Search results for: APBA1 Antibody
#18836734 2008/10/03 To Up
NSF, Unc-18-1, dynamin-1 and HSP90 are inclusion body components in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture.Neuronal intranuclear inclusion disease, a progressive ataxia that may be familial or sporadic, is characterized by numerous neuronal intranuclear inclusion bodies similar to those found in polyglutamine repeat diseases. Previously, we found that the intranuclear inclusion bodies are intensely immunopositive for SUMO-1, a protein which covalently conjugates to other proteins in a similar way to ubiquitin. To identify the SUMO-1-associated proteins in the inclusion bodies, we isolated intranuclear inclusion bodies from fresh, frozen brain tissue of a case with familial neuronal intranuclear inclusion disease and solubilized the proteins. SUMO-1-associated inclusion body proteins were then immunocaptured using an anti-SUMO-1 antibody. The proteins, NSF, dynamin-1 and Unc-18-1 (rbSEC1), involved in membrane trafficking of proteins, and the chaperone HSP90, were identified following anti-SUMO-1-immunocapture by using tandem mass spectrometry and database searching. Immunohistochemistry of brain sections and crude brain homogenates of three cases of familial neuronal intranuclear inclusion disease confirmed the presence of these proteins in intranuclear inclusions.
Dean L Pountney, Mark J Raftery, Fariba Chegini, Peter C Blumbergs, Wei Ping Gai
1571 related Products with: NSF, Unc-18-1, dynamin-1 and HSP90 are inclusion body components in neuronal intranuclear inclusion disease identified by anti-SUMO-1-immunocapture.100ug100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug Lyophilized100ug100ug Lyophilized100ug100ug Lyophilized100ug Lyophilized100ug100ug
#16470387 2006/02/10 To Up
Development, maturation and subsequent activation of follicular dendritic cells (FDC): immunohistochemical observation of human fetal and adult lymph nodes.To elucidate the processes involved in development and activation of human follicular dendritic cells (FDC), immunohistochemistry was performed on paraffin sections of fetal lymph nodes (FLN) obtained from archived autopsy material, and of adult reactive lymph nodes (ARLNs) excised for diagnostic purpose, using a panel of antibodies. Our study showed that tiny clusters of CNA.42(+ )KiM4p(+) cells, surrounded by some B-lymphocytes, initially arose in the cortical area of underdeveloped FLN around the 20th gestational week. No co-expression of CD21 and CD35 was found. In the relatively developed FLN of the same gestational age, small eddies of immature FDC, which expressed CD21, CD35, and nerve growth factor receptor (NGFR), as well as CNA.42 and KiM4p, were observed within ill-defined aggregations of B-lymphocytes. As gestation progressed, more B-lymphocytes assembled in a compact manner and formed primary lymphoid follicles containing an extending web of mature FDC, which expressed CNA.42, KiM4p, CD21, CD35, NGFR, and sometimes CD23 and X-11. In well-developed secondary follicles of ARLNs, activated FDC expressed additional molecules such as CD55, CD106, and S100alpha. Our observations identified the processes of phenotypic alteration of human FDC and established practical indicators determining their developmental stage and functional phase.
Naoko Kasajima-Akatsuka, Kunihiko Maeda
1517 related Products with: Development, maturation and subsequent activation of follicular dendritic cells (FDC): immunohistochemical observation of human fetal and adult lymph nodes.200 25 200 25 200 1.00 flask200 0.1 mg1.00 flask1000 1 ml100ul
#11517249 // To Up
c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK.Using a yeast two-hybrid method, we searched for amyloid precursor protein (APP)-interacting molecules by screening mouse and human brain libraries. In addition to known interacting proteins containing a phosphotyrosine-interaction-domain (PID)-Fe65, Fe65L, Fe65L2, X11, and mDab1, we identified, as a novel APP-interacting molecule, a PID-containing isoform of mouse JNK-interacting protein-1 (JIP-1b) and its human homolog IB1, the established scaffold proteins for JNK. The APP amino acids Tyr(682), Asn(684), and Tyr(687) in the G(681)YENPTY(687) region were all essential for APP/JIP-1b interaction, but neither Tyr(653) nor Thr(668) was necessary. APP-interacting ability was specific for this additional isoform containing PID and was shared by both human and mouse homologs. JIP-1b expressed by mammalian cells was efficiently precipitated by the cytoplasmic domain of APP in the extreme Gly(681)-Asn(695) domain-dependent manner. Reciprocally, both full-length wild-type and familial Alzheimer's disease mutant APPs were precipitated by PID-containing JIP constructs. Antibodies raised against the N and C termini of JIP-1b coprecipitated JIP-1b and wild-type or mutant APP in non-neuronal and neuronal cells. Moreover, human JNK1beta1 formed a complex with APP in a JIP-1b-dependent manner. Confocal microscopic examination demonstrated that APP and JIP-1b share similar subcellular localization in transfected cells. These data indicate that JIP-1b/IB1 scaffolds APP with JNK, providing a novel insight into the role of the JNK scaffold protein as an interface of APP with intracellular functional molecules.
S Matsuda, T Yasukawa, Y Homma, Y Ito, T Niikura, T Hiraki, S Hirai, S Ohno, Y Kita, M Kawasumi, K Kouyama, T Yamamoto, J M Kyriakis, I Nishimoto
2294 related Products with: c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK.100ul100μg100ul100ul100ul 100ul100ul100ul100ul100μg100ul100ul
#11483239 // To Up
Neuronal expression of mint1 and mint2, novel multimodular proteins, in adult murine brain.Mints are multimodular adapter proteins in functioning membrane transport and organization. Mint1 and mint2 are neuron-specific. We localized these isoforms in mouse brain. By in situ hybridization, mRNA encoding mint1 or mint2 was expressed in neurons throughout the brain. Mint1 mRNA expression was greatest in the limbic system including cingulate cortex, hippocampus, anterior thalamic nuclei, medial habenular nucleus, and mammillary body. Mint2 mRNA was rich in cerebral cortex, entorhinal cortex, and hippocampus, but less prominent in other limbic structures. Mint1 mRNA and mint2 mRNA were distributed among hippocampal pyramidal neurons, while mint2 mRNA was especially abundant in CA3. Mint1, but not Mint2 mRNA was abundant in the substantia nigra pars compacta. Immunohistochemistry visualized mint proteins in axon terminals and neuronal somata, generally following mRNA distribution. In the hippocampus, mint1 was rich in the entorhinal projections and mossy fibers of the dentate gyrus, while mint2 was rich in commisural fibers from the contralateral hippocampus and in CA1. Mint1 intensely stained catecholamine-containing neurons such as the substantia nigra pars compacta, ventral tegmental area, and locus ceruleus. Mint2 protein was ubiquitous in these regions. Mint1 and mint2 distribution also differed elsewhere in the brainstem and in the cerebellum. Central nervous system neurons, then, predominantly express either mint1 or mint2. Mints may be involved in synaptic vesicle transport toward the active zone, also participating in transport of certain membrane proteins toward the postsynaptic density. Mint1 and mint2 may divide roles either regionally or depending on neuronal functional characteristics.
Y Nakajima, M Okamoto, H Nishimura, K Obata, H Kitano, M Sugita, T Matsuyama
1948 related Products with: Neuronal expression of mint1 and mint2, novel multimodular proteins, in adult murine brain.50 100 μg10021mg1001 mg21mg501 mg
#10971649 // To Up
Ultrastructural localization of mint1 at synapses in mouse hippocampus.Mint1 and mint2 were isolated in the course of seeking the protein ligands to munc18-1, a neuronal protein essential for synaptic vesicle exocytosis. The mint family of proteins has been highly conserved in the course of evolution, being retained from C. elegans to mammals. Several lines of biochemical and genetic evidence have suggested that mint1 and LIN-10, its homologue in C. elegans, function at synapses in the brain. Because the precise subcellular location of mint1 is incompletely known, we used immunostaining to examine the distribution of mint1 in the mouse brain including ultrastructural localization in synapses. Strong, finely punctate mint1 immunolabeling was detected throughout the brain, including cerebral cortex, striatum, hippocampus, thalamus, basal ganglia and cerebellum. At the most synapses in the molecular layer, mint1 was particularly abundant at the active zone and to a lesser extent in association with synaptic vesicles in the presynaptic terminals. In contrast, a very few synapses showed mint1 immunoreactivity in the postsynaptic density and there was no synapse double-positive in presynaptic and postsynaptic terminals. Mint1 distribution within presynaptic terminals overlapped that of munc18-1. These localization results are consistent with previously demonstrated biochemical interactions and strongly support functions of mint1 in synaptic vesicle exocytosis and synaptic organization in the central nervous system.
M Okamoto, T Matsuyama, M Sugita100 μg4 Membranes/Box1 mg100 μg100ug100.00 ug5ug2ug100ug Lyophilized100ug100.00 ug
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