1009 Results for: "Ba\u0148ky+hru\u0161kovit\u00E9"

Supplier: Bioss

The complement component proteins, C3, C4 and C5, are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Complement Factor B, also designated Properdin Factor B or PBF2, is part of the alternate pathway of the complement system and is cleaved by Factor D into two fragments: Ba and Bb. Bb combines with complement Factor 3b to produce the C3 or C5 convertase and plays a role in the differentiation and proliferation of preactivated B lymphocytes, lysis of erythrocytes, stimulation of lymphocyte blastogenesis and rapid spreading of peripheral blood monocytes. Ba is important in inhibiting the proliferation of preactivated B lymphocytes. Adipsin, also designated complement Factor D, is a serine protease that cleaves complement Factor B and may be involved in obesity. Factor H controls the function of the alternative complement pathway. FHR-1 (complement Factor H related protein 1) may play a role in lipid metabolism.

Supplier: Bioss

The complement component proteins, C3, C4 and C5, are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Complement Factor B, also designated Properdin Factor B or PBF2, is part of the alternate pathway of the complement system and is cleaved by Factor D into two fragments: Ba and Bb. Bb combines with complement Factor 3b to produce the C3 or C5 convertase and plays a role in the differentiation and proliferation of preactivated B lymphocytes, lysis of erythrocytes, stimulation of lymphocyte blastogenesis and rapid spreading of peripheral blood monocytes. Ba is important in inhibiting the proliferation of preactivated B lymphocytes. Adipsin, also designated complement Factor D, is a serine protease that cleaves complement Factor B and may be involved in obesity. Factor H controls the function of the alternative complement pathway. FHR-1 (complement Factor H related protein 1) may play a role in lipid metabolism.

Supplier: Bioss

The complement component proteins, C3, C4 and C5, are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Complement Factor B, also designated Properdin Factor B or PBF2, is part of the alternate pathway of the complement system and is cleaved by Factor D into two fragments: Ba and Bb. Bb combines with complement Factor 3b to produce the C3 or C5 convertase and plays a role in the differentiation and proliferation of preactivated B lymphocytes, lysis of erythrocytes, stimulation of lymphocyte blastogenesis and rapid spreading of peripheral blood monocytes. Ba is important in inhibiting the proliferation of preactivated B lymphocytes. Adipsin, also designated complement Factor D, is a serine protease that cleaves complement Factor B and may be involved in obesity. Factor H controls the function of the alternative complement pathway. FHR-1 (complement Factor H related protein 1) may play a role in lipid metabolism.

Supplier: Bioss

The complement component proteins, C3, C4 and C5, are potent anaphylatoxins that are released during complement activation. Binding of these proteins to their respective G protein-coupled receptors, C3aR, C1R and C5aR, induces proinflammatory events, such as cellular degranulation, smooth muscle contraction, arachidonic acid metabolism, cytokine release, leukocyte activation and cellular chemotaxis. Complement Factor B, also designated Properdin Factor B or PBF2, is part of the alternate pathway of the complement system and is cleaved by Factor D into two fragments: Ba and Bb. Bb combines with complement Factor 3b to produce the C3 or C5 convertase and plays a role in the differentiation and proliferation of preactivated B lymphocytes, lysis of erythrocytes, stimulation of lymphocyte blastogenesis and rapid spreading of peripheral blood monocytes. Ba is important in inhibiting the proliferation of preactivated B lymphocytes. Adipsin, also designated complement Factor D, is a serine protease that cleaves complement Factor B and may be involved in obesity. Factor H controls the function of the alternative complement pathway. FHR-1 (complement Factor H related protein 1) may play a role in lipid metabolism.

Supplier: VWR Collection

12 COMPOSES DANS HCL 1% Ba 100mg/l Be 10mg/l Bi 100mg/l Mo 100mg/l Pt 100mg/l Sb 100mg/l Sn 100mg/l Te 100mg/l V 100mg/l In 100mg/l Ti 100mg/l Pd 100mg/l in HF traces 1 * 100 ml

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

Ubiquitin is an abundant, highly conserved protein found in all eukaryotic cells either free or covalently attached to cellular proteins. The primary function of ubiquitin in mammalian systems is to clear abnormal, foreign, and improperly folded proteins by targeting them for proteosome degradation. UBE2D proteins, including UBE2D1 (ubiquitin-conjugating enzyme E2D1 or UBC5A), UBE2D2 (ubiquitin-conjugating enzyme E2D2 or UBC5B) and UBE2D3 (ubiquitin-conjugating enzyme E2D3 or UBC5C), are E2 ubiquitin-conjugating enzymes that catalyze the ubiquitination of I˚Bå in a phosphorylation and SCFB-TRCP-dependent manner. Specifically, E1 first transfers a ubiquitin residue to the E2 component (a UBE2D protein), and the UBE2D protein then associates with an E3 ubiquitin-protein ligase, which immediately transfers that residue to a protein that is targeted for degradation.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: ERLAB CAPTAIRE

Model technology: Filtration ductless fume hood Captair 392 Smart Filters configuration: 1P1C1P Additional options: light button Ba ck panel: standard Front and Side panel: sequential opening + left waste port Power supply: CH Version: 1 1 * 1 items

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: ERLAB CAPTAIRE

Model technology: Filtration ductless fume hood Captair 633 Smart Filters configuration: 1P1C1P Additional options: light button Ba ck panel: standard Front and Side panel: sequential opening + left waste port Power supply: CH Version: 1 1 * 1 items

Supplier: ERLAB CAPTAIRE

Model technology: Filtration ductless fume hood Captair 483 Smart Filters configuration: 1P1C1P Additional options: light button Ba ck panel: transparent Front and Side panel: sequential opening + right waste port Power supply: CH Version: 1 1 * 1 items

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.

Supplier: Bioss

The COP9 signalosome (CSN) complex is involved in several different developmental and cellular processes. The complex is made up of several widely expressed proteins: CSN1 (COPS1), CSN2 (COPS2), CSN3 (COPS3), CSN4 (COPS4), CSN5 (COPS5), CSN6 (COP6), CSN7a (COPS7, COPS7a) or CSN7b (COP7b) and CSN8 (COP8). The CSN complex acts as a regulator for the ubiquitin conjugation pathway by mediating the deneddylation of the SCF-type E3 ligase complexes, which leads to a decrease in ubiquitin ligase activity of SCF-complexes. It is also involved in the phosphorylation of p53, c-Jun, I˚Bå and IRF-8, as well as CSN-dependent phosphorylation of p53, and c-Jun protects and promotes degradation by the Ubl system. CSN7 is phosphorylated by CK2 and is composed of two subunits; a and b. CSN7a contains a PCI (Proteasome CSN9 initiation factor 3) region, as well as a coiled-coil region and is predicted to interact with CSN2, CSN3, CSN4, CSN5, CSN6, CSN8, and GPS1. CSN7b contains only a PCI region and is predicted to interact with INT6.