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anti-Human BAI1 Antibodies:
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Human Polyclonal BAI1 Primary Antibody for IHC (p), ELISA - ABIN544983
Kaur, Brat, Calkins, Van Meir: Brain angiogenesis inhibitor 1 is differentially expressed in normal brain and glioblastoma independently of p53 expression. in The American journal of pathology 2002
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Human Polyclonal BAI1 Primary Antibody for ICC, IF - ABIN259644
Hochreiter-Hufford, Lee, Kinchen, Sokolowski, Arandjelovic, Call, Klibanov, Yan, Mandell, Ravichandran: Phosphatidylserine receptor BAI1 and apoptotic cells as new promoters of myoblast fusion. in Nature 2013
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We have uncovered a new role for BAI1 in facilitating macrophage anti-viral responses. We show that arming oHSV with antiangiogenic Vstat120 also shields them from inflammatory macrophage antiviral response, without reducing safety
Data suggest agonist-induced signal transduction via either BAI1/ADGRB1 or GPR56/ADGRG1 does not require conserved membrane-proximal stalk region; thus, it appears GAIN domain cleavage via autoproteolysis is not necessary for receptor activation.
BAI1 may be involved in the negative regulation of bladder transitional cell carcinoma microvascular proliferation, and its expression may be associated with a reduction in p53 mutations.
Results show that lower BAI1 expression correlates with poorer patient survival, and high Nestin expression is associated with an increased probability of metastases in breast cancer patients.
recognition of apoptotic cells by BAI1 contributes to their clearance in the human gastric mucosa and this is associated with anti-inflammatory effects
findings demonstrate that BAI1 is a synaptic receptor that can activate both the Rho and ERK pathways, with the N-terminal and C-terminal regions of the receptor playing key roles in the regulation of BAI1 signaling activity
The results of this study indicated that BAI1 plays an important role in synaptogenesis that is mechanistically distinct from its role in phagocytosis.
Proprotein convertases, primarily furin, activate latent matrix metalloproteinase-14, which then directly cleaves BAI1 to release the bioactive fragment.
MBD2 overexpression during gliomagenesis may drive tumor growth by suppressing the antiangiogenic activity of a key tumor BAI1.
brain-specific angiogenesis inhibitor 1 over-expression suppresses tumour angiogenesis
BAI1 was expressed in cerebral neurons but not astrocytes. It was localized in the cytoplasm and cell membrane. BAI1 protein may play an important role in synapse formation and signal transduction
BAI1 was widely expressed in normal brain but was absent in 28 glioma cell lines and in the majority of human glioblastoma investigated. BAI1 expression did not correlate with TP53 status
Study demonstrated that an evolutionarily conserved fragment in the C-terminal cytoplasmic tail of BAI-aGPCRs is specifically recognized by the RBD-ARR-ELMO (RAE) supramodule of the ELMO family scaffolds. The crystal structures of ELMO2-RAE and its complex with BAI1 uncover the molecular basis of BAI/ELMO interactions.
these findings suggest that BAI1 mediates the clearance of Gram-negative bacteria by stimulating both phagocytosis and NADPH oxidase activation, thereby coupling bacterial detection to the cellular microbicidal machinery.
transgenic mice overexpressing BAI1 had fewer apoptotic cells, reduced inflammation, and attenuated disease. Boosting BAI1-mediated uptake by intestinal epithelial cells was important in attenuating inflammation.
BAI1(-) mice have deficits in hippocampus-dependent spatial learning and memory, enhanced long-term potentiation, impaired long-term depression, and postsynaptic density thinning. BAI1 stops PSD-95 polyubiquitination/degradation via interaction with MDM2.
data identify apoptotic cells as a new type of cue that induces signalling via the phosphatidylserine receptor BAI1 to promote fusion of healthy myoblasts, with important implications for muscle development and repair
expression pattern in brain regions and role as anti-angiogenic factor in mature neuropil
findings identify BAI1 as a pattern recognition receptor that mediates nonopsonic phagocytosis of Gram-negative bacteria by macrophages and directly affects the host response to infection
BAI1 is a phosphatidylserine recognition receptor that can directly recruit a Rac-GEF complex to mediate the uptake of apoptotic cells.
Angiogenesis is controlled by a local balance between stimulators and inhibitors of new vessel growth and is suppressed under normal physiologic conditions. Angiogenesis has been shown to be essential for growth and metastasis of solid tumors. In order to obtain blood supply for their growth, tumor cells are potently angiogenic and attract new vessels as results of increased secretion of inducers and decreased production of endogenous negative regulators. BAI1 contains at least one 'functional' p53-binding site within an intron, and its expression has been shown to be induced by wildtype p53. There are two other brain-specific angiogenesis inhibitor genes, designated BAI2 and BAI3 which along with BAI1 have similar tissue specificities and structures, however only BAI1 is transcriptionally regulated by p53. BAI1 is postulated to be a member of the secretin receptor family, an inhibitor of angiogenesis and a growth suppressor of glioblastomas
brain-specific angiogenesis inhibitor 1
, brain-specific angiogenesis inhibitor 1-like