MABN1817
Anti-α-Synuclein Antibody, clone 2F12
clone 2F12, from mouse
Sinónimos:
Alpha-synuclein, NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
Productos recomendados
biological source
mouse
Quality Level
antibody form
purified immunoglobulin
antibody product type
primary antibodies
clone
2F12, monoclonal
species reactivity
rat, human, mouse
technique(s)
ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable (paraffin)
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2bκ
NCBI accession no.
UniProt accession no.
shipped in
ambient
target post-translational modification
unmodified
Gene Information
human ... SNCA(6622)
General description
Alpha-synuclein (UniProt P37840; also known as NACP, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, Synuclein alpha-140) is encoded by the SNCA (also known as NACP, PARK1, PARK4) gene (Gene ID 6622) in human. Pathological aggregates are common features of many neurodegenerative diseases, such as tau neurofibrillary tangles (NFTs) in Alzheimer’s disease (AD) and frontotemporal degeneration, and α-synuclein (α-syn or αS) Lewy bodies (LBs) in Parkinson’s disease (PD) and dementia with LBs (DLB). Alpha-synuclein is a phospholipid-binding protein concentrated in presynaptic terminals where it promotes SNARE complex formation and modulates synaptic functions. Alpha-synuclein is the major component of pathologic inclusions that characterize PD, DLB, and multiple system atrophy (MSA). Research shows that αS exists not only as unfolded monomers, but in large part also as multimers, principally as ~60 kDa tetramers composed of four N-acetylated αS, that assume α-helical conformation and resist aggregation. PD-causing αS missense mutations are found to shift cellular αS from tetramers/multimers to monomers, indicating that decreased α-helical tetramers and increased unfolded monomers initiate pathogenesis. In addition, both casein kinase-1 (CK-1) and CK-2 can catalyze the phosphorylation of αS on Ser129, and Ser129-phosphorylated αS is found in αS inclusions.
Specificity
Clone 2F12 reacted with both monomeric and aggregated forms of alpha-synuclein of human, mouse, and rat species. Clone 2F12 detected both wild-type alpha-synuclein and fPD mutants (Dettmer, U., et al. (2015). Nat. Commun. 6:7314; Dettmer, U., et al. (2013). J. Biol. Chem. 288(9):6371-6385).
Immunogen
Purified human erythrocyte α-synuclein.
Application
Anti-α-Synuclein, clone 2F12, Cat. No. MABN1817, is a highly specific mouse monoclonal antibody that targets α-synuclein and has been tested in ELISA, Immunocytochemistry, Immunohistochemistry (Paraffin), Immunoprecipitation, and Western Blotting.
Immunohistochemistry Analysis: A 1:1,000 dilution from a representative lot detected α-synuclein in human prostate cancer, cerebral cortex, and kidney tissue sections.
ELISA Analysis: A representative lot (0.4 µL in 30 µL buffer/well for coating) captured recombinant human α-synuclein (0.2-40 ng/mL) in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunocytochemistry Analysis: A 1:1,000 dilution from a representative lot immunostained primary mouse cortical neurons (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunohistochemistry Analysis: A 1:11,110 dilution from a representative lot immunostained Lewy bodies (LBs) in striatum tissue sections from Parkinson′s diseased (PD) human brain (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunoprecipitation Analysis: 4 µL from a representative lot immunoprecipitated α-synuclein from 50 µg of HEL human erythroleukemia cell lysate (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
ELISA Analysis: A representative lot captured both endogenous α-synuclein (αS) from human cortical homogenate, as well the exogenously expressed wild type and familial PD (fPD) αS mutants (A30P, E46K, H50Q, G51D, A53T) from sytosolic extracts of transfected M17D human neuroblastoma cells in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
ELISA Analysis: A representative lot captured both pre-aggregated fibrillar recombinant α-synuclein as well as partially purified Lewy bodies (LBs) from a DLB (dementia with LBs) patient with or without prior sample denaturing by boiling with 2% SDS in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Immunocytochemistry Analysis: A representative lot detected cytosolic localization of endogenous rat α-synuclein (αS) and exogenously overexpressed human αS by fluorescent immunocytochemistry staining of 4% paraformaldehyde-fixed, 0.25% Triton X-100-permeabilized primary rat neurons and transfected M17D human neuroblastoma cells (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Western Blotting Analysis: A representative lot detected monomeric α-synuclein (αS) as well as αS multimers (αS60, αS80 and αS100) in extract from disuccinimidyl glutarate (DSG) cross-linked mouse brain bits, human iPSCs (both S A53T mutant and corrected isogenic line) and ESCs (both wild-type and genetically engineered isogenic αS E46K line). A significantly reduced αS60 level was seen with A53T and E46K mutants (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Western Blotting Analysis: A representative lot detected monomeric α-synuclein (αS) as well as αS multimers (αS60, αS80 and αS100) in cytosolic extracts from disuccinimidyl glutarate (DSG) cross-linked primary rat neurons, as well as human HEL erythroid leukemia and M17D neuroblastoma cells (Dettmer, U., et al. (2013). J. Biol. Chem. 288(9):6371-6385).
ELISA Analysis: A representative lot (0.4 µL in 30 µL buffer/well for coating) captured recombinant human α-synuclein (0.2-40 ng/mL) in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunocytochemistry Analysis: A 1:1,000 dilution from a representative lot immunostained primary mouse cortical neurons (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunohistochemistry Analysis: A 1:11,110 dilution from a representative lot immunostained Lewy bodies (LBs) in striatum tissue sections from Parkinson′s diseased (PD) human brain (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
Immunoprecipitation Analysis: 4 µL from a representative lot immunoprecipitated α-synuclein from 50 µg of HEL human erythroleukemia cell lysate (Courtesy of Tim Bartels, Ph.D., Brigham and Women′s Hospital, Boston, MA, U.S.A.).
ELISA Analysis: A representative lot captured both endogenous α-synuclein (αS) from human cortical homogenate, as well the exogenously expressed wild type and familial PD (fPD) αS mutants (A30P, E46K, H50Q, G51D, A53T) from sytosolic extracts of transfected M17D human neuroblastoma cells in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
ELISA Analysis: A representative lot captured both pre-aggregated fibrillar recombinant α-synuclein as well as partially purified Lewy bodies (LBs) from a DLB (dementia with LBs) patient with or without prior sample denaturing by boiling with 2% SDS in a sandwich ELISA application utilizing clone SOY1 (Cat. No. MABN1818; preconjugated with Sulfo tag) as the detection antibody (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Immunocytochemistry Analysis: A representative lot detected cytosolic localization of endogenous rat α-synuclein (αS) and exogenously overexpressed human αS by fluorescent immunocytochemistry staining of 4% paraformaldehyde-fixed, 0.25% Triton X-100-permeabilized primary rat neurons and transfected M17D human neuroblastoma cells (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Western Blotting Analysis: A representative lot detected monomeric α-synuclein (αS) as well as αS multimers (αS60, αS80 and αS100) in extract from disuccinimidyl glutarate (DSG) cross-linked mouse brain bits, human iPSCs (both S A53T mutant and corrected isogenic line) and ESCs (both wild-type and genetically engineered isogenic αS E46K line). A significantly reduced αS60 level was seen with A53T and E46K mutants (Dettmer, U., et al. (2015). Nat. Commun. 6:7314).
Western Blotting Analysis: A representative lot detected monomeric α-synuclein (αS) as well as αS multimers (αS60, αS80 and αS100) in cytosolic extracts from disuccinimidyl glutarate (DSG) cross-linked primary rat neurons, as well as human HEL erythroid leukemia and M17D neuroblastoma cells (Dettmer, U., et al. (2013). J. Biol. Chem. 288(9):6371-6385).
Research Category
Neuroscience
Neuroscience
Quality
Evalulated by Western Blotting in human fetal brain tissue lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected α-synuclein in 10 µg of human fetal brain tissue lysate.
Western Blotting Analysis: A 1:1,000 dilution of this antibody detected α-synuclein in 10 µg of human fetal brain tissue lysate.
Target description
~14.5 kDa observed. 14.46 kDa (human isoform 1; NACP140), 14.49/14.52 kDa (mouse/rat isoform 1) calculated. Uncharacterized bands may be observed in some lysate(s).
Physical form
Format: Purified
Protein G purified.
Purified mouse IgG2b in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.
Storage and Stability
Stable for 1 year at 2-8°C from date of receipt.
Other Notes
Concentration: Please refer to lot specific datasheet.
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.
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Referencia del producto
Descripción
Precios
Storage Class
12 - Non Combustible Liquids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificados de análisis (COA)
Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»
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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
Ulf Dettmer et al.
Human molecular genetics, 26(18), 3466-3481 (2017-09-16)
α-Synuclein (αS) forms round cytoplasmic inclusions in Parkinson's disease (PD) and dementia with Lewy bodies (DLB). Evidence suggests a physiological function of αS in vesicle trafficking and release. In contrast to earlier tenets, recent work indicates that αS normally exists
Joseph R Patterson et al.
NPJ Parkinson's disease, 8(1), 61-61 (2022-05-25)
β2-adrenoreceptor (β2AR) agonists have been associated with a decreased risk of developing Parkinson's disease (PD) and are hypothesized to decrease expression of both alpha-synuclein mRNA (Snca) and protein (α-syn). Effects of β2AR agonist clenbuterol on the levels of Snca mRNA
John B Sanderson et al.
Brain communications, 2(1), fcaa010-fcaa010 (2020-04-14)
Since researchers identified α-synuclein as the principal component of Lewy bodies and Lewy neurites, studies have suggested that it plays a causative role in the pathogenesis of dementia with Lewy bodies and other 'synucleinopathies'. While α-synuclein dyshomeostasis likely contributes to
Fabian Stahl et al.
Scientific reports, 11(1), 19857-19857 (2021-10-08)
Multiplications, mutations and dysregulation of the alpha synuclein gene (SNCA) are associated with the demise of dopaminergic neurons and are considered to play important roles in the pathogenesis of familial and sporadic forms of Parkinson's disease. Regulation of SNCA expression
Insup Choi et al.
Nature communications, 11(1), 1386-1386 (2020-03-15)
Microglia maintain brain homeostasis by removing neuron-derived components such as myelin and cell debris. The evidence linking microglia to neurodegenerative diseases is growing; however, the precise mechanisms remain poorly understood. Herein, we report a neuroprotective role for microglia in the
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