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anti-Human CAND1 Anticorps:
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Human Polyclonal CAND1 Primary Antibody pour ELISA, IHC - ABIN4359844
Liu, Furukawa, Matsumoto, Xiong: NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. dans Molecular cell 2002
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Human Polyclonal CAND1 Primary Antibody pour EIA, IP - ABIN117944
Concejero, Chen, Wang, Wang, Lin, Liu, Yang, Yong, Lin, Jawan, Huang, Cheng, Eng: Living donor liver transplantation for hepatocellular carcinoma: a single-center experience in Taiwan. dans Transplantation 2008
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Human Polyclonal CAND1 Primary Antibody pour EIA, IP - ABIN117945
Feng, Shen, Sullivan, Rubio, Xiong, Sun, Deng: Arabidopsis CAND1, an unmodified CUL1-interacting protein, is involved in multiple developmental pathways controlled by ubiquitin/proteasome-mediated protein Degradation. dans The Plant cell 2004
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Human Monoclonal CAND1 Primary Antibody pour IF, IHC (p) - ABIN565932
Korzeniewski, Hohenfellner, Duensing: CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer. dans Neoplasia (New York, N.Y.) 2012
miR-33a and CAND1 played an important role in lung cancer proliferation and cell migration
describe the identification of the structural determinants responsible for the CA IX/CAND1 interaction
Data show that the differentiation of LiSa-2 preadipocytes is associated with an increase of cullin-associated and neddylation-dissociated 1 (CAND1), COP9 signalosome (CSN), neddylated cullin 3 (Cul3) and the BTB protein Keap1.
The Epstein-Barr virus protein BPLF1, is targeted to cullin-RING ubiquitin ligases (CRLs) via the interaction of the conserved helix-2 with helix-23 of cullins, at a site involved in electrostatic interaction with CAND1.
We demonstrate that the accumulation of p27 is associated with an increase of CAND1 and a decrease of Skp2 during adipogenesis of human LiSa-2 preadipocytes. CAND1 knockdown reduces p27 and blocks adipogenesis.
Study shows that Cand1 can unambiguously stimulate SCF activity in vitro by enabling an F box protein-Skp1 complex to access Cul1 that was previously occupied by a different F box protein-Skp1 complex, and that Cand1 promotes assembly in vivo of new F box proteins with pre-existing Cul1 molecules.
CAND1 promotes PLK4-mediated centriole overduplication and is frequently disrupted in prostate cancer.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
COMMD1 (copper metabolism MURR1 domain-containing protein 1) regulates Cullin RING ligases by preventing CAND1 (Cullin-associated Nedd8-dissociated protein 1) binding.
CAND1 does not function by sequestering cullins in vivo to prevent substrate receptor autoubiquitination and is likely to regulate cullin RING ligase activity via alternative mechanisms
miR-148a is an androgen-responsive microRNA that promotes LNCaP prostate cell growth by repressing its target CAND1 expression.
selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation
binds to unneddylated CUL1 and regulates the formation of SCF ubiquitin E3 ligase complex
TIP120A functions as a negative regulator of SCF E3 ubiquitin ligases and may modulate other cullin ligases in a similar fashion.
CAND1 & COP9 signalosome (CSN), major deneddylase of cullins, bind to unneddylated CUL1 in mutually exclusive way. Suppression of CAND1 expression by siRNA enhanced interaction between CUL1 & CSN, suggesting that CAND1 inhibited binding of CSN to CUL1.
SCCRO recruits Ubc12 approximately NEDD8 to the CAND1-Cul1-ROC1 complex but that this is not sufficient to dissociate or overcome the inhibitory effects of CAND1 on cullin neddylation
HVE/CAND1 gene acts upstream of ATHB-8 at least in higher order veins, in a pathway that involves AXR1, but not LOP1, PIN1, CVP1 or CVP2.
The disruption of the CAND1-CUL1 interaction results in an increased abundance of assembled SCF(TIR1) complex; stabilization of the CAND1-CUL1 interaction diminishes SCF(TIR1) complex abundance.
the adaptive exchange hypothesis, which posits that regulation of the koff of an FBP from SCF by the actions of substrate, Nedd8, and Cand1 molds the cellular repertoire of SCF complexes and that the plasticity afforded by this exchange mechanism may enable large variations in FBP expression during development and in FBP gene number during evolution.
Enhances transcription from various types of promoters. Regulatory protein that interferes with the assembly of the SCF (SKP1-CUL1-F-box protein) ubiquitin ligase complex and thereby down-regulates ubiquitination of target proteins. Prevents neddylation of CUL1 by physically blocking access to the neddylation site. Disrupts interactions between CUL1 and SKP1 and between CUL1 and F-box proteins (By similarity).
TBP interacting protein
, TBP-interacting protein 120A
, TBP-interacting protein of 120 kDa A
, cullin-associated NEDD8-dissociated protein 1
, cullin-associated and neddylation-dissociated protein 1
, p120 CAND1
, TBP-interacting protein TIP120A
, cullin associated and neddylation disassociated 1
, cullin-associated and neddylation-dissociated 1
, TIP120 protein
, cullin-associated NEDD8-dissociated protein 1-like
, cullin-associated and neddylation-dissociated 2 (putative)
, TBP-interacting protein