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The beta3-endonexin can act as a novel anti-angiogenic factor (show VEGFA Proteins) specifically in the response to hypoxia due to its negative impact on the activation of HIF-1 (show HIF1A Proteins).
Data propose that CENP-P (show CENPP Proteins)/O/R/Q/U self-assembles on kinetochores with varying stoichiometry and undergoes a pre-mitotic maturation step that could be important for kinetochores switching into the correct conformation for microtubule-attachment.
The presence of various isoforms and the relationship between subcellular localization and integrin-activating function of beta(3)-endonexin is described.
This protein downregulates urokinase-type plasminogen activator receptor (show PLAUR Proteins) promoter activity.
Results suggest that breast cancer cells contain a novel "death switch" that can be specifically triggered by NRIF3 or death domain 1.
Metastasis-associated protein 1 interacts with NRIF3, an estrogen-inducible nuclear receptor coregulator
findings suggest that NRIF3-Ser28 is a physiologic target of Pak1 (show PAK1 Proteins) signaling and contributes to the enhanced NRIF3 co-activator activity, leading to coordinated potentiation of ERalpha (show ESR1 Proteins) transactivation
These results indicate Cenp-r functions bilaterally in cancer development: during early developmental stages, Cenp-r functions as a tumor suppressor, but during the expansion and progression of papillomas it functions as a tumor-promoting factor
in contrast to uPAR (show PLAUR Proteins) or NF-kappaB (show NFKB1 Proteins), the expression of beta(3)-endonexin was reduced in extracts of advanced atherosclerotic aortic tissue
This gene encodes a transcriptional coregulator that binds to and enhances the activity of members of the nuclear receptor families, thyroid hormone receptors and retinoid X receptors. This protein also acts as a corepressor of NF-kappaB-dependent signaling. This protein induces apoptosis in breast cancer cells through a caspase 2-mediated signaling pathway. This protein is also a component of the centromere-specific histone H3 variant nucleosome associated complex (CENP-NAC) and may be involved in mitotic progression by recruiting the histone H3 variant CENP-A to the centromere. Alternate splicing results in multiple transcript variants.
beta 3 endonexin
, centromere protein R
, integrin beta-3-binding protein
, nuclear receptor-interacting factor 3