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Catalog Number: (BOSSBS-13148R-CY5)
Supplier: Bioss
Description: The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. A wide range of enzymes facilitate in the proteolytic Ub pathway, including monoclonal nonspecific suppressor factor-beta (MNSF-beta), a subunit of MNSF, which is a lymphokine product of a murine T cell hybrid-oma that restricts the production of LPS-induced immunoglobulin secreting cells in an antigen-nonspecific manner. MNSF-beta is a ubiquitin-like fusion protein consisting of the ribosomal protein S30 and a protein that shares 36% sequence identity with ubiquitin. This ubiquitin-like segment (Ubi-L) can be cleaved from MNSF-beta in the cytosol.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13148R-CY3)
Supplier: Bioss
Description: The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. A wide range of enzymes facilitate in the proteolytic Ub pathway, including monoclonal nonspecific suppressor factor-beta (MNSF-beta), a subunit of MNSF, which is a lymphokine product of a murine T cell hybrid-oma that restricts the production of LPS-induced immunoglobulin secreting cells in an antigen-nonspecific manner. MNSF-beta is a ubiquitin-like fusion protein consisting of the ribosomal protein S30 and a protein that shares 36% sequence identity with ubiquitin. This ubiquitin-like segment (Ubi-L) can be cleaved from MNSF-beta in the cytosol.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-13148R-A350)
Supplier: Bioss
Description: The ubiquitin (Ub) pathway involves three sequential enzymatic steps that facilitate the conjugation of Ub and Ub-like molecules to specific protein substrates. The first step requires the ATP-dependent activation of the Ub C-terminus and the assembly of multi-Ub chains by the Ub-activating enzyme known as the E1 component. The Ub chain is then conjugated to the Ub-conjugating enzyme (E2) to generate an intermediate Ub-E2 complex. The Ub-ligase (E3) then catalyzes the transfer of Ub from E2 to the appropriate protein substrate. A wide range of enzymes facilitate in the proteolytic Ub pathway, including monoclonal nonspecific suppressor factor-beta (MNSF-beta), a subunit of MNSF, which is a lymphokine product of a murine T cell hybrid-oma that restricts the production of LPS-induced immunoglobulin secreting cells in an antigen-nonspecific manner. MNSF-beta is a ubiquitin-like fusion protein consisting of the ribosomal protein S30 and a protein that shares 36% sequence identity with ubiquitin. This ubiquitin-like segment (Ubi-L) can be cleaved from MNSF-beta in the cytosol.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11766R)
Supplier: Bioss
Description: In eukaryotic systems, initiation of transcription from protein-coding genes is a complex process requiring RNA polymerase II and broad families of auxiliary transcription factors. Such factors can be divided into two major functional classes: the basal factors that are required for transcription of all Pol II genes, including TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH; and sequence-specific factors that regulate gene expression. The basal transcription factors and Pol II form a specific multiprotein complex near the transcription start site by interacting with core promotor elements such as the TATA box generally located 25-30 base pairs upstream of the transcription start site. Binding of TFIID to the TATA element initiates assembly of the other factors into a pre-initiation complex. The TATA-binding subunit of TFIID (designated TFIIDt or TBP) from higher eukaryotes contains a highly conserved 180 amino acid C-terminal domain.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11766R-CY3)
Supplier: Bioss
Description: In eukaryotic systems, initiation of transcription from protein-coding genes is a complex process requiring RNA polymerase II and broad families of auxiliary transcription factors. Such factors can be divided into two major functional classes: the basal factors that are required for transcription of all Pol II genes, including TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH; and sequence-specific factors that regulate gene expression. The basal transcription factors and Pol II form a specific multiprotein complex near the transcription start site by interacting with core promotor elements such as the TATA box generally located 25-30 base pairs upstream of the transcription start site. Binding of TFIID to the TATA element initiates assembly of the other factors into a pre-initiation complex. The TATA-binding subunit of TFIID (designated TFIIDt or TBP) from higher eukaryotes contains a highly conserved 180 amino acid C-terminal domain.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11766R-A350)
Supplier: Bioss
Description: In eukaryotic systems, initiation of transcription from protein-coding genes is a complex process requiring RNA polymerase II and broad families of auxiliary transcription factors. Such factors can be divided into two major functional classes: the basal factors that are required for transcription of all Pol II genes, including TFIIA, TFIIB, TFIID, TFIIE, TFIIF and TFIIH; and sequence-specific factors that regulate gene expression. The basal transcription factors and Pol II form a specific multiprotein complex near the transcription start site by interacting with core promotor elements such as the TATA box generally located 25-30 base pairs upstream of the transcription start site. Binding of TFIID to the TATA element initiates assembly of the other factors into a pre-initiation complex. The TATA-binding subunit of TFIID (designated TFIIDt or TBP) from higher eukaryotes contains a highly conserved 180 amino acid C-terminal domain.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11805R-A488)
Supplier: Bioss
Description: AT-motif binding factor 1 (ATBF1) binds to the AT-rich core sequence element in the human a-fetoprotein enhancer (1). Alternative splicing generates the ATBF1-A and ATBF1-B (2,3). While ATBF1-A contains a 920-amino acid extension at the N-terminus, both ATBF1-A and ATBF1-B contain 4 DNA-binding homeobox domains (2,3). Additionally, ATBF1-A contains 23 zinc finger motifs while ATBF1-B contains 18 zinc finger motifs (1–3). The N-terminal extension unique to ATBF1-A has transcriptional repressor activity (4). In the small intestine, ATBF1-A inhibits expression of the brushborder enzyme aminopeptidase-N through direct binding to the AT motif element (5). Besides functioning in transcription regulation, ATBF1 also functions in ATPase activity (6). ATPase activity associated with ATBF1-A is DNA/RNA-dependent and requires both homeobox domains and zinc finger motifs (6). ATBF1 is highly expressed in spleen and brain tissues (7). The gene encoding human ATBF1 maps to chromosome 16q22.3-q23.1 (8).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-1122R-A488)
Supplier: Bioss
Description: The semaphorins are a family of proteins that are involved in signaling. All the family members have a secretion signal, a 500-amino acid sema domain, and 16 conserved cysteine residues(Kolodkin et al., 1993 [PubMed 8269517]). Sequence comparisons have grouped the secreted semaphorins into 3 general classes, all of which also have an immunoglobulin domain. The semaphorin III family, consisting of human semaphorin III (SEMA3A; MIM 603961), chicken collapsin, and mouse semaphorins A, D, and E, all have a basic domain at the C terminus. Chicken collapsin contributes to path finding by axons during development by inhibiting extension of growth cones (Luo et al., 1993 [PubMed 8402908]) through an interaction with a collapsin response mediator protein of relative molecular mass 62K (CRMP62) (Goshima et al., 1995 [PubMed7637782]), a putative homolog of an axonal guidance associated UNC33 gene product (MIM 601168). SEMA3F is a secreted member of the semaphorin III family.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-11805R-HRP)
Supplier: Bioss
Description: AT-motif binding factor 1 (ATBF1) binds to the AT-rich core sequence element in the human a-fetoprotein enhancer (1). Alternative splicing generates the ATBF1-A and ATBF1-B (2,3). While ATBF1-A contains a 920-amino acid extension at the N-terminus, both ATBF1-A and ATBF1-B contain 4 DNA-binding homeobox domains (2,3). Additionally, ATBF1-A contains 23 zinc finger motifs while ATBF1-B contains 18 zinc finger motifs (1–3). The N-terminal extension unique to ATBF1-A has transcriptional repressor activity (4). In the small intestine, ATBF1-A inhibits expression of the brushborder enzyme aminopeptidase-N through direct binding to the AT motif element (5). Besides functioning in transcription regulation, ATBF1 also functions in ATPase activity (6). ATPase activity associated with ATBF1-A is DNA/RNA-dependent and requires both homeobox domains and zinc finger motifs (6). ATBF1 is highly expressed in spleen and brain tissues (7). The gene encoding human ATBF1 maps to chromosome 16q22.3-q23.1 (8).
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9474R-A350)
Supplier: Bioss
Description: Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9474R-A680)
Supplier: Bioss
Description: Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localised to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localisation signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-9474R-CY5.5)
Supplier: Bioss
Description: Members of the NFAT (nuclear factor of activated T cells) family of transcription factors are related to NFkB/Rel proteins and form cooperative complexes with the AP-1 proteins, Fos and Jun, on DNA to regulate cytokine expression in T cells. NFAT proteins are widely expressed and alternatively modified to generate splice variants, and they are localized to both the cytosol (NFATc) and to the nucleus (NFATn). NFAT1, NFAT2, and NFAT4 are predominantly expressed in immune cells, and NFAT2 and NFAT3 are expressed at high levels in cardiac tissues. In addition to activating cytokine gene transcription, NFAT2 is also implicated in cardiac valve development, and NFAT3 is involved in cardiac hypertrophy. NFAT5 is detected in both immune and nonimmune cells and, like other NFAT proteins, contains a highly conserved Rel-like binding domain that mediates NFAT proteins associating with specific consensus sequences on DNA. NFAT proteins are activated by increases in intracellular calcium, which leads to the calmodulin-dependent phosphatase, calcineurin, dephosphorylating NFAT proteins. This activating event induces a conformational change in the protein structure that exposes the nuclear localization signal and facilitates the translocation of NFAT proteins from the cytosol into the nucleus.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8682R-A750)
Supplier: Bioss
Description: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilise the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilised antigen based chromatography.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8682R-FITC)
Supplier: Bioss
Description: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8682R-A647)
Supplier: Bioss
Description: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM: 1 * 100 µl


Catalog Number: (BOSSBS-8682R-CY5)
Supplier: Bioss
Description: The activation of RaP1 by cAMP is independent of PKA and is mediated by recently discovered family of guanine nucleotide exchange factors (GEFs) called cAMP-GEFs or Epacs. The Epac signaling therefore represents a novel mechanism for cAMP signaling with in the cAMP cascade. There are 2 members of the Epac family, Epac1 and Epac 2. Both proteins are multidomain proteins containing an autoinhibitory cAMP-binding domain that inhibits the catalytic region and a DEP domain (dishevelled, Egl-10 and pleckstrin homology domain) targeting the membrane anchors. EPAC2 has an additional cAMP-binding site in its N-terminus that binds cAMP with low affinity. EPAC1 mRNA is broadly expressed, with particularly high levels occurring in the thyroid, ovary, kidney and certain brain regions, whereas expression of EPAC2 mRNA appears to be restricted to the brain and adrenal glands. Epac 1 and Epac 2 also interact with light chain 2 (LC2) or MAP1A that serves as a scaffolding structure to stabilize the signal transduction complex. The Epac 1-selective were generated against unique antigenic sequences form near N-terminus and between RasGEFN and Ras GEF domains. The to Epac 1are affinity purified over immobilized antigen based chromatography.
UOM: 1 * 100 µl


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Stock for this item is limited, but may be available in a warehouse close to you. Please make sure that you are logged in to the site so that available stock can be displayed. If the call is still displayed and you need assistance, please call us on +353 1 88 22222
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