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anti-Human Angiomotin Antibodies:
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Human Polyclonal Angiomotin Primary Antibody for DB - ABIN1881054
Heller, Adu-Gyamfi, Smith-Kinnaman, Babbey, Vora, Xue, Bittman, Stahelin, Wells: Amot recognizes a juxtanuclear endocytic recycling compartment via a novel lipid binding domain. in The Journal of biological chemistry 2010
Show all 5 Pubmed References
Human Polyclonal Angiomotin Primary Antibody for WB - ABIN531071
Chan, Lim, Chong, Pobbati, Huang, Hong: Hippo pathway-independent restriction of TAZ and YAP by angiomotin. in The Journal of biological chemistry 2011
Show all 2 Pubmed References
Human Polyclonal Angiomotin Primary Antibody for IF (p), IHC (p) - ABIN754873
Shimada, Abe, Kohno, Satohisa, Konno, Takahashi, Hatakeyama, Arimoto, Kakuki, Kaneko, Takano, Saito, Kojima: Loss of tricellular tight junction protein LSR promotes cell invasion and migration via upregulation of TEAD1/AREG in human endometrial cancer. in Scientific reports 2017
Angiomotin promotes prostate cancer cell proliferation by signaling through the Hippo-YAP pathway.
The authors propose that phosphorylation of Amot(S176) is a critical post-translational modification that suppresses YAP's ability to promote cell proliferation and tumorigenesis by altering the subcellular localization of an essential YAP co-factor.
Data indicate that Amot is crucial for the maintenance of nuclear YAP to promote renal epithelial and RCC proliferation.
Decreased AMOT-p130 expression coupled with high nuclear YAP1 expression resulted in shorter overall survival and disease-free survival in patients with advanced gastric cancer.
Study focused on the methylation profile of the AMOT promoter CpG island during development, comparing it in circulating cord blood endothelial progenitor cells (ECFC) of cord blood from term versus preterm newborns. Findings highlight importance of pro-angiogenic AMOT gene methylation in ECFC, suggesting that epigenetic mechanisms may control the regulation of angiogenesis during development.
AMOT may function as an oncogene in the progression of colon cancer by activating the YAP-ERK/PI3K-AKT signaling pathway.
The lncRNA SNHG12 promotes cell proliferation and migration by upregulating AMOT gene expression in osteosarcoma cells in vivo and in vitro.
angiomotin and Merlin respectively interface cortical actin filaments and core kinases in Hippo signaling
Study shows miR-205 significantly downregulated and directly target the 3'-UTR of AMOT in breast cancer. In vitro, miR-205 regulates the proliferation and invasion of breast cancer cells through suppression of AMOT expression.
Amot was highly expressed in breast cancer tissues and was important in the promotion of breast cancer cell proliferation and invasion. Amot knockdown in MCF-7 cells decreased the expression of YAP, YAP/TAZ and LATS1.
experiments indicate that AMOT and other motin family members function together with NEDD4L to help complete immature virion assembly prior to ESCRT-mediated virus budding
AMOT is a crucial suppressor of lung cancer metastasis and highlight its critical role as a tumor suppressor and its potential as a prognostic biomarker and therapeutic target for lung cancer.
expression is upregulated in sinonasal inverted papilloma
angiomotin proteins connect F-actin architecture to YAP regulation.
function of Angiomotins and other members of the Motin protein family
Scaffold proteins angiomotin (Amot) and angiomotin-related AmotL1 and AmotL2 were recently identified as negative regulators of YAP and TAZ by preventing their nuclear translocation.
Within the nucleus, Amot-p130 was associated with the transcriptional complex containing Yap and Teads (TEA domain family members) and contributed to the regulation of a subset of Yap target genes, many of which are associated with tumorigenesis.
These results collectively suggest that the Hippo pathway negatively regulates the actin-binding activity of Amot family members through direct phosphorylation.
Thus AMOT is a direct substrate of Lats1/2 mediating functions of the Hippo pathway in endothelial cell migration and angiogenesis.
Data indicate that the phosphorylation of Amot130 by LATS1/2 is found to be a key feature that enables it to inhibit Yes-associated protein (YAP) dependent signaling and cell growth.
Collectively, we have uncovered that AMOT acts as a YAP stimulator in high glucose level.
Rho attenuates the interaction between Amot and Nf2 by binding to the coiled-coil domain of Amot.
TFPI-1 interacts with AMOT, which led to a decrease in the phosphorylation of YAP and further increased the genes expression of the proliferation and migration involved. Our results further confirmed that atherosclerosis was a localized disease.
a new function of RNF146 and tankyrase in stabilizing the Crumbs complex through downregulation of AMOT proteins at the apical membrane, is reported.
The loss of Angiomotin, together with Angiomotin-like 2, leads to differentiation of inner cell mass cells and compromised peri-implantation development.
The phosphorylation of S176 in the N-terminal domain of Amot is a critical step for activation of the Hippo pathway in adherens junctions and cell polarity disconnects the Hippo pathway from cell-cell adhesion by sequestering Amot from AJs.
Amot, Amotl1, and Amotl2 are differentially expressed in uterine cells during the peri-implantation period.
A vaccine targeting angiomotin induces an antibody response which alters tumor vessel permeability and hampers the growth of established tumors.
Depletion of Angiomotin in Nf2(-/-) Schwann cells attenuates the Ras-MAPK signaling pathway, impedes cellular proliferation in vitro and tumorigenesis in vivo
Angiomotin may promote neoplastic angiogenesis by both stimulating invasion as well as stabilizing established tubes.
angiomotin, in addition to controlling cell motility, may play a role in the assembly of endothelial cell-cell junctions
p80- and p130-angiomotin play coordinating roles in vascular tube formation by affecting cell migration and cell shape, respectively.
Data show that MUPP1 interacts with angiomotin (Amot), JEAP/Amot-like 1 and MASCOT/Amot-like 2, and that all the Amot/JEAP family proteins also interacted with Patj, a close relative of MUPP1.
75% of Amot knockout mice die between embryonic day 11 (E11) and E11.5 and exhibit severe vascular insufficiency in the intersomitic region as well as dilated vessels in the brain.
Homo-oligomerization of p80-Amot and hetero-oligomerization of both isoforms are critical for a switch between a migratory and a non-migratory cell phenotype in endothelial cells.
Amot and AmotL1 have similar effects on endothelial migration and tight junction formation in vitro. In vivo Amot appears to control the cell polarity and AmotL1 affects the stability of cell-cell junctions.
knockdown of Amot reduced the number of filopodia of endothelial tip cells and severely impaired the migration of intersegmental vessels
This gene belongs to the motin family of angiostatin binding proteins characterized by conserved coiled-coil domains and C-terminal PDZ binding motifs. The encoded protein is expressed predominantly in endothelial cells of capillaries as well as larger vessels of the placenta where it may mediate the inhibitory effect of angiostatin on tube formation and the migration of endothelial cells toward growth factors during the formation of new blood vessels. Alternative splicing results in multiple transcript variants encoding different isoforms.
angiomotin p130 isoform
, angiomotin p80 isoform