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Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1\; MIM 601912), are structurally related to ubiquitin (MIM 191339) and can be ligated to target proteins in a similar manner as ubiquitin. Zusätzlich bieten wir Ihnen SENP6 Proteine (3) und viele weitere Produktgruppen zu diesem Protein an.
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Human Polyclonal SENP6 Primary Antibody für IHC (p), WB - ABIN388052
Ota, Suzuki, Nishikawa, Otsuki, Sugiyama, Irie, Wakamatsu, Hayashi, Sato, Nagai, Kimura, Makita, Sekine, Obayashi, Nishi, Shibahara, Tanaka, Ishii, Yamamoto, Saito, Kawai, Isono, Nakamura, Nagahari et al.: Complete sequencing and characterization of 21,243 full-length human cDNAs. ... in Nature genetics 2003
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Human Monoclonal SENP6 Primary Antibody für IHC (p), ELISA - ABIN565219
Dou, Huang, Singh, Carpenter, Yeh: Regulation of DNA repair through deSUMOylation and SUMOylation of replication protein A complex. in Molecular cell 2010
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Dog (Canine) Polyclonal SENP6 Primary Antibody für ELISA - ABIN250012
Kim, Baek, Jeon, Nishimori, Suzuki, Uchida, Shimbara, Saitoh, Tanaka, Chung: A new SUMO-1-specific protease, SUSP1, that is highly expressed in reproductive organs. in The Journal of biological chemistry 2000
Human Polyclonal SENP6 Primary Antibody für ELISA, WB - ABIN314340
Choi, Chung, Rho, Lee, Lee, Choi, Seol, Baek, Bang, Chung: Negative modulation of RXRalpha transcriptional activity by small ubiquitin-related modifier (SUMO) modification and its reversal by SUMO-specific protease SUSP1. in The Journal of biological chemistry 2006
Negative regulation of TLR inflammatory signaling by the SUMO-deconjugating enzyme SENP6.
LANA could bind to the promoter region of the SENP6 gene and inhibit SENP6 expression while the regulated SENP6 could in turn modulate the abundance of LANA through desumoylation.
the structure of SENP2 (zeige SUMO1 Antikörper)-Loop1 in complex with SUMO2 (zeige SUMO2 Antikörper) was solved at 2.15 A resolution, and reveals the details of an interface exclusive to SENP6/7 and the formation of unique contacts between both proteins
Loop 1 insertion in SENP6 and SENP7 as a platform to discriminate between SUMO1 and SUMO2/3 isoforms in this subclass of the SUMO protease family.
study of substrate specificity of SENP6; it is also capable of cleaving mixed chains of SUMO-1 (zeige SUMO1 Antikörper) and SUMO-2 (zeige SUMO2 Antikörper)/3; mutation of catalytic cysteine of results in its accumulation in PML (zeige PML Antikörper) NBs (zeige NBN Antikörper); findings indicate SUMO-modified PML (zeige PML Antikörper) is a substrate of SENP6
Results reveal a novel mechanism whereby the finely balanced activities of SENP6 and RNF4 control vertebrate kinetochore assembly through SUMO-targeted destabilization of inner plate components.
SENP1 (zeige SENP1 Antikörper) localization is influenced by expression and localization of SUMO-1 (zeige SUMO1 Antikörper)-conjugated target proteins within the cell.
SUSP1 plays an important role in the control of the transcriptional activity of RXRalpha (zeige RXRA Antikörper) and thus in the RXRalpha (zeige RXRA Antikörper)-mediated cellular processes
We have investigated the specificity of SUSP1 using vinyl sulfone inhibitors and model substrates. SUSP1 has a strong paralogue bias toward SUMO2 (zeige SUMO2 Antikörper)/3 and acts preferentially on substrates containing three or more SUMO2 (zeige SUMO2 Antikörper)/3 moieties
SENP6 and SENP7 exhibit lower rates for processing pre-SUMO1, pre-SUMO2, or pre-SUMO3 in comparison with SENP2
Ubiquitin-like molecules (UBLs), such as SUMO1 (UBL1\; MIM 601912), are structurally related to ubiquitin (MIM 191339) and can be ligated to target proteins in a similar manner as ubiquitin. However, covalent attachment of UBLs does not result in degradation of the modified proteins. SUMO1 modification is implicated in the targeting of RANGAP1 (MIM 602362) to the nuclear pore complex, as well as in stabilization of I-kappa-B-alpha (NFKBIA\; MIM 164008) from degradation by the 26S proteasome. Like ubiquitin, UBLs are synthesized as precursor proteins, with 1 or more amino acids following the C-terminal glycine-glycine residues of the mature UBL protein. Thus, the tail sequences of the UBL precursors need to be removed by UBL-specific proteases, such as SENP6, prior to their conjugation to target proteins (Kim et al., 2000
SUMO1/sentrin specific peptidase 6
, SUMO1/sentrin specific protease 6
, SUMO-1-specific protease 1
, SUMO/sentrin specific protease 6
, sentrin-specific protease 6
, sentrin/SUMO-specific protease SENP6
, SUMO/sentrin specific peptidase 6
, Sumo1/sentrin/SMT3 specific peptidase 6