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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. Additionally we are shipping STIP1 Homology and U-Box Containing Protein 1 Proteins (20) and STIP1 Homology and U-Box Containing Protein 1 Kits (10) and many more products for this protein.
Showing 10 out of 108 products:
Human Polyclonal STUB1 Primary Antibody for EIA, IHC (p) - ABIN359012
Peng, Morishima, Jenkins, Dunbar, Lau, Patterson, Pratt, Osawa: Ubiquitylation of neuronal nitric-oxide synthase by CHIP, a chaperone-dependent E3 ligase. in The Journal of biological chemistry 2004
Show all 10 references for ABIN359012
Human Polyclonal STUB1 Primary Antibody for EIA, FACS - ABIN954992
Stankiewicz, Nikolay, Rybin, Mayer: CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates. in The FEBS journal 2010
Show all 3 references for ABIN954992
Human Polyclonal STUB1 Primary Antibody for IP, PLA - ABIN262267
Tsvetkov, Adamovich, Elliott, Shaul: E3 ligase STUB1/CHIP regulates NAD(P)H:quinone oxidoreductase 1 (NQO1) accumulation in aged brain, a process impaired in certain Alzheimer disease patients. in The Journal of biological chemistry 2011
Show all 2 references for ABIN262267
Cow (Bovine) Polyclonal STUB1 Primary Antibody for EIA, WB - ABIN374173
Jiang, Ballinger, Wu, Dai, Cyr, Höhfeld, Patterson: CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation. in The Journal of biological chemistry 2001
Chicken Polyclonal STUB1 Primary Antibody for IHC, WB - ABIN2774916
Parsons, Tait, Finch, Dianova, Allinson, Dianov: CHIP-mediated degradation and DNA damage-dependent stabilization regulate base excision repair proteins. in Molecular cell 2008
Through selective degradation of Clp subunits, AtCHIP could positively regulate homeostasis of Clp proteolytic subunits and maximize the production of functional chloroplasts. Similar results were obtained from transgenic tobacco plants.
we propose that CHIP and NBR1 (show NBR1 Antibodies) mediate two distinct but complementary anti-proteotoxic pathways and protein's propensity to aggregate under stress conditions is one of the critical factors for pathway selection of protein degradation
Hsc70-4 and CHIP were highly induced in ppi2 mutant plants, where they mediated the degradation of chloroplast-targeted precursors through the ubiquitin-26S proteasome (show Psmd4 Antibodies) system.
AtCHIP, an E3 ubiquitin liagase, functions upstream of protein phosphatase 2A in stress-responsive signal transduction pathways under conditions of low temperature or in the dark. [AtCHIP]
The interaction of CHIP with FtsH1 in vitro, in normal and in CHIP-over-expressing plants is reported.
PABPN1 (show PABPN1 Antibodies) interacts with and is stabilized by heat shock protein 90 (show HSP90 Antibodies).
CHIP targets Osx (show SP7 Antibodies) for ubiquitination and degradation in osteoblasts after chronic exposure to TNF-alpha (show TNF Antibodies).
CHIP/TRAF3 (show TRAF3 Antibodies)/NIK (show MAP4K4 Antibodies) interactions recruit NIK (show MAP4K4 Antibodies) to E3 ligase complexes for ubiquitination and degradation, thus maintaining NIK (show MAP4K4 Antibodies) at low levels
Cbl-b, together with Stub1, ubiquitinate Foxp3 (show FOXP3 Antibodies), and regulate tTreg development.
CHIP regulates the levels of FMR1 (show FMR1 Antibodies) as an E3 ubiquitin ligase (show MUL1 Antibodies) in phosphorylation-dependent manner, suggesting that CHIP regulates FMR1 (show FMR1 Antibodies)-mediated translational repression by regulating the levels of FMR1 (show FMR1 Antibodies).
The cardiac CHIP appears to play a role in regulating autophagy during the development of cardiac hypertrophy, possibly by its role in supporting Akt (show AKT1 Antibodies) signalling, induced by voluntary running in vivo.
Ebp1 (show NFKB1 Antibodies) p42 (show EPB42 Antibodies) isoform regulates the proteasomal degradation of the p85 (show ECM1 Antibodies) regulatory subunit of PI3K by recruiting a chaperone-E3 ligase complex HSP70 (show HSP70 Antibodies)/CHIP.
CHIP as a novel causative gene for autosomal recessive cerebellar ataxia (show USP14 Antibodies)
CHIP inhibits NF-kappaB (show NFKB1 Antibodies) signaling by promoting TRAF6 (show TRAF6 Antibodies) degradation and plays an important role in osteoclastogenesis and bone remodeling.
regulation of IL-4 (show IL4 Antibodies) receptor signaling in lung inflammation
Cdk5 (show CDK5 Antibodies)-mediated phosphorylation of CHIP negatively regulates its neuroprotective function, thereby contributing to neuronal cell death progression following neurotoxic stimuli.
CHIP is a bona fide negative regulator of the RIPK1 (show RIPK1 Antibodies)-RIPK3 (show RIPK3 Antibodies) necrosome formation leading to desensitization of TNF (show TNF Antibodies)-mediated necroptosis
Protein-protein interactions modulate the docking-dependent E3-ubiquitin ligase (show MUL1 Antibodies) activity of CHIP.
Data show that the E3 ubiquitin ligase (show MUL1 Antibodies) CHIP interacts with protein arginine methyltransferase-5 (PRMT5 (show PRMT5 Antibodies)) both in vivo and in vitro.
These results indicate that CHIP decreases the Kv1.5 (show KCNA5 Antibodies) protein level and functional channel by facilitating its degradation in concert with chaperone Hsc70 (show HSPA8 Antibodies)
detailed and systematic investigation to characterize if there are significant differences in the CHIP in vitro ubiquitination of human Hsp70 (show HSP70 Antibodies) and Hsc70 (show HSPA8 Antibodies).
CHIP stabilizes amyloid precursor protein (show APP Antibodies) via proteasomal degradation and p53 (show TP53 Antibodies)-mediated trans-repression of BACE1 (show BACE Antibodies).
Our findings demonstrate for the first time that CHIP may be involved in RCC (show XRCC1 Antibodies) angiogenesis through regulating VEGF (show VEGFA Antibodies) secretion and expression of VEGFR2 (show KDR Antibodies).
results indicate that the post-endocytic ubiquitination of CFTR (show CFTR Antibodies) by CHIP is a critical step in the peripheral quality control of cell surface DeltaF508 CFTR (show CFTR Antibodies)
CHIP docks onto Hsp70/Hsc70 and defines a bipartite mode of interaction between TPR domains and their binding partners.
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
STIP1 homology and U-box containing protein 1
, STIP1 homology and U box-containing protein 1
, E3 ubiquitin-protein ligase CHIP
, carboxy terminus of Hsp70-interacting protein
, CLL-associated antigen KW-8
, antigen NY-CO-7
, heat shock protein A binding protein 2 (c-terminal)
, serologically defined colon cancer antigen 7
, STIP1 homology and U-Box containing protein 1