MABN894
Anti-Synapsin-1 Antibody, clone 10.22
clone 10.22, from mouse
別名:
Synapsin I, Synapsin-1
製品名
Anti-Synapsin-1 Antibody, clone 10.22, clone 10.22, from mouse
biological source
mouse
conjugate
unconjugated
antibody form
purified antibody
antibody product type
primary antibodies
clone
10.22, monoclonal
species reactivity
rat, mouse, human, fish, bovine
technique(s)
immunofluorescence: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Quality Level
Gene Information
human ... SYN1(6853)
Analysis Note
Evaluated by Western Blotting in rat brain cytosol tissue lysate.
Western Blotting Analysis: 0.5 µg/mL of this antibody detected Synapsin-1 in 10 µg of rat brain cytosol tissue lysate.
Western Blotting Analysis: 0.5 µg/mL of this antibody detected Synapsin-1 in 10 µg of rat brain cytosol tissue lysate.
Application
Immunohistochemistry Analysis: A 1:50 dilution from a representative lot detected Synapsin-1 in human, mouse, and rat cerebral cortex tissues.
Western Blotting Analysis: A representative lot detected synapsin Ia/Ib in mouse cortical neuron lysates (Medrihan, L., et al. (2013). Nat. Commun. 4:1512).
Western Blotting Analysis: A representative lot detected purified bovine brain synapsin Ia/Ib (Messa, M., et al. (2010). J. Cell Sci. 123(13):2256-2265).
Western Blotting Analysis: A representative lot detected synapsin-1 in Torpedo (electric ray) synaptosomal preparations and in GST-cyclophilin B pull-downs (Lane-Guermonprez, L., et al. (2005). J. Neurochem. 93(6):1401-1411).
Western Blotting Analysis: A representative lot detected synapsin-1 in the same rat brain subcellular fractions as cyclophilin B (Lane-Guermonprez, L., et al. (2005). J. Neurochem. 93(6):1401-1411).
Western Blotting Analysis: A representative lot detected synapsin Ia/Ib, but not IIa/IIb, in rat brain post-nuclear supernatants (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Immunoprecipitation Analysis: A representative lot immunoprecipitated synapsin Ia/Ib, but not IIa/IIb, from rat brain synaptosomal preparations using protein G beads with pre-bound rabbit anti-mouse IgG (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Immunofluorescence Analysis: Clone 10.22 ascites fluid was employed to localize synapsin-1 immunoreactivity within retinal inner plexiform layer (IPL) of floating or whole-mount rat retinas (Mandell, J.W., et al. (1992). J. Neurosci. 12(5):1736-1749).
Note: Clone 10.22 does not bind significantly to protein G. For immunoprecipitation application, pre-coat protein G beads with an anti-mouse IgG antibody is recommended (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Western Blotting Analysis: A representative lot detected synapsin Ia/Ib in mouse cortical neuron lysates (Medrihan, L., et al. (2013). Nat. Commun. 4:1512).
Western Blotting Analysis: A representative lot detected purified bovine brain synapsin Ia/Ib (Messa, M., et al. (2010). J. Cell Sci. 123(13):2256-2265).
Western Blotting Analysis: A representative lot detected synapsin-1 in Torpedo (electric ray) synaptosomal preparations and in GST-cyclophilin B pull-downs (Lane-Guermonprez, L., et al. (2005). J. Neurochem. 93(6):1401-1411).
Western Blotting Analysis: A representative lot detected synapsin-1 in the same rat brain subcellular fractions as cyclophilin B (Lane-Guermonprez, L., et al. (2005). J. Neurochem. 93(6):1401-1411).
Western Blotting Analysis: A representative lot detected synapsin Ia/Ib, but not IIa/IIb, in rat brain post-nuclear supernatants (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Immunoprecipitation Analysis: A representative lot immunoprecipitated synapsin Ia/Ib, but not IIa/IIb, from rat brain synaptosomal preparations using protein G beads with pre-bound rabbit anti-mouse IgG (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Immunofluorescence Analysis: Clone 10.22 ascites fluid was employed to localize synapsin-1 immunoreactivity within retinal inner plexiform layer (IPL) of floating or whole-mount rat retinas (Mandell, J.W., et al. (1992). J. Neurosci. 12(5):1736-1749).
Note: Clone 10.22 does not bind significantly to protein G. For immunoprecipitation application, pre-coat protein G beads with an anti-mouse IgG antibody is recommended (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Research Category
Neuroscience
Neuroscience
Research Sub Category
Developmental Neuroscience
Developmental Neuroscience
This Anti-Synapsin-1 Antibody, clone 10.22 is validated for use in Western Blotting, Immunohistochemistry (Paraffin), Immunoprecipitation, Immunofluorescence for the detection of Synapsin-1.
Biochem/physiol Actions
Clone 10.22 reacts with both synapsin-1 spliced isoforms (Ia and Ib), but not synapsin-2 spliced isoform IIa or IIb (Vaccaro, P., et al. (1997). Brain Res. Mol. Brain Res. 52(1):1-16).
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
Synapsin-1 (UniProt P17599; also known as Synapsin I) is encoded by the SYN1 gene (Gene ID 281510) in bovine species. The synapins constitute a family of abundant neuronal phosphoproteins that regulate SV trafficking and neurotransmitter release at the pre-synaptic terminal. Three genes exisit in mammals, encoding altogether 11 synapsin members by alternative splicings (Synapsin Ia & Ib by SYN1, Synapsin IIa & IIb by SYN2, Synapsin IIIa through IIIf by SYN3), Syn III is the most precociously expressed isoform that has a role in the early phases of neural development and is downregulated in mature neurons. On the other hand, Syn I and Syn II are expressed at low levels at birth and their expressions progressively increase during synaptogenesis to reach a stable plateau at 1–2 months of life. The NH2-terminal region is divided into A, B, and C domains and is highly conserved among synapsin isoforms. Synapsins are regulated by postransloational phosphorylations. Domain A contains PKA and CaMKI/IV phosphorylation sites, domain B contains MAPK/Erk phosphorylation sites, and domain C is phosphorylated by Src. The C-terminal region contains spliced domains and diverge among synapsin isoforms (domain D in Syn Ia and Ib, domain G in Syn IIa and IIb, domain H in Syn IIa, and domain J in Syn IIIa), although they all bear proline-rich regions binding to several SH3-containing proteins and additional phosphorylation sites for CaMKII, MAPK/Erk, and cdk1/5.
~75 kDa observed.
Immunogen
Epitope: Pro-rich domain D.
Purified bovine brain synapsin-1.
Other Notes
Concentration: Please refer to lot specific datasheet.
Physical form
Format: Purified
Protein G Purified
Purified mouse monoclonal IgG1 antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Preparation Note
Stable for 1 year at 2-8°C from date of receipt.
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保管分類
12 - Non Combustible Liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
試験成績書（COA）
製品のロット番号・バッチ番号を入力して、試験成績書（COA） を検索できます。ロット番号・バッチ番号は、製品ラベルに「Lot」または「Batch」に続いて記載されています。
Natali L Chanaday et al.
eLife, 7 (2018-04-24)
Coupling of synaptic vesicle fusion and retrieval constitutes a core mechanism ensuring maintenance of presynaptic function. Recent studies using fast-freeze electron microscopy and capacitance measurements reported an ultrafast mode of endocytosis operating at physiological temperatures. Here, using rat hippocampal neurons
Susanne Wegmann et al.
Science advances, 5(6), eaaw6404-eaaw6404 (2019-06-30)
The incidence of Alzheimer's disease (AD), which is characterized by progressive cognitive decline that correlates with the spread of tau protein aggregation in the cortical mantle, is strongly age-related. It could be that age predisposes the brain for tau misfolding
Saravanan Gunaseelan et al.
Human molecular genetics, 30(1), 5-20 (2021-01-05)
FEZ1-mediated axonal transport plays important roles in central nervous system development but its involvement in the peripheral nervous system is not well-characterized. FEZ1 is deleted in Jacobsen syndrome (JS), an 11q terminal deletion developmental disorder. JS patients display impaired psychomotor
Toshiyuki Mizui et al.
Journal of neurochemistry, 109(2), 611-622 (2009-02-19)
Drebrin is a well-known side-binding protein of F-actin in the brain. Immunohistochemical data suggest that the peripheral parts of growing axons are enriched in the drebrin E isoform and mature axons are not. It has also been observed that drebrin
Kanzo Suzuki et al.
Cell reports, 37(5), 109918-109918 (2021-11-04)
Ketamine is a noncompetitive glutamatergic N-methyl-d-aspartate receptor (NMDAR) antagonist that exerts rapid antidepressant effects. Preclinical studies identify eukaryotic elongation factor 2 kinase (eEF2K) signaling as essential for the rapid antidepressant action of ketamine. Here, we combine genetic, electrophysiological, and pharmacological
関連コンテンツ
Alzheimer’s Disease is a progressively deteriorating disease. It manifests itself with memory loss, confusion, problems with judgment, planning, concentration, and personality changes; and in it’s later stages, a decline in physical abilities. The disease’s causes, cures, and preventions are unknown; however, key proteins likely involved in the degenerative mechanism have been identified. Alzheimer’s Disease is characterized by neuronal loss, alterations in neurotransmitter systems, and the presence of neurofibrillary tangles composed of abnormally hyperphosphorylated tau proteins. A prominent feature of Alzheimer’s Disease is the formation of senile plaques in selected regions of the brain. The center of these plaques are composed mainly of fibrillary aggregates of a common, but not well understood, b amyloid peptides (Aβ). The Aβ peptides are generated from the larger amyloid-β precursor protein (APP) by the sequential action of β- and γ-secretase, and it is generally accepted that oligomeric forms of this Aβ are neurotoxic, resulting in disease progression.
グローバルトレードアイテム番号
| カタログ番号 | GTIN |
|---|---|
| MABN894 | 04055977312935 |
ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.
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