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anti-Mouse (Murine) Antibodies:
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Rat (Rattus) Polyclonal APBA1 Primary Antibody for ICC, IHC - ABIN1742315
Boyken, Grønborg, Riedel, Urlaub, Jahn, Chua: Molecular profiling of synaptic vesicle docking sites reveals novel proteins but few differences between glutamatergic and GABAergic synapses. in Neuron 2013
Human Polyclonal APBA1 Primary Antibody for ELISA, WB - ABIN547903
Jacobs, Williams, Francis: Cyclin-dependent kinase 5, Munc18a and Munc18-interacting protein 1/X11alpha protein up-regulation in Alzheimer's disease. in Neuroscience 2006
Human Polyclonal APBA1 Primary Antibody for WB - ABIN541353
Verlaeten, Casery, Cavagna, Naville, Giraudon, Belin, Begeot, Bernard: Identification of Urop11, a novel leptin-modulated gene that is upregulated in the hypothalamus of mice with virus-induced obesity. in Journal of molecular endocrinology 2007
Results indicate that both X11 and X11L exert largely in brain neurons, but X11 may also function in peripheral tissues.
Due to the multiple interacting partners of X11alpha, dysfunction or alteration in X11alpha will have a significant cellular effect.
Mint1 826 bridges APP to the small GTPase
Expression of Apba1 in the mouse hippocampus is modulated by a sequence variant (B2 SINE indel) in the 3' UTR of Comt (catechol-O-methyltransferase).
Our data support a function for both GSK3 and CDK5 in amyloid precursor protein processing, further implicating these two kinases in the pathogenesis of Alzheimer's disease.
Mints are important regulators of presynaptic neurotransmitter release that are essential for mouse survival.
Can be considered a key molecule in the hypothalamic integration pathway, important as a target of leptin action.
Reports have demonstrated that KIF17-Mint1 association was disrupted and transported cargo was released from its microtubule-based transport when Ser 1029 of KIF17 was phosphorylated.
X11s associate primarily with APP molecules that are outside of DRM, that the dissociation of APP-X11/X11L complexes leads to entry of APP into DRM, and that cleavage of uncomplexed APP by BACE within DRM
These results suggest that the three Mint/X11 proteins regulate Abeta production by a novel mechanism that may have implications for therapeutic approaches to altering APP cleavage in Alzheimer's disease.
Mint1 causes amyloid precursor protein accumulation in the trans-Golgi network.
Mints are necessary for activity-induced APP and PS1 trafficking and provide insight into the cellular fate of APP in endocytic pathways essential for Abeta production.
an autoinhibitory mechanism in Mint1 is important for regulating APP processing and may provide novel therapies for Alzheimer's disease
Transcriptional co-activators Taz and Yap mediate signaling via the amyloid beta protein precursor paralogues APLP1 and APLP2 through interactions with Mint1 and Mint3.
Study identified the conserved binding site for the peptide on the CASK calmodulin kinase domain. A related EPIWVMRQ peptide from Mint1 was also discovered to be sufficient for binding.
Our findings show a new function for X11alpha that may impact on Alzheimer's disease pathogenesis.
Methylation of MINT1 was significantly more prevalent in UC-CRC cases compared with controls.
ApoEr2 regulates cell movement, and both X11alpha and Reelin enhance this effect.
A novel consensus sequence for interaction with the PDZ-1 and PDZ-2 domains of amyloid precursor protein (APP)-interacting proteins Mint1, Mint2, and Mint3 is reported, with multiple novel interactors for these proteins.
Munc18a acts through direct and indirect interactions with X11 proteins and powerfully regulates APP metabolism and Abeta secretion.
Coexpression of X11alpha with amyloid protein precursor retarded its maturation, prolonged its half-life, and inhibited amyloid protein precursor, Abeta40, and Abeta42 secretion.
human X11alpha inhibits Abeta production and deposition in vivo in the brain in transgenic mice harboring a familial Alzheimer's disease mutant APP that produces increased levels of Abeta.
Involvement of X11L in the phosphorylation of APP family proteins in cellular stress and suggest that X11L protein may be .
X11alpha and X11beta have roles in beta-amyloid precursor protein processing
Mediates exocytosis and decreases beta-amyloid peptide formation in Alzheimer disease.
Data show that neuronal munc18-1-interacting protein 1 is an inclusion body component in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture.
The protein encoded by this gene is a member of the X11 protein family. It is a neuronal adapter protein that interacts with the Alzheimer's disease amyloid precursor protein (APP). It stabilizes APP and inhibits production of proteolytic APP fragments including the A beta peptide that is deposited in the brains of Alzheimer's disease patients. This gene product is believed to be involved in signal transduction processes. It is also regarded as a putative vesicular trafficking protein in the brain that can form a complex with the potential to couple synaptic vesicle exocytosis to neuronal cell adhesion.
amyloid beta (A4) precursor protein-binding, family A, member 1
, amyloid beta A4 precursor protein-binding, family A, member 1
, amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)
, ketopantoate reductase
, 2-dehydropantoate 2-reductase
, Amyloid beta A4 precursor protein-binding family A member 1
, amyloid beta A4 precursor protein-binding family A member 1-like
, adapter protein X11alpha
, amyloid beta A4 precursor protein-binding family A member 1
, neuron-specific X11 protein
, neuronal Munc18-1-interacting protein 1
, amyloid beta (A4) precursor protein-binding family A APBA1: amyloid beta (A4) precursor protein-binding family A member 1 (X11)
, amyloid beta (A4) precursor protein-binding, family A, APBA1: amyloid beta (A4) precursor protein-binding, family A, member 1 (X11)
, adaptor protein X11alpha
, neuronal munc18-1-interacting protein 1
, phosphotyrosine-binding/-interacting domain (PTB)-bearing protein