Hledali jste: 1H-Indazole-4-boronic acid

Katalogové číslo: (BOSSBS-3016R-A750)

Dodavatel: Bioss

Popis: p44/42 MAP Kinase(Thr202); ERK (extracellular signal regulated kinase), also known as MAPK (mitogen activated protein kinase) has two closely related isoforms of 44 kDa and 42 kDa, respectively. These kinases belong to a family of serine/threonine kinases that are activated upon treatment of cells with a large variety of stimuli including mitogens, hormones, growth factors, cytokines, and bioactive peptides. Cell stimulation induces the activation of a signaling cascade, the downstream effects of which have been linked to the regulation of cell growth and differentiation as well as the cytoskeleton. ERK1 and ERK2 are phosphorylated within the activation loop on both a Threonine and a Tyrosine residue (within a Thr-Glu-Tyr motif) by MEKs (MAPK/ERK kinases), thereby greatly elevating the activity of ERK1&2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-3016R-A488)

Dodavatel: Bioss

Popis: p44/42 MAP Kinase(Thr202); ERK (extracellular signal regulated kinase), also known as MAPK (mitogen activated protein kinase) has two closely related isoforms of 44 kDa and 42 kDa, respectively. These kinases belong to a family of serine/threonine kinases that are activated upon treatment of cells with a large variety of stimuli including mitogens, hormones, growth factors, cytokines, and bioactive peptides. Cell stimulation induces the activation of a signaling cascade, the downstream effects of which have been linked to the regulation of cell growth and differentiation as well as the cytoskeleton. ERK1 and ERK2 are phosphorylated within the activation loop on both a Threonine and a Tyrosine residue (within a Thr-Glu-Tyr motif) by MEKs (MAPK/ERK kinases), thereby greatly elevating the activity of ERK1&2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-9362R)

Dodavatel: Bioss

Popis: The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This unit is responsible of the trypsin-like activity.The proteasome represents a large protein complex that exists inside all eukaryotes and archaea, and in some bacteria. The main function of proteasomes is to degrade unnecessary or damaged proteins by proteolysis. The most common form of the proteasome, known as the 26S Proteasome, contains one 20S Proteasome core particle structure and two 19S regulatory caps. The 20S Proteasome core is hollow and forms an enclosed cavity, where proteins are degraded, as well as openings at the two ends to allow the target protein to enter. The 20S Proteasome core particle contains many subunits, depending on the organism.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-6944R-A750)

Dodavatel: Bioss

Popis: DEAD-box proteins, characterised by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX32 is a 743 amino acid nuclear protein that localises to the mitochondria and is a member of the DEAD box helicase family. Expressed in various tissues, DDX32 is up-regulated by ionomycin in T lymphocytes and down-regulated in acute lymphoblastic leukemia. Considered a novel RNA helicase, DDX32 may play an important role in the development of colorectal cancer and may be involved in regulating T-cell response to certain apoptotic stimuli.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-3016R-A647)

Dodavatel: Bioss

Popis: p44/42 MAP Kinase(Thr202); ERK (extracellular signal regulated kinase), also known as MAPK (mitogen activated protein kinase) has two closely related isoforms of 44 kDa and 42 kDa, respectively. These kinases belong to a family of serine/threonine kinases that are activated upon treatment of cells with a large variety of stimuli including mitogens, hormones, growth factors, cytokines, and bioactive peptides. Cell stimulation induces the activation of a signaling cascade, the downstream effects of which have been linked to the regulation of cell growth and differentiation as well as the cytoskeleton. ERK1 and ERK2 are phosphorylated within the activation loop on both a Threonine and a Tyrosine residue (within a Thr-Glu-Tyr motif) by MEKs (MAPK/ERK kinases), thereby greatly elevating the activity of ERK1&2.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-0052R-CY5.5)

Dodavatel: Bioss

Popis: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-0052R-CY5)

Dodavatel: Bioss

Popis: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP1. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-13001R-A488)

Dodavatel: Bioss

Popis: DEAD-box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp, are putative RNA helicases implicated in several cellular processes involving modifications of RNA secondary structure and ribosome/spliceosome assembly. Based on their distribution patterns, some members of this family may be involved in embryogenesis, spermatogenesis, and cellular growth and division. DDX15 (DEAH-box protein 15), also known as DHX15, DBP1 or HRH2, is a nuclear ATP-dependent RNA helicase that is involved in pre-mRNA splicing and is a member of the DEAH-box subfamily of DEAD-box proteins. Expressed throughout the body, DDX15 is a pre-mRNA processing factor that plays a role in spliceosome disassembly after the release of mature mRNA. When localized to the nucleoli, DDX15 is thought to interact with the La/SSB autoantigen, an RNA chaperone that functions in various intracellular processes. DDX15 is 795 amino acids in length and is the human ortholog of the S. cerevisiae protein Prp43. helicase 2.

Měrná jednotka: 1 * 100 µl

Akce

Dodavatel: Thermo Fisher Scientific

Popis: Glycinamide hydrochloride (H-Gly-NH2.HCl) ≥98%

Bezpečnostní list Certifikáty

Dodavatel: Apollo Scientific

Popis: H-L-Dap(boc)-OMe·HCl

Katalogové číslo: (BOSSBS-6463R-A647)

Dodavatel: Bioss

Popis: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-6463R-A555)

Dodavatel: Bioss

Popis: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-6463R-HRP)

Dodavatel: Bioss

Popis: Most upstream protease of the activation cascade of caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A induced cell death. Binding to the adapter molecule FADD recruits it to either receptor. The resulting aggregate called death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. The active dimeric enzyme is then liberated from the DISC and free to activate downstream apoptotic proteases. Proteolytic fragments of the N-terminal propeptide (termed CAP3, CAP5 and CAP6) are likely retained in the DISC. Cleaves and activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May participate in the GZMB apoptotic pathways. Cleaves ADPRT. Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein. Isoform 5, isoform 6, isoform 7 and isoform 8 lack the catalytic site and may interfere with the pro-apoptotic activity of the complex.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-4250R-A750)

Dodavatel: Bioss

Popis: The three dimensional structure of many extracellular proteins is stabilised by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-4250R-A647)

Dodavatel: Bioss

Popis: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Měrná jednotka: 1 * 100 µl

Akce

Katalogové číslo: (BOSSBS-4250R-A350)

Dodavatel: Bioss

Popis: The three dimensional structure of many extracellular proteins is stabilized by the formation of disulphide bonds. Studies suggest that a microsomal enzyme known as Protein Disulphide Isomerase (PDI) is involved in disulphide-bond formation and isomerization, as well as the reduction of disulphide bonds in proteins. PDI, which catalyses disulphide interchange between thiols and protein dilsulphides, has also been referred to as thiol:protein-disulphide oxidoreductase and as glutathione:insulin transhydrogenase because of its role in reduction of disulphide bonds. The highly conserved sequence Lys-Asp-Glu-Leu (KDEL) is present at the carboxy-terminus of PDI and other soluble endoplasmic reticulum (ER) resident proteins including the 78 and 94 kDa glucose regulated proteins (GRP78 and GRP94 respectively). The presence of carboxy-terminal KDEL appears to be necessary for ER retention and appears to be sufficient to reduce the secretion of proteins from the ER. This retention is reported to be mediated by a KDEL receptor.

Měrná jednotka: 1 * 100 µl

Akce