110513 Results for: "Amberlite\u00AE+MB-20&pageNo=30"

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GDF10, or growth differentiation factor 10, bone morphogenetic protein (BMP) family and the TGF-beta superfamily. This group of proteins is characterized by a polybasic proteolytic processing site which is cleaved to produce a mature protein containing seven conserved cysteine residues. GDF10 is expressed in femur, brain, lung, skeletal muscle, pancreas and testis.

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Actin-depolymerizing factor (ADF), also known as destrin, is a member of the ADF/Cofilin/destrin superfamily that has the ability to rapidly depolymerize F-Actin in a stoichiometric manner. The Actin-depolymerizing activity of ADF is reversibly controlled by changes in KCl concentration but is insensitive to calcium concentration. ADF depolymerizes F-Actin by interacting directly with F-Actin protomers. ADF shares 71% sequence homology with Cofilin, however the two proteins differ in their interaction with Actin. The difference in the function of ADF and Cofilin results from the subtle difference in their amino acid sequence rather than possible differences in posttranslational modifications. As a result of different cleavage sites on ADF and Cofilin, the proteins differ in their overall tertiary folds. Sensitivity to polyphosphoinositides may be a common feature in vitro among Actin-binding proteins such as ADF and Cofilin that can bind to G-Actin and regulate the state of Actin polymerization. ADF and Cofilin are Actin-depolymerizing proteins whose activities are possibly regulated by their phosphorylation/dephosphorylation.

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Serine protease inhibitor. This inhibitor acts as 'bait' for tissue plasminogen activator, urokinase, protein C and matriptase-3/TMPRSS7. Its rapid interaction with PLAT may function as a major control point in the regulation of fibrinolysis.

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This gene encodes a serum protein found in association with the major histocompatibility complex (MHC) class I heavy chain on the surface of nearly all nucleated cells. The protein has a predominantly beta-pleated sheet structure that can form amyloid fibrils in some pathological conditions. A mutation in this gene has been shown to result in hypercatabolic hypoproteinemia.

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Substrate-specific adapter of a BCR (BTB-CUL3-RBX1) E3 ubiquitin ligase complex required for cell division. BCR E3 ubiquitin ligase complexes mediate the ubiquitination of target proteins.

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Plays an important role in the regulation of glutamine catabolism. Promotes mitochondrial respiration and increases ATP generation in cells by catalyzing the synthesis of glutamate and alpha-ketoglutarate. Increases cellular anti-oxidant function via NADH and glutathione production. May play a role in preventing tumor proliferation.

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Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues.

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Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Zinc finger and BTB domain-containing protein 43 (ZBTB43), also known as ZNF297B or ZBTB22B, is a 467 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZBTB43 contains a BTB domain, also known as a POZ domain, which inhibits DNA binding and mediates homotypic and heterotypic dimerization. Characteristics of the BTB domain and the interaction of ZBTB43 with BDP1 suggest that ZBTB43 functions as a transcription regulator.

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Protocadherins are a large family of cadherin-like cell adhesion proteins that are involved in the establishment and maintenance of neuronal connections in the brain. There are three protocadherin gene clusters, designated alpha, beta and gamma, all of which contain multiple tandemly arranged genes. PCDHB14 (Protocadherin beta 14) is a 798 amino acid protein that is one of 16 proteins in the protocadherin beta cluster. Unlike the alpha and gamma gene clusters whos genes are spliced to downstream constant region exons during transcription, members of the beta cluster (such as PCDHB14) do not use constant-region exons to produce mRNAs. As a result, each protocadherin beta gene encodes the transmembrane, extracellular and short cytoplasmic domains of the protein. Localized to the cell membrane, PCDHB14 is a single-pass type I membrane protein that contains six cadherin domains.

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The exosome is a multi-subunit complex composed of several highly conserved proteins, 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. EXOSC10, also known as PMSCL, PMSCL2, p2, p3, p4, RRP6, Rrp6p, PM-Scl, or PM/Scl-100, is an 885 amino acid protein that contains one HRDC domain and one 3’-5’ enonuclease domain. Localized to both the cytoplasm and the nucleus, EXOSC10 is part of the post-splicing exosome complex and is involved in mRNA surveillance, mRNA nuclear export and nonsense-mediated decay of mRNAs containing premature stop codons. against EXOSC10 have been found in patients with scleroderma and/or polymyositis (chronic diseases of the skin and muscle, respectively), suggesting that EXOSC10 may be involved in the pathogenesis of these diseases. Two isoforms of EXOSC10 exist due to alternative splicing events.

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Guanylate cyclases belong to the adenylyl cyclase class-4/guanylyl cyclase family. There are two forms of guanylate cyclase. The soluble forms, known as GCS or sGC, act as receptors for nitric oxide. The membrane-bound receptor forms, known as GC, are peptide hormone receptors. GCS, a cGMP-synthesizing enzyme, is the major receptor for the neurotransmitter nitric oxide (NO). It plays a crucial role in smooth muscle contractility, platelet reactivity and neurotransmission. GCS is a heme containing heterodimer, consisting of one alpha subunit, designated GCS-alpha-1, and one beta subunit. The heme moeity mediates NO activation, and this heme group also binds carbon monoxide, which weakly stimulates the enzyme. Both NO and CO stimulation are enhanced by the allosteric activator 3-(5'-hydroxymethyl-2'furyl)-benzyl-indazole, YC-1. YC-1 can also stimulate GCS in a NO-independent manner. Both the alpha and beta subunits are required for cGMP generation, and at least two isoforms exist for each subunit. Heterodimers consisting of alpha-1/beta-1 and alpha-2/beta-1 have been identified, and both display similar enzymatic activity.

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Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding domain of NR3C1 and mediates its nuclear export. Involved in maternal gene expression regulation. May participate in oocyte maturation via the regulation of calcium homeostasis (By similarity).

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Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-1, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19.

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Methylation at the 5'-position of cytosine is the only known naturally occurring covalent modification of the mammalian genome. DNA methylation requires the enzymatic activity of DNA 5-cytosine methyltransferase (Dnmt) proteins, which catalyze the transfer of a methyl group from S-adenosyl methionine to the 5'-position of cytosines, thereby repressing expression of the target gene. Dnmt3L (DNA (cytosine-5)-methyltransferase 3-like) is a 387 amino acid protein that contains one ADD-type zinc finger and is a member of the Dnmt family. Localized to the nucleus and expressed at lows levels in thymus, testis and ovary, Dnmt3L does not exhibit DNA methyltransferase activity, but is able to stimulate de novo methylation by Dnmt3 and is thought to play a key role in the establishment of genomic imprints. Additionally, Dnmt3L interacts with histone deacetylase 1 (HDAC1) and, through this interaction, mediates transcriptional repression. Multiple isoforms of Dnmt3L exist due to alternative splicing events.

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G-protein coupled receptor for CRH (corticotropin-releasing factor), UCN (urocortin), UCN2 and UCN3. Has high affinity for UCN. Ligand binding causes a conformation change that triggers signaling via guanine nucleotide-binding proteins (G proteins) and down-stream effectors, such as adenylate cyclase. Promotes the activation of adenylate cyclase, leading to increased intracellular cAMP levels.

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Probable inhibitory regulator of the Ras-cyclic AMP pathway.

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The C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily consists of a variety of proteins that share a common protein fold and have diverse functions, including cell-cell signaling, cell adhesion, glycoprotein turnover and immune responses. CLEC-9A (C-type lectin domain family 9 member A), also known as DNGR1 (dendritic cell natural killer lectin group receptor 1), is a 241 amino acid single-pass type II membrane protein that contains one C-type lectin domain and belongs to the CTL/CTLD superfamily. Expressed in myeloid lineage cells, brain, spleen and thymus, CLEC-9A is a group V C-type lectin-like receptor (CTLR) that acts as an activation receptor. The gene encoding CLEC-9A maps to human chromosome 12p13.2 and mouse chromosome 6 F3.

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Hamartin, or TSC1, is a suspected tumor suppressor implicated in the disease tuberous sclerosis 1. It is a negative regulator of cell division controlling the transition from G0/G1 to S phase, and it seems to act through the phosphatidylinositol 3 kinase/Akt pathway. TSC1 interacts with tuberin m(TSC2), which is thought to be a GAP (GTPase Activating Protein) for the Rap1 and Rab5 small G Proteins. The Hamartin/Tuberin complex has been shown to inhibit mTor. Hamartin has also been shown to interact with ERM (Ezrin-Radixin-Moesin) proteins and with F-actin, suggesting a role for TSC proteins in modulation of cell adhesion and morphology.

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Oligomeric Apaf-1 mediates the cytochrome c-dependent autocatalytic activation of pro-caspase-9 (Apaf-3), leading to the activation of caspase-3 and apoptosis. This activation requires ATP. Isoform 6 is less effective in inducing apoptosis.

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SUV39H1 is targeted to histone H3 via its interaction with RB1 and is involved in many processes, such as repression of MYOD1-stimulated differentiation, regulation of the control switch for exiting the cell cycle and entering differentiation, repression by the PML-RARA fusion protein, BMP-induced repression, repression of switch recombination to IgA and regulation of telomere length. Component of the eNoSC (energy-dependent nucleolar silencing) complex, a complex that mediates silencing of rDNA in response to intracellular energy status and acts by recruiting histone-modifying enzymes. The eNoSC complex is able to sense the energy status of cell: upon glucose starvation, elevation of NAD(+)/NADP(+) ratio activates SIRT1, leading to histone H3 deacetylation followed by dimethylation of H3 at 'Lys-9' (H3K9me2) by SUV39H1 and the formation of silent chromatin in the rDNA locus.

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The Gab family of adaptor proteins function as molecular scaffolds that mediate protein recruit-ment to RTKs. Cytokine/growth factor triggering of protein tyrosine kinase receptors (RTKs) initiates signaling cascades that progress to the nucleus where signals for activation, proliferation and differentiation occur. This scaffolding mechanism represents a critical link in cytokine/growth factor signaling routes. Gab 1-4 contain Pleckstrin homology and potential binding sites for SH2 and SH3 domain-containing proteins. The recruitment of signaling partners to Gab family members is phosphorylation-dependent. Insulin receptor and EGF receptor signaling are among the cascades that rely on Gab family members to elicit a nuclear response to an extracellular stimulus. Gab 4 (GRB2-associated-binding protein 4), also designated GRB2-associated-binding protein 2-like (Gab 2-like), is a 574 amino acid protein that shares 62% sequence similarity with Gab 2 and contains one Pleckstrin homology domain.

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Water is a critical component of all living cells. Interestingly, tissue membranes show a great degree of water permeability. Mammalian red cells, renal proximal tubules, and descending thin limb of Henle are extraordinarily permeable to water. Water crosses hydrophobic plasma membranes either by simple diffusion or through a facilitative transport mechanism mediated by special protein "aquaporin". Over the last decade, genes for several members of aquaporin family have been cloned, expressed, and their distribution studied in many tissues. AQP0 or MIP26 (major intrinsic protein 26kD), and Aquaporin 1 (AQP1, purified from red cells) also called CHIP28 (channel forming integral protein, 28kD; 268aa; gene locus 7p14) has been the foundation of the growing family of aquaporin. The lens specific AQP0 represents up to 80% of total lens membrane protein. Defects in MIP26 are cause of autosomal dominant cataract. The cataract Fraser mutation (CATFR or Shriveled) is a transposon induced splicing error that substitutes a long terminal repeat sequence for the C terminus of MIP. The lens opacity mutation (LOP) is an amino acid substitution that inhibits targeting of MIP to the cell membrane.

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Glial fibrillary acidic protein (GFAP) is a member of the class III intermediate filament protein family. It is heavily, and specifically, expressed in astrocytes and certain other astroglia in the central nervous system, in satellite cells in peripheral ganglia, and in non myelinating Schwann cells in peripheral nerves. In addition, neural stem cells frequently strongly express GFAP. to GFAP are therefore very useful as markers of astrocytic cells. In addition many types of brain tumor, presumably derived from astrocytic cells, heavily express GFAP. GFAP is also found in the lens epithelium, Kupffer cells of the liver, in some cells in salivary tumors and has been reported in erythrocytes.

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Substrate-recognition component of the CSA complex, a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex, involved in transcription-coupled nucleotide excision repair. The CSA complex (DCX(ERCC8) complex) promotes the ubiquitination and subsequent proteasomal degradation of ERCC6 in a UV-dependent manner; ERCC6 degradation is essential for the recovery of RNA synthesis after transcription-coupled repair. It is required for the recruitment of XAB2, HMGN1 and TCEA1/TFIIS to a transcription-coupled repair complex which removes RNA polymerase II-blocking lesions from the transcribed strand of active genes.

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This gene is a member of the glycoprotein hormone beta chain family and encodes the beta 3 subunit of chorionic gonadotropin (CG). Glycoprotein hormones are heterodimers consisting of a common alpha subunit and an unique beta subunit which confers biological specificity. CG is produced by the trophoblastic cells of the placenta and stimulates the ovaries to synthesize the steroids that are essential for the maintenance of pregnancy. The beta subunit of CG is encoded by 6 genes which are arranged in tandem and inverted pairs on chromosome 19q13.3 and contiguous with the luteinizing hormone beta subunit gene. [provided by RefSeq].

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Binds to and inhibits the transcriptional repressor ZBTB33, which may lead to activation of target genes of the Wnt signaling pathway (By similarity). May associate with and regulate the cell adhesion properties of both C- and E-cadherins. Implicated both in cell transformation by SRC and in ligand-induced receptor signaling through the EGF, PDGF, CSF-1 and ERBB2 receptors. Promotes GLIS2 C-terminal cleavage.

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GGTLC2

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Acts as decoy receptor for TNFSF11/RANKL and thereby neutralizes its function in osteoclastogenesis. Inhibits the activation of osteoclasts and promotes osteoclast apoptosis in vitro. Bone homeostasis seems to depend on the local ratio between TNFSF11 and TNFRSF11B. May also play a role in preventing arterial calcification. May act as decoy receptor for TNFSF1/TRAIL and protect against apoptosis. TNFSF1/TRAIL binding blocks the inhibition of osteoclastogenesis.

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Receptor for the CX3C chemokine fractalkine and mediates both its adhesive and migratory functions. Acts as coreceptor with CD4 for HIV-1 virus envelope protein (in vitro). Isoform 2 and isoform 3 seem to be more potent HIV-1 coreceptors than isoform 1.

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This gene product is highly similar to Schizosaccharomyces pombe rad9, a cell cycle checkpoint protein required for cell cycle arrest and DNA damage repair in response to DNA damage. This protein is found to possess 3' to 5' exonuclease activity, which may contribute to its role in sensing and repairing DNA damage. It forms a checkpoint protein complex with RAD1 and HUS1. This complex is recruited by checkpoint protein RAD17 to the sites of DNA damage, which is thought to be important for triggering the checkpoint-signaling cascade. Use of alternative polyA sites has been noted for this gene. [provided by RefSeq].