Rad50, another component of the MRN complex, is postulated to bind to DNA ends and hold them in close proximity, thus facilitating searches for regions of sequence homology, and also possibly stimulating the activity of DNA ligases and/or restricting Mre11 activity. Mutations in Mre11 may cause breast cancer.

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The protein encoded by this gene belongs to the family of P-type cation transport ATPases, and to the subfamily of Na+/K+-ATPases. Na+/K+ -ATPase is an integral membrane protein responsible for establishing and maintaining the electrochemical gradients of Na and K ions across the plasma membrane. These gradients are essential for osmoregulation, for sodium-coupled transport of a variety of organic and inorganic molecules, and for electrical excitability of nerve and muscle. This enzyme is composed of two subunits, a large catalytic subunit (alpha) and a smaller glycoprotein subunit (beta). The catalytic subunit of Na+/K+ -ATPase is encoded by multiple genes. This gene encodes an alpha 1 subunit. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, May2009].

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The Annexins are a family of structurally similar proteins. Annexins bind to phospholipids and may be involved in regulation of membrane transport, membrane channel activity, and interaction of the cell membrane with the extracellular matrix. Annexin A4 (ANXA4) belongs to the annexin family of calcium dependent phospholipid binding proteins. Although their functions are still not clearly defined, several members of the annexin family have been implicated in membrane related events along exocytotic and endocytotic pathways. ANXA4 has 45 to 59% identity with other members of its family and shares a similar size and exon intron organization. Isolated from human placenta, ANXA4 encodes a protein that has possible interactions with ATP, and has in vitro anticoagulant activity and also inhibits phospholipase A2 activity. ANXA4 is almost exclusively expressed in epithelial cells.

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The protein encoded by this gene is a regulatory protein involved in mitosis. The gene product complexes with p34(cdc2) to form the maturation-promoting factor (MPF). Two alternative transcripts have been found, a constitutively expressed transcript and a cell cycle-regulated transcript, that is expressed predominantly during G2/M phase. The different transcripts result from the use of alternate transcription initiation sites. [provided by RefSeq, Jul 2008].

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Postsynaptic density scaffolding protein. Binds and cross-links cytoplasmic regions of GRM1, GRM5, ITPR1, DNM3, RYR1, RYR2, SHANK1 and SHANK3. By physically linking GRM1 and GRM5 with ER-associated ITPR1 receptors, it aids the coupling of surface receptors to intracellular calcium release. May also couple GRM1 to PI3 kinase through its interaction with AGAP2. Isoforms can be differently regulated and may play an important role in maintaining the plasticity at glutamatergic synapses.

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Anti-FOXO4 Rabbit Polyclonal Antibody

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E3 ubiquitin-protein ligase accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. This protein inhibits TGF-beta signaling by triggering SMAD2 and TGFR1 ubiquitination and proteasome-dependent degradation. Furthermore, it promotes ubiquitination and internalization of various plasma membrane channels such as ENaC, Nav1.2, Nav1.3, Nav1.5, Nav1.7, Nav1.8, Kv1.3, EAAT1 or CLC5, and promotes the ubiquitination and degradation of SGK.

Supplier: Bioss

Acts downstream of various receptor and cytoplasmic protein tyrosine kinases to participate in the signal transduction from the cell surface to the nucleus. Dephosphorylates ROCK2 at Tyr-722 resulting in stimulatation of its RhoA binding activity.

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The steady state of protein tyrosyl phosphorylation in cells is regulated by the opposing action of tyrosine kinases and protein tyrosine phosphatases (PTPs). Several groups have independently identified a non transmembrane PTP, designated SHPTP1 (also known as PTP1C, HCP and SHP), which is primarily expressed in hematopoietic cells and characterized by the presence of two SH2 domains N terminal to the PTP domain. A second and much more widely expressed PTP with SH2 domains, SHPTP2 (also designated PTP1D and Syp), has been identified. SHP2 is a protein tyrosine phosphatase that is widely expressed and plays a regulatory role in various cell signaling events that are important for many cell functions, such as mitogenic activation, metabolic control, transcription regulation, and cell migration.

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The protein encoded by this gene is a guanine nucleotide exchange factor (GEF) similar to the Saccharomyces cerevisiae CDC25 gene product. Functional analysis has demonstrated that this protein stimulates the dissociation of GDP from RAS protein. The studies of the similar gene in mouse suggested that the Ras-GEF activity of this protein in brain can be activated by Ca2+ influx, muscarinic receptors, and G protein beta-gamma subunit. Mouse studies also indicated that the Ras-GEF signaling pathway mediated by this protein may be important for long-term memory. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Mar 2009]

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This gene encodes a member of the mitogen-activated protein kinase (MAPK) family. Members of this family 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. They form a three-tiered signaling module composed of MAPKKKs, MAPKKs, and MAPKs. This protein is phosphorylated at serine and threonine residues by MAPKKKs and subsequently phosphorylates downstream MAPK targets at threonine and tyrosine residues. A similar protein in mouse has been reported to play a role in liver organogenesis. A pseudogene of this gene is located on the long arm of chromosome X. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013]

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PCB (Pyruvate carboxylase) requires biotin and ATP to catalyse the carboxylation of pyruvate to oxaloacetate. The active enzyme is a homotetramer arranged in a tetrahedron which is located exclusively in the mitochondrial matrix. PCB is involved in gluconeogenesis, lipogenesis, insulin secretion and synthesis of the neurotransmitter glutamate. Mutations in this gene have been associated with pyruvate carboxylase deficiency. Alternatively spliced transcript variants with different 5' UTRs, but encoding the same protein, have been found for this gene.

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Serine/threonine kinase which acts as a master kinase, phosphorylating and activating a subgroup of the AGC family of protein kinases. Its targets include: protein kinase B (PKB/AKT1, PKB/AKT2, PKB/AKT3), p70 ribosomal protein S6 kinase (RPS6KB1), p90 ribosomal protein S6 kinase (RPS6KA1, RPS6KA2 and RPS6KA3), cyclic AMP-dependent protein kinase (PRKACA), protein kinase C (PRKCD and PRKCZ), serum and glucocorticoid-inducible kinase (SGK1, SGK2 and SGK3), p21-activated kinase-1 (PAK1), protein kinase PKN (PKN1 and PKN2). Plays a central role in the transduction of signals from insulin by providing the activating phosphorylation to PKB/AKT1, thus propagating the signal to downstream targets controlling cell proliferation and survival, as well as glucose and amino acid uptake and storage. Negatively regulates the TGF-beta-induced signaling by: modulating the association of SMAD3 and SMAD7 with TGF-beta receptor, phosphorylating SMAD2, SMAD3, SMAD4 and SMAD7, preventing the nuclear translocation of SMAD3 and SMAD4 and the translocation of SMAD7 from the nucleus to the cytoplasm in response to TGF-beta. Activates PPARG transcriptional activity and promotes adipocyte differentiation. Activates the NF-kappa-B pathway via phosphorylation of IKKB. The tyrosine phosphorylated form is crucial for the regulation of focal adhesions by angiotensin II. Controls proliferation, survival, and growth of developing pancreatic cells. Participates in the regulation of Ca(2+) entry and Ca(2+)-activated K(+) channels of mast cells. Essential for the motility of vascular endothelial cells (ECs) and is involved in the regulation of their chemotaxis. Plays a critical role in cardiac homeostasis by serving as a dual effector for cell survival and beta-adrenergic response. Plays an important role during thymocyte development by regulating the expression of key nutrient receptors on the surface of pre-T cells and mediating Notch-induced cell growth and proliferative responses.

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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 C20orf173 gene product has been provisionally designated C20orf173 pending further characterization.

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PGLS belongs to the glucosamine/galactosamine-6-phosphate isomerase family, 6-phosphogluconolactonase subfamily. It is implicated in the hydrolysis of 6-phosphogluconolactone to 6-phosphogluconate.

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Transporter that appears to play an indispensable role in the selective transport of the dietary cholesterol in and out of the enterocytes and in the selective sterol excretion by the liver into bile.

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PFKFB2 is involved in both the synthesis and degradation of fructose-2,6-bisphosphate, a regulatory molecule that controls glycolysis in eukaryotes. It has a 6-phosphofructo-2-kinase activity that catalyzes the synthesis of fructose-2,6-bisphosphate, and a fructose-2,6-biphosphatase activity that catalyzes the degradation of fructose-2,6-bisphosphate. PFKFB2 regulates fructose-2,6-bisphosphate levels in the heart, while a related enzyme encoded by a different gene regulates fructose-2,6-bisphosphate levels in the liver and muscle. This enzyme functions as a homodimer. There are two named isoforms.

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Protease that catalyzes two essential functions in the SUMO pathway: processing of full-length SUMO3 to its mature form and deconjugation of SUMO2 and SUMO3 from targeted proteins. Has weak proteolytic activity against full-length SUMO1 or SUMO1 conjugates. Required for cell division.

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Tau proteins are important Promotes microtubule assembly and stability, and might be involved in the establishment and maintenance of neuronal polarity. The C-terminus binds axonal microtubules while the N-terminus binds neural plasma membrane components, suggesting that tau functions as a linker protein between both. Axonal polarity is predetermined by tau localization (in the neuronal cell) in the domain of the cell body defined by the centrosome. The short isoforms allow plasticity of the cytoskeleton whereas the longer isoforms may preferentially play a role in its stabilization. Tau proteins subcellular located in the axons of neurons, in the cytoso l and in association with plasma membrane components. It expressed in neurons. PNS-tau is expressed in the peripheral nervous system while the others are expressed in the central nervous system.

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May be a signaling adapter molecule involved in p75NTR-mediated apoptosis induced by NGF. Plays a role in zinc-triggered neuronal death (By similarity). May play an important role in the pathogenesis of neurogenetic diseases.Tissue specificity: Found in ovarian granulosa cells, testis, prostate and seminal vesicle tissue. High levels also detected in liver.

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Apoptosis is related to many diseases and induced by a family of cell death receptors and their ligands. Cell death signals are transduced by death domain containing adapter molecules and members of the caspase family of proteases. These death signals finally cause the degradation of chromosomal DNA by activated DNase. DFF45/ICARD has been identified as inhibitor of caspase activated DNase DFF40/CAD. DFF45 related proteins CIDE A and CIDE B (for cell death inducing DFF like effector A and B) were recently identified. CIDE contains a new type of domain termed CIDE N, which has high homology with the regulatory domains of DFF45/ICAD and DFF40/CAD. Expression of CIDE A induces DNA fragmentation and activates apoptosis, which is inhibited by DFF45. CIDE A is a DFF45 inhibitable effector that promotes cell death and DNA fragmentation. CIDE A is expressed in many tissues.