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High AJUBA level enhances cervical cancer cells.
Data show that AJUBA upregulated MMP10 (show MMP10 Proteins) and MMP13 (show MMP13 Proteins) expression in esophageal squamous cell carcinoma (ESCC).
Mechanistic investigations reveal that AJUBA specifically binds the FERM domain of JAK1 (show JAK1 Proteins) to dissociate JAK1 (show JAK1 Proteins) from the IFNgamma recepter, resulting in an inhibition of STAT1 (show STAT1 Proteins) phosporylation and concomitantly its nuclear translocation. Clinically, the level of AJUBA in CRC (show CALR Proteins) specimens is negatively correlated with the levels of IFIT2 (show IFIT2 Proteins) and pSTAT1
AJUBA is a LIM domain protein and contributes to the formation and stability of cadherin-mediated cell-cell adhesion. Loss of AJUBA enhances Prostate cancer cell migration and downregulation of AJUBA expression is observed in metastatic Prostate cancer.
Mutations of the LIM protein AJUBA mediate sensitivity of head and neck squamous cell carcinomas to treatment with PLK1 inhibitors.
mitotic phosphorylation of Ajuba is sufficient to promote cell proliferation and anchorage-independent growth in vitro and tumorigenesis in vivo
The results in this study uncovered that JUB was a regulator involved in proliferation of glioma cells, and it could be used as a potential therapeutic target for glioma.
AJUBA negatively regulates YAP activity through the LATS family, and inactivation of AJUBA is a novel key mechanism in malignant mesothelioma cell proliferation
the LIM protein JUB serves as a tumor-promoting gene in colorectal cancer by promoting epithelial-mesenchymal transition, a critical process of metastasis.
The LIM (show PDLIM5 Proteins) domain of Ajuba can competitively bind to the N-terminal of Aurora-A (show AURKA Proteins), and inhibited the interaction between N-terminal and C-terminal of Aurora A (show AURKA Proteins).
Ajuba recruits p300/CBP (show CREBBP Proteins) via its LIM (show PDLIM5 Proteins) domain and facilitates p300/CBP (show CREBBP Proteins) binding to PPARg (show PPARG Proteins). Moreover, Ajuba, PPARg (show PPARG Proteins), p300/CBP (show CREBBP Proteins) can cooperatively occupy the PPARg (show PPARG Proteins) target promoters and concomitantly increases histone acetylation at these loci.
Ajuba is a novel coactivator for liver X receptors and may play important role in lipid and glucose metabolism.
Findings support the importance of adhesion molecules (VE-cadherin and CD31), survivin, and Ajuba in modulating the Hippo pathway, which regulates, in part, proliferation and survival in hemangioendotheliomas.
PKD1-mediated phosphorylation of SNAI1 occurs in the nucleus and generates a nuclear, inactive DNA/SNAI1 complex that shows decreased interaction with its co-repressor Ajuba.
This paper presents evidence indicating that the human and mouse Ajuba is a new cytosolic component of the IL-1 (show IL1A Proteins) signaling pathway, influencing the assembly and activity of the aPKC/p62 (show GTF2H1 Proteins)/TRAF6 (show TRAF6 Proteins) multiprotein signaling complex.
identification of the protein arginine methyltransferase 5 (PRMT5 (show PRMT5 Proteins)) as an effector recruited to SNAIL (show SNAI1 Proteins) through an interaction with AJUBA that functions to repress the SNAIL (show SNAI1 Proteins) target gene, E-cadherin (show CDH1 Proteins)
cytoplasmic LIM protein that binds glial glutamate transporter GLT-1 and is proposed to allow glial glutamate transporter GLT-1 to regulate intracellular signaling or interact with the cytoskeleton
LIM domain-containing protein ajuba
, jub, ajuba homolog
, protein ajuba
, Ajuba protein
, ajuba homolog