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Results identified a new role of CHIP in adipocyte differentiation. CHIP interacts with and mediates the ubiquitylation of PPARgamma (show PPARG Proteins) , which results in negative effects on adipogenesis.
The overexpression of CHIP significantly increased the migration and invasion of the DU145 cells, which is possible due to activation of the AKT (show AKT1 Proteins) signaling pathway and upregulation of vimentin (show VIM Proteins). The expression level of CHIP was observed to be increased in human prostate cancer tissues compared with the adjacent normal tissue.
Here the authors show that the mammalian ubiquitin ligase C-terminal Hsp70-interacting protein (CHIP), if freed from chaperones during acute stress, can dock on cellular membranes thus performing a proteostasis sensor function.
These results suggest that in the early response to stressful stimuli, MLK4beta-MLK3 (show MAP3K11 Proteins) binding is important for regulating MLK3 (show MAP3K11 Proteins) activity and MAPK (show MAPK1 Proteins) signalling, and after prolonged periods of stress exposure, MLK4beta and MLK3 (show MAP3K11 Proteins) proteins decline via CHIP-dependent degradation.
Prostate cancer cells expressing an S273A mutant of CHIP have attenuated AR degradation upon 2-ME treatment compared with cells expressing wild-type CHIP, supporting the idea that CHIP phosphorylation by Aurora A (show AURKA Proteins) activates its E3 ligase activity for the AR
PC-1 (show PCSK1 Proteins) works in conjunction with E3 ligase CHIP to regulate androgen receptor (show AR Proteins) stability and activity.
Some STUB1 mutations known to cause spinocerebellar ataxia, autosomal recessive 16 have a profound impact on the protein structure, stability, and ability of CHIP to dimerize in vitro.
These findings provide clinical and imaging support for the notion that CHIP is a crucial converging point of manifold neurodegenerative processes, corresponding with its universal biological function in neurodegeneration and reveal the second STUB1 family with ataxia plus hypogonadism.
the CHIP/CLEC-2 (show CLEC1B Proteins) axis may play an important role in the modulation of immune response.
these findings indicate that the stability of the DDIAS protein is regulated by CHIP/HSP70 (show HSP70 Proteins)-mediated proteasomal degradation and that CHIP overexpression stimulates the apoptosis of lung cancer cells in response to DNA-damaging agents
these results indicate that phosphorylation of CHIP at Ser20 by Cdk5 (show CDK5 Proteins) activation inhibits CHIP-mediated truncated apoptosis-inducing factor (show AIFM1 Proteins) (tAIF) degradation, thereby contributing to tAIF-induced neuronal cell death following rotenone treatment
CHIP was as a master regulator of AQP2 (show AQP2 Proteins) degradation via HSP70 (show HSP70 Proteins) that has dual functions: (1) as chaperone for AQP2 (show AQP2 Proteins) and (2) as an anchoring protein for MDM2 (show MDM2 Proteins) E3 ligase, which is likely to be involved in AQP2 (show AQP2 Proteins) degradation.
Consistent with reduced transcription factor EB (TFEB (show TFEB Proteins)) activity, accumulation of phosphorylated TFEB (show TFEB Proteins) in STUB1-deficient cells resulted in reduced autophagy and reduced mitochondrial biogenesis. These studies reveal that the ubiquitin-proteasome pathway participates in regulating autophagy and lysosomal functions by regulating the activity of TFEB (show TFEB Proteins).
ACR (show ACR Proteins) interacts with proteins that regulate the ubiquitin-proteasome system, predominantly with the E3 ubiquitin-protein ligases Stub1, which binds the NH2 terminus of the ACR (show ACR Proteins), and CRL4(CRBN (show CRBN Proteins)), which is formed by Cul4a (show CUL4A Proteins)/b, Ddb1, and Crbn (show CRBN Proteins), and interacts with the COOH terminus of the ACR (show ACR Proteins) via Crbn (show CRBN Proteins).
The chaperone protein Hsp70 (show HSP70 Proteins) was found to be important for CHIP and NUCB1 (show NUCB1 Proteins) interaction as well as CHIP-mediated NUCB1 (show NUCB1 Proteins) down-regulation.
CHIP is a negative regulator of RIPK1 (show RIPK1 Proteins) and RIPK3 (show RIPK3 Proteins), thus inhibiting necroptosis.
our study demonstrated that over-expressing miR (show MLXIP Proteins)-21 in UCBMSCs could improve neovascularization in Critical limb ischemia (CLI (show CLU Proteins)) through enhancing HIF-1alpha (show HIF1A Proteins) activity by targeting CHIP, which may hold great therapeutic promise in treating CLI (show CLU Proteins)
PABPN1 (show PABPN1 Proteins) interacts with and is stabilized by heat shock protein 90 (show HSP90 Proteins).
CHIP targets Osx (show SP7 Proteins) for ubiquitination and degradation in osteoblasts after chronic exposure to TNF-alpha (show TNF Proteins).
STUB1, or CHIP, is a ubiquitin ligase/cochaperone that participates in protein quality control by targeting a broad range of chaperone protein substrates for degradation (Min et al., 2008
CLL-associated antigen KW-8
, E3 ubiquitin-protein ligase CHIP
, STIP1 homology and U box-containing protein 1
, antigen NY-CO-7
, carboxy terminus of Hsp70-interacting protein
, heat shock protein A binding protein 2 (c-terminal)
, serologically defined colon cancer antigen 7
, STIP1 homology and U-Box containing protein 1
, STIP1 homology and U-box containing protein 1