Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, M, R||IP, WB||M||Purified||Monoclonal Antibody|
|Description||Anti-Calsenilin/DREAM Antibody, clone 40A5|
|Presentation||0.1M Tris-glycine, pH 7.4, 0.15M NaCl, 0.05% sodium azide before the addition of glycerol to 30%|
|Application||Detect Calsenilin/DREAM using this Anti-Calsenilin/DREAM Antibody, clone 40A5 validated for use in IP & WB.|
|Safety Information according to GHS|
|Storage and Shipping Information|
|Storage Conditions||2 years at -20°C|
|Material Size||100 µL|
|Anti-Calsenilin/DREAM, clone 40A5||2476953|
|Anti-Calsenilin/DREAM, clone 40A5 - 26762||26762|
|Anti-Calsenilin/DREAM, clone 40A5 -2844282||2844282|
|Anti-Calsenilin/DREAM, clone 40A5, (mouse ascites)||2839444|
|Reference overview||Pub Med ID|
|Independent genomic control of neuronal number across retinal cell types.|
Keeley, PW; Whitney, IE; Madsen, NR; St John, AJ; Borhanian, S; Leong, SA; Williams, RW; Reese, BE
Developmental cell 30 103-9 2014
The sizes of different neuronal populations within the CNS are precisely controlled, but whether neuronal number is coordinated between cell types is unknown. We examined the covariance structure of 12 different retinal cell types across 30 genetically distinct lines of mice, finding minimal covariation when comparing synaptically connected or developmentally related cell types. Variation mapped to one or more genomic loci for each cell type, but rarely were these shared, indicating minimal genetic coregulation of final number. Multiple genes, therefore, participate in the specification of the size of every population of retinal neuron, yet genetic variants work largely independent of one another during development to modulate those numbers, yielding substantial variability in the convergence ratios between pre- and postsynaptic populations. Density-dependent cellular interactions in the outer plexiform layer overcome this variability to ensure the formation of neuronal circuits that maintain constant retinal coverage and complete afferent sampling.
|Modulation of A-type potassium channels by a family of calcium sensors.|
An, W F, et al.
Nature, 403: 553-6 (2000) 2000
|DREAM is a Ca2+-regulated transcriptional repressor.|
Carrión, A M, et al.
Nature, 398: 80-4 (1999) 1999
Fluxes in amounts of intracellular calcium ions are important determinants of gene expression. So far, Ca2+-regulated kinases and phosphatases have been implicated in changing the phosphorylation status of key transcription factors and thereby modulating their function. In addition, direct effectors of Ca2+-induced gene expression have been suggested to exist in the nucleus, although no such effectors have been identified yet. Expression of the human prodynorphin gene, which is involved in memory acquisition and pain, is regulated through its downstream regulatory element (DRE) sequence, which acts as a location-dependent gene silencer. Here we isolate a new transcriptional repressor, DRE-antagonist modulator (DREAM), which specifically binds to the DRE. DREAM contains four Ca2+-binding domains of the EF-hand type. Upon stimulation by Ca2+, DREAM's ability to bind to the DRE and its repressor function are prevented. Mutation of the EF-hands abolishes the response of DREAM to Ca2+. In addition to the prodynorphin promoter, DREAM represses transcription from the early response gene c-fos. Thus, DREAM represents the first known Ca2+-binding protein to function as a DNA-binding transcriptional regulator.
|Evidence that tumor necrosis factor alpha converting enzyme is involved in regulated alpha-secretase cleavage of the Alzheimer amyloid protein precursor.|
Buxbaum, J D, et al.
J. Biol. Chem., 273: 27765-7 (1998) 1998
The amyloid protein, Abeta, which accumulates in the brains of Alzheimer patients, is derived by proteolysis of the amyloid protein precursor (APP). APP can undergo endoproteolytic processing at three sites, one at the amino terminus of the Abeta domain (beta-cleavage), one within the Abeta domain (alpha-cleavage), and one at the carboxyl terminus of the Abeta domain (gamma-cleavage). The enzymes responsible for these activities have not been unambiguously identified. By the use of gene disruption (knockout), we now demonstrate that TACE (tumor necrosis factor alpha converting enzyme), a member of the ADAM family (a disintegrin and metalloprotease-family) of proteases, plays a central role in regulated alpha-cleavage of APP. Our data suggest that TACE may be the alpha-secretase responsible for the majority of regulated alpha-cleavage in cultured cells. Furthermore, we show that inhibiting this enzyme affects both APP secretion and Abeta formation in cultured cells.