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anti-Human TAB1 Antikörper:
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Human Polyclonal TAB1 Primary Antibody für IF, WB - ABIN541243
Irie, Muta, Takeshige: TAK1 mediates an activation signal from toll-like receptor(s) to nuclear factor-kappaB in lipopolysaccharide-stimulated macrophages. in FEBS letters 2000
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Human Polyclonal TAB1 Primary Antibody für DB, ELISA - ABIN548637
Singhirunnusorn, Suzuki, Kawasaki, Saiki, Sakurai et al.: Critical roles of threonine 187 phosphorylation in cellular stress-induced rapid and transient activation of transforming growth factor-beta-activated kinase 1 (TAK1) in a signaling complex ... in The Journal of biological chemistry 2005
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Human Monoclonal TAB1 Primary Antibody für ELISA, WB - ABIN532683
Sun, Yoshizuka, New, Moser, Li, Liao, Xie, Chen, Deng, Yamout, Dong, Frangou, Yates, Wright, Han: PRAK is essential for ras-induced senescence and tumor suppression. in Cell 2007
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Silencing of TAB1, but not TAK1, prevented p38MAPK activation, which is indicative of TAB1-mediated autophosphorylation of p38MAPK
Based on the crystal structure of the p38alpha-TAB1 complex authors replaced threonine 185 of p38alpha with glycine (T185G) to prevent an intramolecular hydrogen bond with Asp150 from being formed. This mutation did not interfere with TAB1 binding to p38alpha.
High TAB1 expression is associated with colorectal cancer.
TAB1 was identified as a functional target of miR-134, and the expression of TAB1 was increased by the transcription factors of NF-kappaB1, c-Rel, and ELK1 via miR-134.
we show that IL-1 induces robust p38a activation both in the nucleus and in the cytoplasm/membrane.Following stimulation, p38a activity returns to a basal level in absence of receptor degradation. While nuclear pulse is controlled by MKP1 through a negative feedback to pp38, its basal activity is controlled by both TAB1 and MKP1 through a positive feedback loop.
TAK1/TAB1 expression in non-small cell lung carcinoma tissue is significantly increased and closely associated with patient clinical prognosis.
miR-29a repressed TAB1-mediated TIMP-1 production in dermal fibroblasts, demonstrating that miR-29a may be a therapeutic target in SSc.
Data indicate that mitogen-activated protein kinase (MAPK) p38 activation is triggered by AMP-activated protein kinases (AMPK) and mediated by TAB1 protein.
The amino acid sequence between positions 373 and 502 of TAB1 is required for TP interaction.
USP18 inhibits NF-kappaB and NFAT activation during Th17 differentiation by deubiquitinating the TAK1-TAB1 complex.
We found that endothelial TAK1 and TAB2, but not TAB1, were critically involved in vascular formation
TAK1 plays a critical role in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.
data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression
Phosphorylation and polyubiquitination of TAK1 are necessary for activation of NF-kappaB by the Kaposi's sarcoma-associated herpesvirus vGPCR.
Co-expression of TAK1 and TAB1 resulted in a functional and active TAK1-TAB1 complex capable of directly activating full-length heterotrimeric mammalian AMP-activated protein kinase (AMPK) in vitro.
interaction with p38alpha leads to autophosphorylation and activation of p38alpha
The TAK1-TAB1 fusion protein is a novel constitutively active mitogen-activated protein kinase kinase kinase that stimulates AP-1 and NF-kappaB signaling pathways
TauAlphaBeta1beta is involved in regulating p38alpha activity in physiological conditions
These results suggest that the TAK1-NLK MAPK cascade is activated by the noncanonical Wnt-5a/Ca(2+) pathway and antagonizes canonical Wnt/beta-catenin signaling.
characterized the molecular mechanisms of cellular stress-induced TAK1 activation, focusing mainly on the phosphorylation of TAK1 at Thr-187 and Ser-192 in the activation loop; TAB1 and TAB2 were differentially involved in the phosphorylation of TAK1
our study uncovers that RNF114-mediated ubiquitination and degradation of TAB1 activate the NF-kappaB pathway during MZT, and thus directly link maternal clearance to early embryo development.
We confirmed that PGC-1b inhibited downstream inflammatory signals via binding with TAB1 and thus preventing TAB1/TAK1 binding and TAK1 activation.
The E3 ubiquitin ligase Itch inhibits p38alpha signaling and skin inflammation through the ubiquitylation of Tab1.
TAB1 and TAB2 are required for activated macrophages, making TAB1 and TAB2 effective targets to control inflammation by modulating macrophage survival.
Both the MEKK1 PHD and TAB1 are critical for ES-cell differentiation
The enhanced JNK and IkappaB kinase activation in DUSP14-deficient T cells was attenuated by TAB1 short hairpin RNA knockdown.
TAB1 binding stabilizes active p38alpha and induces rearrangements within the activation segment by helical extension of the Thr-Gly-Tyr motif, allowing autophosphorylation in cis
O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress.
Epithelial TAK1 activity is regulated through two unique, TAB1-dependent basal & TAB2-mediated stimuli-dependent mechanisms.
XIAP-TAB1-TAK1 complex is dependent on NRAGE for IKK-alpha/beta phosphorylation and NF-kappaB activation.
TAB1 plays an important role in mammalian embryogenesis and is required for TAK1 activation in TGF-beta signaling
We propose that TAB1 promotes nitric oxide-induced p38 autophosphorylation. In addition, nitric oxide-induced p38 activation seems to promote JNK inhibition and ERK activation, but this effect appears to not require TAB1.
TAB1alpha, but not TAB1beta, plays an important role in the activation of p38 in insulin-producing cells and therefore also in cytokine-induced beta-cell death.
another MAP3K (MAPK kinase kinase) may mediate the IL-1/TNFalpha-induced activation of these signalling pathways in TAB1(-/-) and MEKK3(-/-) MEFs
a TAB1:TAK1:IKK beta:NF-kappaB signaling axis forms aberrantly in breast cancer cells and, consequently, enables oncogenic signaling by TGF-beta
Cell shrinkage under the osmotic stress condition increases the concentration of TAB1-TAK1 and may oligomerize and activate TAK1 in a TAB1-dependent manner.
p38 was inactivated upon infection in a Leishmania surface protease Leishmania surface protease GP63 protein degradation-dependent manner, which likely involves cleavage of the upstream adaptor TAB1.
TGF-beta1 activates TAK1 via TAB1-mediated autophosphorylation, independent of TGF-beta receptor kinase activity in mesangial cells
The protein encoded by this gene was identified as a regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is known to mediate various intracellular signaling pathways, such as those induced by TGF beta, interleukin 1, and WNT-1. This protein interacts and thus activates TAK1 kinase. It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1. This protein can also interact with and activate the mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus represents an alternative activation pathway, in addition to the MAPKK pathways, which contributes to the biological responses of MAPK14 to various stimuli. Alternatively spliced transcript variants encoding distinct isoforms have been reported.
TAK1-binding protein 1
, TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
, mitogen-activated protein kinase kinase kinase 7-interacting protein 1
, transforming growth factor beta-activated kinase-binding protein 1
, TGF-beta-activated kinase 1-binding protein 1
, Tak1-binding protein 1
, beta activated kinase-1 binding protein-1
, mitogen activated protein kinase kinase kinase 7 interacting protein 1
, mitogen-activated protein kinase kinase kinase 7 interacting protein 1