19552 Results for: "Sodium+carbonate+decahydrate"

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The protein encoded by this gene is a member of the STAT protein family. In response to cytokines and growth factors, STAT family members are phosphorylated by the receptor associated kinases, and then form homo- or heterodimers that translocate to the cell nucleus where they act as transcription activators. In response to interferon (IFN), this protein forms a complex with STAT1 and IFN regulatory factor family protein p48 (ISGF3G), in which this protein acts as a transactivator, but lacks the ability to bind DNA directly. Transcription adaptor P300/CBP (EP300/CREBBP) hasbeen shown to interact specifically with this protein, which is thought to be involved in the process of blocking IFN-alpha response by adenovirus. Multiple transcript variants encoding different isoforms have been found for this gene.

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Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation

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Transcription factor that can activate or repress transcription in response to physiological and pathological stimuli. Binds with high affinity to GC-rich motifs and regulates the expression of a large number of genes involved in a variety of processes such as cell growth, apoptosis, differentiation and immune responses. Highly regulated by post-translational modifications (phosphorylations, sumoylation, proteolytic cleavage, glycosylation and acetylation). Binds also the PDGFR-alpha G-box promoter. May have a role in modulating the cellular response to DNA damage. Implicated in chromatin remodeling. Plays a role in the recruitment of SMARCA4/BRG1 on the c-FOS promoter. Plays an essential role in the regulation of FE65 gene expression.

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AURKB (aurora kinase B, AIK2 or aurora-B), with 344-amino acid protein(about 39 kDa),localizes to microtubules near kinetochores, specifically to the specialized microtubules called K-fibers. AURKB is a mitotic protein kinase, which phosphorylates histone H3 and regulates Chromosomal segregation during mitosis and meiosis.It may regulates several stages of mitosis such as centrosome separation, chromosome segregation and cytokinesis.Component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of mitosis. The CPC complex has essential functions at the centromere in ensuring correct chromosome alignment and segregation and is required for chromatin-induced microtubule stabilization and spindle assembly. ARK-2 transcripts arepresent at high levels in human thymus and fetal liver.ARK-2 protein levels are maximal during both S and G2/M phases

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The scaffolding protein encoded by Caveolin-1 is the main component of the caveolae plasma membranes found in most cell types. The protein links integrin subunits to the tyrosine kinase FYN, an initiating step in coupling integrins to the Ras-ERK pathway and promoting cell cycle progression. The gene is a tumor suppressor gene candidate and a negative regulator of the Ras-p42/44 MAP kinase cascade. CAV1 and CAV2 are located next to each other on chromosome 7 and express colocalizing proteins that form a stable hetero-oligomeric complex. By using alternative initiation codons in the same reading frame, two isoforms (alpha and beta) are encoded by a single transcript from this gene.

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The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation

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Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance, lamellipodial and filopodial dynamics, platelet activation and cell migration. VASP promotes actin filament elongation. It protects the barbed end of growing actin filaments against capping and increases the rate of actin polymerization in the presence of capping protein. VASP stimulates actin filament elongation by promoting the transfer of profilin-bound actin monomers onto the barbed end of growing actin filaments. Plays a role in actin-based mobility of Listeria monocytogenes in host cells. Regulates actin dynamics in platelets and plays an important role in regulating platelet aggregation.

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SIRT5 is a human member of a family of proteins called Sirtuins (Sir2-like proteins) and are present in prokaryotes and eukaryotes. All Sir2-like proteins have a sirtuin core domain, which contains a series of sequence motifs conserved in organisms ranging from bacteria to humans. Bacterial, yeast and mammalian sirtuins are able to metabolize NAD and possibly at as mono-ADP-ribosyltransferases. The enzymatic function of sirtuins is not yet completely understood but recent reports of histone-activated Sir2-mediated NAD metabolism and NAD-activated Sir2-mediated histone deacetylation suggest a possible coupled reciprocal activation mechanism involving interactions of Sir2 with NAD and the N epsilon-acetyl-lysine groups of acetylated histones.

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MSH2 is a 100 kDa nuclear antigen and encodes a protein of 934 amino acids. The MSH2 gene is one of 4 known genes encoding proteins involved in the repair of mismatch nucleotides following DNA replication or repair. Mutations in the MSH2 gene contribute to the development of sporadic colorectal carcinoma. MSHS mutations are responsible for 50% of inherited non-polyposis colorectal (HNPCC). The repair of mismatch DNA is essential to maintaining the integrity of genetic information over time. An alteration of microsatellite repeats is the result of slippage owing to strand misalignment during DNA replication and is referred to as microsatellite instability (MSI). These defects in DNA repair pathways have been related to human carcinogenesis. MSH-2 is involved in the initial cognition of mismatch nucleotides during the replication mismatch repair process.

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RET (ret proto-oncogene) is a member of the cadherin superfamily and a receptor tyrosine kinase, which are cell-surface molecules that transduce signals for cell growth and differentiation. It can undergo oncogenic activation in vivo and in vitro by cytogenetic rearrangement. Ligands that bind the Ret receptor include the glial cell line-derived neurotropic factor (GDNF) and its congeners neurturin, persephin and artemin. Alterations in the corresponding Ret gene are associated with diseases including papillary thyroid carcinoma, multiple endocrine neoplasia (type 2A and 2B), familial medullary thyroid carcinoma and a congenital developmental disorder known as Hirschsprung抯 disease. The Tyr905 residue located in the Ret kinase domain plays a crucial role in Ret catalytic and biological activity. Substitution of Phe for Tyr905 dramatically inhibits Ret autophosphorylation activity.

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The Itg-Beta3 gene encodes the beta subunit of the platelet membrane adhesive protein receptor complex Itg-Beta3 protein, which belongs to the Integrin class of cell adhesion molecule receptors that share a common heterotrimeric structure with Alpha and Beta subunits. It is a common Beta subunit of the platelet complex and of two other Integrins (Fibronectin and Vitronectin Receptors), which have distinct Alpha subunits. Itg-Beta3 has been implicated in a wide variety of functions, including platelet aggregation and thrombosis and implantation, placentation, angiogenesis, bone remodeling, and tumor progression. Glanzmann Thrombasthenia can result from defects in the genes for either the Itg-Alpha2B or the Itg-Beta3 subunit

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Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation.

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ATM encoded by this gene belongs to the PI3/PI4-kinase family. This protein is an important cell cycle checkpoint kinase that phosphorylates; thus, it functions as a regulator of a wide variety of downstream proteins, including tumor suppressor proteins p53 and BRCA1, checkpoint kinase CHK2, checkpoint proteins RAD17 and RAD9, and DNA repair protein NBS1. This protein and the closely related kinase ATR are thought to be master controllers of cell cycle checkpoint signaling pathways that are required for cell response to DNA damage and for genome stability. Mutations in this gene are associated with ataxia telangiectasia, an autosomal recessive disorder. Two transcript variants encoding different isoforms have been found for this gene.

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The BRCA1-BARD1 heterodimer coordinates a diverse range of cellular pathways such as DNA damage repair, ubiquitination and transcriptional regulation to maintain genomic stability. Acts by mediating ubiquitin E3 ligase activity that is required for its tumor suppressor function. Plays a central role in DNA repair by facilitating cellular response to DNA repair. Required for appropriate cell cycle arrests after ionizing irradiation in both the S-phase and the G2 phase of the cell cycle. Involved in transcriptional regulation of P21 in response to DNA damage. Required for FANCD2 targeting to sites of DNA damage. May function as a transcriptional regulator. Inhibits lipid synthesis by binding to inactive phosphorylated ACACA and preventing its dephosphorylation

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Mediates B-cell B-cell interactions. May be involved in the localization of B-cells in lymphoid tissues. Binds sialylated glycoproteins; one of which is CD45. Preferentially binds to alpha-2, 6-linked sialic acid. The sialic acid recognition site can be masked by cis interactions with sialic acids on the same cell surface. Upon ligand induced tyrosine phosphorylation in the immune response seems to be involved in regulation of B-cell antigen receptor signaling. Plays a role in positive regulation through interaction with Src family tyrosine kinases and may also act as an inhibitory receptor by recruiting cytoplasmic phosphatases via their SH2 domains that block signal transduction through dephosphorylation of signaling molecules.

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IL-36G is is a member of the interleukin 1 cytokine family whose gene and eight other interleukin 1 family genes form a cytokine gene cluster on chromosome 2. IL-36G is thought to activate the NF-kappaB pathway through IL-1 receptor family members IL-1RL2 and IL-1RAcP. Like the related proteins IL-36A and IL-36B, IL-36G requires post-translational processing for full agonist activity, but the cleavage mechanism is currently unknown. IL-36G expression is stimulated by interferon-gamma, tumor necrosis factor-alpha and interleukin 1. The IL-36 cytokines have been suggested to amplify Th1 responses by enhancing proliferation and Th1 polarization of naive CD4+ T cells.

Supplier: Thermo Scientific

Process a range of general-purpose applications including cell culture, microplate, bioproduction, blood separation, and microbiology with the Thermo Scientific™ Multifuge™ X4 Pro centrifuge series featuring new touch screen technology, making daily tasks easier.

Supplier: Rockland Immunochemicals

Anti-Chicken Red Blood Cell Antibody may be used in hemagglutination assays. Haemagglutination assay or HA is a method of quantification for viruses or bacteria by hemagglutination. Some viral families and many bacteria have envelope or surface proteins which are able to agglutinate (stick to) human or animal red blood cells (RBC) and bind to N-acetylneuraminic acid. As each of the agglutinating molecule attaches to multiple RBCs, a lattice-structure will form. Normally, a virus dilution (e.g. 2-fold from 1:4 to 1:4096) will be applied to an RBC dilution (e.g. 0.1% to 0.7% in steps of 0.2%) for approx. 30 min, often at 4° C, otherwise viruses with neuraminidase activity will detach the virus from the RBCs. Then the lattice forming parts will be counted and the titer calculated. The titer of a hemagglutination assay is determined by the last viable "lattice" structure found. This is because it is at the point where, if diluted anymore, the amount of Virus particles will be less than that of the RBCs and thus not be able to agglutinate them together. Anti-CHICKEN Red Blood Cell Antibody is used to sensitize erythrocytes and quantitate agglutination.

Supplier: Rockland Immunochemicals

Anti-Sheep Red Blood Cell Antibody may be used in hemagglutination assays. Anti-SHEEP Red Blood Cell Antibody is used to sensitize erythrocytes and quantitate agglutination. Haemagglutination assay or HA is a method of quantification for viruses or bacteria by hemagglutination. Some viral families and many bacteria have envelope or surface proteins which are able to agglutinate (stick to) human or animal red blood cells (RBC) and bind to N-acetylneuraminic acid. As each of the agglutinating molecule attaches to multiple RBCs, a lattice-structure will form. Normally, a virus dilution (e.g. 2-fold from 1:4 to 1:4096) will be applied to an RBC dilution (e.g. 0.1% to 0.7% in steps of 0.2%) for approx. 30 min, often at 4° C, otherwise viruses with neuraminidase activity will detach the virus from the RBCs. Then the lattice forming parts will be counted and the titer calculated. The titer of a hemagglutination assay is determined by the last viable "lattice" structure found. This is because it is at the point where, if diluted anymore, the amount of Virus particles will be less than that of the RBCs and thus not be able to agglutinate them together.

Supplier: Rockland Immunochemicals

Anti-Sheep Red Blood Cell Antibody may be used in hemagglutination assays. Haemagglutination assay or HA is a method of quantification for viruses or bacteria by hemagglutination. Some viral families and many bacteria have envelope or surface proteins which are able to agglutinate (stick to) human or animal red blood cells (RBC) and bind to N-acetylneuraminic acid. As each of the agglutinating molecule attaches to multiple RBCs, a lattice-structure will form. Normally, a virus dilution (e.g. 2-fold from 1:4 to 1:4096) will be applied to an RBC dilution (e.g. 0.1% to 0.7% in steps of 0.2%) for approx. 30 min, often at 4° C, otherwise viruses with neuraminidase activity will detach the virus from the RBCs. Then the lattice forming parts will be counted and the titer calculated. The titer of a hemagglutination assay is determined by the last viable "lattice" structure found. This is because it is at the point where, if diluted anymore, the amount of Virus particles will be less than that of the RBCs and thus not be able to agglutinate them together. Anti-SHEEP Red Blood Cell Antibody is used to sensitize erythrocytes and quantitate agglutination.

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Key regulator of entry into cell division that acts as a tumor suppressor. 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, SUV420H1 and SUV420H2, leading to epigenetic transcriptional repression. Controls histone H4 'Lys-20' trimethylation. Inhibits the intrinsic kinase activity of TAF1. In case of viral infections, interactions with SV40 large T antigen, HPV E7 protein or adenovirus E1A protein induce the disassembly of RB1-E2F1 complex thereby disrupting RB1's activity.

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Involved in chromosome cohesion during cell cycle and in DNA repair. Central component of cohesin complex. The cohesin complex is required for the cohesion of sister chromatids after DNA replication. The cohesin complex apparently forms a large proteinaceous ring within which sister chromatids can be trapped. At anaphase, the complex is cleaved and dissociates from chromatin, allowing sister chromatids to segregate. The cohesin complex may also play a role in spindle pole assembly during mitosis. Involved in DNA repair via its interaction with BRCA1 and its related phosphorylation by ATM, or via its phosphorylation by ATR. Works as a downstream effector both in the ATM/NBS1 branch and in the ATR/MSH2 branch of S-phase checkpoint.

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NF-κ-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-κ-B is a homo- or heterodimeric complex formed by the Rel-like domain-containing proteins RELA/p65, RELB, NFKB1/p105, NFKB1/p50, REL and NFKB2/p52 and the heterodimeric p65-p50 complex appears to be most abundant one. The dimers bind at kappa-B sites in the DNA of their target genes and the individual dimers have distinct preferences for different kappa-B sites that they can bind with distinguishable affinity and specificity. Different dimer combinations act as transcriptional activators or repressors, respectively.

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FES (feline sarcoma oncogene) and Fer are the only two members of a unique family of cytoplasmic protein tyrosine kinases.FES and Fer contain a central Src homology-2 (SH2) domain and a carboxy-terminal tyrosine kinase catalytic domain. They are structurally distinguished from other members of cytoplasmic protein tyrosine kinase subfamilies by the presence of amino-terminal Fer/CIP4 homology and coiled-coil domains. FES was originally identified as an oncogene from avian and feline retroviruses. Human c-Fes has been implicated in myeloid, vascular endothelial and neuronal cell differentiation. FES has tyrosine-specific protein kinase activity and that activity is required for maintenance of cellular transformation. Mutations may activate the FES kinase and thereby contribute to cancer. However, recent data strongly suggests that the c-FES protein-tyrosine kinase is a tumor suppressor rather than a dominant oncogene in colorectal cancer.

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Cyclin-dependent kinase activity is regulated by T-loop phosphorylation (Thr172 in the case of CDK4), by the abundance of their cyclin partners, and by association with CDK inhibitors of the Cip/Kip or INK family of proteins. The inactive ternary complex of CDK4/cyclin D and p27 Kip1/Cip1 requires extracellular mitogenic stimuli for the release and degradation of p27, which affects progression through the restriction point and pRb-dependent entry into S-phase. The active complex of CDK4/cyclin D targets the retinoblastoma protein for phosphorylation, allowing the release of E2F transcription factors that activate G1/S-phase gene expression. In HeLa cells, upon UV irradiation, upregulation of p16 INK4A association with CDK4/cyclin D3 leads to a G2 delay, implicating CDK4/cyclin D3 activity in progression through the G2-phase of the cell cycle.

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Heterogeneous nuclear ribonucleoprotein A1 (hnRNP A1) is a member of the hnRNP A/B family of related RNA binding proteins that bind pre-mRNA and are involved in the processing, metabolism and transport of nuclear pre-mRNA transcripts. hnRNP A1 regulates the alternative splicing of c-Src, c-H-Ras and modifies initiation of translation of the fibroblast growth factor 2 mRNA. hnRNP A1 expression level is elevated in many cancers; knockdown of hnRNP A1 leads to apoptosis in various cancer cells. Although predominantly nuclear, hnRNP A1 is continually transported from the nucleus to the cytoplasm where it disassociates from mRNA and is rapidly re-imported into the nucleus. hnRNP A1 binds to cis-acting repressive sequences (CRS) of HIV-1 to influence HIV-1 production. HIV-1 enhances hnRNP A1 expression and promotes the relocalization of hnRNP A1 to the cytoplasm ,

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Hsp90 is a member of the heat shock protein 90 family that functions as a molecular chaperone and has ATPase activity. Hsp90 family proteins are highly conserved between isoforms and species. Several signal transduction pathways depend on Hsp90 function including erbB2, steroid hormone receptors (such as androgen, progesterone, glucocorticoid, and aryl-hydrocarbon), and hypoxia sensing (Hif1alpha). Recent reports show that tumor cells are more sensitive to Hsp90 inhibition and that Hsp90 from tumor cells is more sensitive to small molecule inhibitors (eg 17AAG). The mechanism of this differential sensitivity of normal versus tumor Hsp90 is not known (although mutation has been ruled out). One possible mechanism may be differences in post-translational modification of tumor Hsp90. Hsp90 is a cytoplasmic protein that forms a homodimer in vivo, and interacts with TOM34, AHSA1, HDAC6 and SMYD3.

Supplier: SARSTEDT

S-Monovette® is a blood collection system that combines two blood collection techniques – aspiration and vacuum. The S-Monovette® is suitable for all vein conditions and achieves an optimal sample quality, thereby producing the best results. The aspiration technique is a gentle technique for routine blood collection. Using the vacuum technique, a "fresh" vacuum is always available.

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Alpha-tubulin belongs to the tubulin superfamily, which is composed of six distinct families. Along with beta-tubulins, alpha-tubulins are the major components of microtubules. These microtubules are involved in a wide variety of cellular activities ranging from mitosis and transport events to cell movement and the maintenance of cell shape. Alpha- and beta-tubulin dimers are assembled to 13 protofilaments that form a microtubule of 22-nm diameter (reviewed in 1). Tyrosine ligase adds a C-terminal tyrosine to monomeric alpha-tubulin. Assembled microtubules can again be detyrosinated by a cytoskeleton-associated carboxypeptidase (2). Another post-translational modification of detyrosinated alpha-tubulin is C-terminal polyglutamylation, which is characteristic of microtubules in neuronal cells and the mitotic spindle (3). Like GAPDH and beta-Actin, this antibody makes an excellent loading control in immunoblots.

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CCNT1 Antibody: Cyclins function as regulators of CDK kinases and exhibit distinct expression and degradation patterns which contribute to the temporal coordination of each mitotic event. The cyclin-T1 protein (CCNT1) belongs to the highly conserved cyclin family, whose members are characterized by a dramatic periodicity in protein abundance through the cell cycle. CCNT1 tightly associates with CDK9 kinase, and was found to be a major subunit of the transcription elongation factor p-TEFb. The kinase complex containing CCNT1 and the elongation factor can interact with, and act as a cofactor of human immunodeficiency virus type 1 (HIV-1) Tat protein, and was shown to be both necessary and sufficient for full activation of viral transcription. CCNT1 and its kinase partner were also found to be involved in the phosphorylation and regulation of the carboxy-terminal domain (CTD) of the largest RNA polymerase II subunit.