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SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. Additionally we are shipping SUMO2 Proteins (33) and SUMO2 Kits (10) and many more products for this protein.
Showing 10 out of 218 products:
Human Polyclonal SUMO2 Primary Antibody for IHC (p), WB - ABIN388085
Mori, Miki, Tanji, Ogura, Yagihashi, Jensen, Wakabayashi: Incipient intranuclear inclusion body disease in a 78-year-old woman. in Neuropathology : official journal of the Japanese Society of Neuropathology 2011
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Human Monoclonal SUMO2 Primary Antibody for - ABIN1449280
Fernández-Miranda, Pérez de Castro, Carmena, Aguirre-Portolés, Ruchaud, Fant, Montoya, Earnshaw, Malumbres: SUMOylation modulates the function of Aurora-B kinase. in Journal of cell science 2010
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Human Monoclonal SUMO2 Primary Antibody for WB - ABIN1882280
Xu, Au: Mapping residues of SUMO precursors essential in differential maturation by SUMO-specific protease, SENP1. in The Biochemical journal 2005
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Human Polyclonal SUMO2 Primary Antibody for EIA, IHC (p) - ABIN356794
Zhang, Sarge: Sumoylation regulates lamin A function and is lost in lamin A mutants associated with familial cardiomyopathies. in The Journal of cell biology 2008
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Human Polyclonal SUMO2 Primary Antibody for EIA, WB - ABIN356737
Mannen, Tseng, Cho, Li: Cloning and expression of human homolog HSMT3 to yeast SMT3 suppressor of MIF2 mutations in a centromere protein gene. in Biochemical and biophysical research communications 1996
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Human Monoclonal SUMO2 Primary Antibody for EIA, IF - ABIN492386
Ii, Mullen, Slagle, Brill: Stimulation of in vitro sumoylation by Slx5-Slx8: evidence for a functional interaction with the SUMO pathway. in DNA repair 2007
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Xenopus laevis Polyclonal SUMO2 Primary Antibody for WB - ABIN650620
Keane, Ettenberg, Nau, Banerjee, Cuello, Penninger, Lipkowitz: cbl-3: a new mammalian cbl family protein. in Oncogene 1999
Show all 2 references for ABIN650620
Human Polyclonal SUMO2 Primary Antibody for EIA, WB - ABIN783834
Kamitani, Kito, Nguyen, Fukuda-Kamitani, Yeh: Characterization of a second member of the sentrin family of ubiquitin-like proteins. in The Journal of biological chemistry 1998
The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation.
This study demonstrated that two polymorphisms of SUMO2 were significantly associated with an increased risk of AD in female group.
FOXP2 (show FOXP2 Antibodies) can be modified with all three human SUMO proteins and that PIAS1 (show PIAS1 Antibodies) promotes this process.
Hsp27-Ubc9 pathway recognizes the conformation of mutant CFTR which leads to its SUMO-2 conjugation and degradation by the ubiquitin-proteasome system.
Data suggest that RAP80 (show UIMC1 Antibodies) SIM (show SIM2 Antibodies) (SUMO interacting motif) binds SUMO-2; both specificity and affinity are enhanced through phosphorylation of canonical CK2 (show CSNK2A1 Antibodies) (casein kinase 2) site within the SIM (show SIM2 Antibodies).
Small ubiquitin-related modifier 2/3 interacts with p65 (show GORASP1 Antibodies) and stabilizes it in the cytoplasm in HBV-associated hepatocellular carcinoma.
Data show that substantial increases in the binding of small ubiquitin-like modifier 2 (SUMO-2) to active DNA regulatory elements in response to heat stress.
Data suggest that small ubiquitin-related modifier protein SUMO1 (show SUMO1 Antibodies) modification of the promyelocytic leukemia protein (PML (show PML Antibodies)) RING domain promotes SUMO2 conjugation to Lys160.
present a comprehensive proteomic analysis of changes in the cellular SUMO2 proteome during HSV-1 infection
Genome-wide analysis of sumoylation dynamics in response to replication stress reveals novel SUMO-2 modified target proteins and acceptor lysines relevant for genome stability.
cyclin E (show CCNE1 Antibodies) is dynamically and highly conjugated to SUMO2/3 on chromatin, independently of Cdk2 (show CDK2 Antibodies) activity and origin activation.
we provide evidence for the existence of a preferential conjugation of AtSUMO1/2 compared with AtSUMO3/5, which is determined by a role of the E1-activating enzyme in SUMO paralogue discrimination.
SUM3 (show SUMO3 Antibodies) promotes plant defense downstream of salicylic acid, while SUM1 (show SUMO1 Antibodies) and SUM2 together prevent salicylic acid accumulation in noninfected plants.
SIZ1-mediated conjugation of SUMO1 (show SUMO1 Antibodies) and SUMO2 to other intracellular proteins is essential in Arabidopsis, possibly through stress-induced modification of a potentially diverse pool of nuclear proteins.
SUMO-2 inhibits aggregation of CPEB3 (show CPEB3 Antibodies).
The present study used immunohistochemical and immunoblot analysis with the different developmental stages of mice and demonstrated the developmentally regulated distribution of SUMO2/3 in the brain.
SUMO-2-Tg mouse lines exhibited cardiomyopathy with various severities. SUMO-2 directly regulated apoptosis by at least partially targeting calpain 2 (show CAPN2 Antibodies) and calpastatin (show CAST Antibodies).
Results indicate that a functional SUMO1 (show SUMO1 Antibodies)-3 expression is essential for emotionality and cognition
Expression levels and not functional differences between SUMO2 and SUMO3 (show SUMO3 Antibodies) are critical for normal embryogenesis.
Stress-induced phosphorylation of Thr486 in c-Myb (show MYB Antibodies) by p38 (show CRK Antibodies) mitogen-activated protein kinases attenuates conjugation of SUMO-2/3.
post-ischemic activation of SUMO2/3 conjugation may define the fate of neurons exposed to a transient interruption of blood supply
Alterations in SUMO substrate conjugation may occur and global posttranslational modifications by ubiquitin may play an important role in the mechanisms underlying Alzheimer disease.
activation of SUMO2/3 conjugation is an endogenous neuroprotective stress response.
These results indicate that the functional role of SUMO-2/3 in the regulation of NFkappaB activity was conserved during evolution.
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002
SMT3 suppressor of mif two 3 homolog 2 (S. cerevisiae)
, small ubiquitin-related modifier 2
, SMT3 homolog 2
, SMT3 suppressor of mif two 3 homolog 2
, sentrin 2
, ubiquitin-like protein SMT3A
, ubiquitin-like protein SMT3B
, small ubiquitin-related modifier 2-B
, SMT3 homolog 1
, SMT3 suppressor of mif two 3 homolog 1
, SMT3 suppressor of mif two 3 homolog 3
, small ubiquitin-related modifier 3
, MIF2 suppressor
, SMT3 supressor of mif two 3 homolog 2