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Votre recherche pour: Nepsilon-trifluoroacetyl-L-lysine


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Référence Produit: (BOSSBS-2893R-A488)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-2893R-A555)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (PIER26777)
Fournisseur: Thermo Fisher Scientific
Description: Pierce™ Sulfo-NHS-Acetate is a small compound used for blocking primary amines (eg. lysine side chains). This compound forms stable, covalent amide bonds with amine groups to prevent specific interactions or conjugations.
UOM: 1 * 100 mg


Référence Produit: (BOSSBS-2893R-A680)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-2893R-A647)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-2893R-A750)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-2893R)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-2894R)
Fournisseur: Bioss
Description: Responsible for the deacetylation of lysine residues on the N-terminal part of the core histones (H2A, H2B, H3 and H4). Histone deacetylation gives a tag for epigenetic repression and plays an important role in transcriptional regulation, cell cycle progression and developmental events. Histone deacetylases act via the formation of large multiprotein complexes.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-1499R-A680)
Fournisseur: Bioss
Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-1499R-A750)
Fournisseur: Bioss
Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
UOM: 1 * 100 µl


Référence Produit: (ENZOALX350183C100)
Fournisseur: Enzo Life Sciences
Description: Anabaenopeptins are a highly diverse group of bioactive peptides produced by several genera of cyanobacteria such as Anabaena, Planktothrix, Microcystis and Nodularia. These peptides are commonly detected in cyanobacterial blooms along with the well known microcystins. Unique cyclic peptides where lysine is conserved in position 2 and cyclisation is achieved by linkage of the lysine to the C-terminal amino acid. In addition the side chain of a single amino acid is attached via a ureido bond. Bioactive peptides originally isolated from Anabaena flos-aquae NRC 525-17 where they were shown to be non-toxic in mice but had dose dependant relaxations in rat aortic preparations with endothelium precontracted with 0.1µM norpinephrine.
Anabaenopeptins inhibit protein phosphatase.
UOM: 1 * 100 µG


Référence Produit: (PRSI26-966)
Fournisseur: ProSci Inc.
Description: The covalent modification of proteins by the small ubiquitin-like protein SUMO is implicated in the regulation of nucleocytoplasmic transport, genomic stability, gene transcription, and other processes. Sumoylation is catalyzed on target lysine residues by a multienzyme process and is reversed by desumoylating enzymes such as SENP1.
UOM: 1 * 50 µG


Référence Produit: (BOSSBS-10501R-CY7)
Fournisseur: Bioss
Description: This gene encodes a trypsinogen, which is a member of the trypsin family of serine proteases. This enzyme is secreted by the pancreas and cleaved to its active form in the small intestine. It is active on peptide linkages involving the carboxyl group of lysine or arginine. This gene and several other trypsinogen genes are localized to the T cell receptor beta locus on chromosome 7. [provided by RefSeq, Jul 2008].
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-1499R-CY7)
Fournisseur: Bioss
Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-1499R-FITC)
Fournisseur: Bioss
Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
UOM: 1 * 100 µl


Référence Produit: (BOSSBS-1499R-A488)
Fournisseur: Bioss
Description: Ubiquitin-like protein that can be covalently attached to proteins as a monomer or a lysine-linked polymer. Covalent attachment via an isopeptide bond to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by E3 ligases such as PIAS1-4, RANBP2 or CBX4. This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Involved for instance in targeting RANGAP1 to the nuclear pore complex protein RANBP2. Polymeric SUMO1 chains are also susceptible to polyubiquitination which functions as a signal for proteasomal degradation of modified proteins. May also regulate a network of genes involved in palate development.
UOM: 1 * 100 µl


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Le stock de cet article est limité mais peut être disponible dans un entrepôt proche de vous. Merci de vous assurer que vous êtes connecté sur le site afin que le stock disponible soit affiché. Si l'call est toujours affiché et vous avez besoin d'aide, s'il vous plaît appelez-nous au 01 45 14 89 12.
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