132 Results for: "csn"

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

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognises 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonising the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

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

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognises 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonising the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: Bioss

Metalloprotease that specifically cleaves 'Lys-63'-linked polyubiquitin chains. Does not have activity toward 'Lys-48'-linked polyubiquitin chains. Component of the BRCA1-A complex, a complex that specifically recognizes 'Lys-63'-linked ubiquitinated histones H2A and H2AX at DNA lesions sites, leading to target the BRCA1-BARD1 heterodimer to sites of DNA damage at double-strand breaks (DSBs). In the BRCA1-A complex, it specifically removes 'Lys-63'-linked ubiquitin on histones H2A and H2AX, antagonizing the RNF8-dependent ubiquitination at double-strand breaks (DSBs). Catalytic subunit of the BRISC complex, a multiprotein complex that specifically cleaves 'Lys-63'-linked ubiquitin in various substrates. Mediates the specific 'Lys-63'-specific deubiquitination associated with the COP9 signalosome complex (CSN), via the interaction of the BRISC complex with the CSN complex.

Supplier: JiPo

Porcelain, for desiccators acc. DIN and CSN.

Supplier: Abcam

Rabbit monoclonal [3F9] to COPS3/CSN3.

Supplier: ProSci Inc.

COPS2 is an essential component of the COP9 signalosome complex (CSN). The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively. COPS2 is involved in early stage of neuronal differentiation via its interaction with NIF3L1.

Supplier: ProSci Inc.

CSN8 Antibody: The COP9 signalosome (CSN) is an evolutionarily conserved protein complex of the eight subunits that interacts with deubiquitinating enzymes and protein kinases and is highly homologous to the lid sub-complex of 26S proteasome. The CSN complex is an essential regulator of 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-comlpexes such as SCF, CSA or DDB2. It is also involved in phosphorylation of p53, c-jun/JUN, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN8 encodes the smallest and the least conserved but first identified subunit of CSN. Recent studies show CSN8 is essential for Drosophila development and is essential for peripheral T cell homeostasis and antigen receptor-induced entry into the cell cycle from quiescence.

Supplier: ProSci Inc.

Component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes, leading to decrease the Ubl ligase activity of SCF-type complexes such as SCF, CSA or DDB2. The complex is also involved in phosphorylation of p53/TP53, JUN, I-kappa-B-alpha/NFKBIA, ITPK1 and IRF8/ICSBP, possibly via its association with CK2 and PKD kinases. CSN-dependent phosphorylation of TP53 and JUN promotes and protects degradation by the Ubl system, respectively.

Supplier: ProSci Inc.

COPS2 is an essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP. COPS2 is also innvolved in early stage of neuronal differentiation via its interaction with NIF3L1.

Supplier: ProSci Inc.

COPS2 is an essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/Ion ChannelSBP. COPS2 is also innvolved in early stage of neuronal differentiation via its interaction with NIF3L1.

Supplier: ProSci Inc.

COPS2 is an essential component of the COP9 signalosome complex (CSN), a complex involved in various cellular and developmental processes. The CSN complex is an essential regulator of the ubiquitin (Ubl) conjugation pathway by mediating the deneddylation of the cullin subunits of SCF-type E3 ligase complexes. The complex is also involved in phosphorylation of p53/TP53, c-jun/JUN, IkappaBalpha/NFKBIA, ITPK1 and IRF8/ICSBP. COPS2 is also innvolved in early stage of neuronal differentiation via its interaction with NIF3L1.

Supplier: Abcam

Rabbit monoclonal [EPR6463] to CSN7A - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR5139] to CSN8 - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR7453] to CSN4 - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR6465] to CSN7b - BSA and Azide free.

Supplier: Abcam

Rabbit monoclonal [EPR6464] to CSN7b - BSA and Azide free.