Sie suchten nach: Fmoc-val-OSu

Artikel-Nr: (BOSSBS-1271R-HRP)

Lieferant: Bioss

Beschreibung: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-CY5.5)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-CY5)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-1271R-A750)

Lieferant: Bioss

Beschreibung: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-1271R-A350)

Lieferant: Bioss

Beschreibung: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-A750)

Lieferant: Bioss

Beschreibung: 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. Hydrolyses the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC. Likely target for the cowpox virus CRMA death inhibitory protein.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-13390R-FITC)

Lieferant: Bioss

Beschreibung: GLUD2 is both mitochondrial matrix enzymes belonging to the Glu/Leu/Phe/Val dehydrogenases family. Exisiting as homohexamers, GLUD1 catalyzes the oxidative deamination of glutamate to ?ketoglutarate and ammonia while GLUD2 is involved in the recycling of glutamate during neurotransmission. GLUD1 is critical for regulating amino acid induced insulin secretion and is allosterically activated by ADP and inhibited by GTP and ATP. Mutations in the gene encoding GLUD1 causes hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 may also be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. GLUD2 is expressed in testis and retina, with lower levels found in brain.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-13390R-A488)

Lieferant: Bioss

Beschreibung: GLUD2 is both mitochondrial matrix enzymes belonging to the Glu/Leu/Phe/Val dehydrogenases family. Exisiting as homohexamers, GLUD1 catalyzes the oxidative deamination of glutamate to ?ketoglutarate and ammonia while GLUD2 is involved in the recycling of glutamate during neurotransmission. GLUD1 is critical for regulating amino acid induced insulin secretion and is allosterically activated by ADP and inhibited by GTP and ATP. Mutations in the gene encoding GLUD1 causes hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 may also be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. GLUD2 is expressed in testis and retina, with lower levels found in brain.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-13390R-A350)

Lieferant: Bioss

Beschreibung: GLUD2 is both mitochondrial matrix enzymes belonging to the Glu/Leu/Phe/Val dehydrogenases family. Exisiting as homohexamers, GLUD1 catalyzes the oxidative deamination of glutamate to ?ketoglutarate and ammonia while GLUD2 is involved in the recycling of glutamate during neurotransmission. GLUD1 is critical for regulating amino acid induced insulin secretion and is allosterically activated by ADP and inhibited by GTP and ATP. Mutations in the gene encoding GLUD1 causes hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 may also be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. GLUD2 is expressed in testis and retina, with lower levels found in brain.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-CY7)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-1271R-A555)

Lieferant: Bioss

Beschreibung: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-1271R-CY7)

Lieferant: Bioss

Beschreibung: Serine protease that shows proteolytic activity against a non-specific substrate beta-casein. Promotes or induces cell death either by direct binding to and inhibition of BIRC proteins(also called inhibitor of apoptosis proteins, IAPs), leading to an increase in caspase activity, or by a BIRC inhibition-independent, caspase-independent and serine protease activity-dependent mechanism. Isoform 2 seems to be proteolytically inactive. [CATALYTIC ACTIVITY] Cleavage of non-polar aliphatic amino-acids at the P1 position, with a preference for Val, Ile and Met. At the P2 and P3 positions, Arg is selected most strongly with a secondary preference for other hydrophilic residues. [SUBUNIT] Homotrimer. Interacts with MXI2. The mature protein, but not the precursor, binds to BIRC2, BIRC3 and XIAP.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-13390R-A555)

Lieferant: Bioss

Beschreibung: GLUD2 is both mitochondrial matrix enzymes belonging to the Glu/Leu/Phe/Val dehydrogenases family. Exisiting as homohexamers, GLUD1 catalyzes the oxidative deamination of glutamate to ?ketoglutarate and ammonia while GLUD2 is involved in the recycling of glutamate during neurotransmission. GLUD1 is critical for regulating amino acid induced insulin secretion and is allosterically activated by ADP and inhibited by GTP and ATP. Mutations in the gene encoding GLUD1 causes hyperinsulinism-hyperammonemia syndrome (HHS), which is an inherited condition characterized by high insulin and ammonia levels in the blood. GLUD1 may also be involved in learning and memory reactions by increasing the turnover of the excitatory neurotransmitter glutamate. GLUD2 is expressed in testis and retina, with lower levels found in brain.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-CY3)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-0052R-FITC)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion

Artikel-Nr: (BOSSBS-6463R-CY7)

Lieferant: Bioss

Beschreibung: 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.

UOM: 1 * 100 µl

Aktion