MABN389
Anti-Aggregated a-Synuclein Antibody, clone 5G4
clone 5G4, from mouse, purified by affinity chromatography
Szinonimák:
Aggregated a-synuclein, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP
Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez
Összes fotó(1)
About This Item
UNSPSC kód:
12352203
eCl@ss:
32160702
NACRES:
NA.41
klón:
5G4, monoclonal
application:
ELISA
IHC
WB
IHC
WB
faj reaktivitás:
human
technika/technikák:
ELISA: suitable
immunohistochemistry: suitable
western blot: suitable
immunohistochemistry: suitable
western blot: suitable
citations:
32
Javasolt termékek
biológiai forrás
mouse
Minőségi szint
antitest forma
affinity purified immunoglobulin
antitest terméktípus
primary antibodies
klón
5G4, monoclonal
tisztítva
affinity chromatography
faj reaktivitás
human
technika/technikák
ELISA: suitable
immunohistochemistry: suitable
western blot: suitable
izotípus
IgG1κ
NCBI elérési szám
UniProt elérési szám
kiszállítva
dry ice
célzott transzláció utáni módosítás
unmodified
Géninformáció
human ... SNCA(6622)
Általános leírás
α-Synuclein, also known as Non-A beta component of AD amyloid or Non-A4 component of amyloid, or NACP, and encoded by the gene SNCA/NACP/PARK1, is a protein originally identified as non-Abeta component protein (NACP) in the amyloid enriched fraction isolated from Alzheimer’s brain tissue. α-Synuclein is expressed in neural tissue and non-neural tissues too. In neurons, α-Synuclein is localized to the nucleus, presynaptic termini and mitochondria of certain brain regions. α-Synuclein is a molecular chaperone that binds various proteins and compounds including synaptobrevin-2 protein and membrane phospholipids and is involved in vesicle trafficking and membrane transport within neurons. Natural, non-mutated α-Synuclein has autoproteolytic activity and naturally forms stable alpha helical tetramers. However, mutated α-Synuclein can aggregate to form insoluble pathological complexes such as Lewy Bodies inside neurons. Lewy Bodies also contain ubiquitin and it is thought that they are evidence of disrupted proteasome function with regards to α-synuclein but research is still continuing.
Pepscan epitope mapping experiments showed that the epitope of 5G4 seems to be hidden inside full-length a-synuclein in aqueous solution, and this fact could depend on a specific conformation of the molecule. Thus, after conformational change, like b-sheet building, the binding structure of 5G4 may be accessible in biological samples.
This antibody can be used as a sandwich ELISA pair with Cat. No. MABN633, Anti-a-Synuclein, clone 10D2.
Pepscan epitope mapping experiments showed that the epitope of 5G4 seems to be hidden inside full-length a-synuclein in aqueous solution, and this fact could depend on a specific conformation of the molecule. Thus, after conformational change, like b-sheet building, the binding structure of 5G4 may be accessible in biological samples.
This antibody can be used as a sandwich ELISA pair with Cat. No. MABN633, Anti-a-Synuclein, clone 10D2.
Immunogén
KLH-conjugated linear peptide corresponding to human Aggregated a-Synuclein.
Alkalmazás
Research Category
Neuroscience
Neuroscience
Research Sub Category
Neurodegenerative Diseases
Neurodegenerative Diseases
This Anti-Aggregated a-Synuclein Antibody, clone 5G4 is validated for use in western blotting, IHC & ELISA for the detection of Aggregated a-Synuclein.
Western Blotting Analysis: 2 µg/mL from a representative lot detected Aggregated a-Synuclein in human brain tissue lysate.
ELISA Analysis: A representative lot from an independent laboratory detected Aggregated a-Synuclein in a sandwich ELISA with Cat. No. MABN633, Anti-a-Synuclein, clone 5G4 (Kovacs, G. G., et al. (2012). Acta Neuropathol. 123(1):37-50.).
ELISA Analysis: A representative lot from an independent laboratory detected Aggregated a-Synuclein in a sandwich ELISA with Cat. No. MABN633, Anti-a-Synuclein, clone 5G4 (Kovacs, G. G., et al. (2012). Acta Neuropathol. 123(1):37-50.).
Minőség
Evaluated by Immunohistochemistry in brain tissue from a Parkinson′s disease patient.
Immunohistochemistry Analysis: A representative lot detected Aggregated a-Synuclein in brain tissue from a Parkinson′s disease patient.
Immunohistochemistry Analysis: A representative lot detected Aggregated a-Synuclein in brain tissue from a Parkinson′s disease patient.
Cél megnevezése
~15 kDa observed. Uncharacterized band(s) may be observed in some cell lysates.
Fizikai forma
Affinity purified
Purified mouse monoclonal IgG1κ in buffer containing PBS without preservatives.
Tárolás és stabilitás
Stable for 1 year at -20°C from date of receipt.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Handling Recommendations: Upon receipt and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage IgG and affect product performance.
Egyéb megjegyzések
Jogi nyilatkozat
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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javasolt
Tárolási osztály kódja
12 - Non Combustible Liquids
WGK
WGK 2
Lobbanási pont (F)
Not applicable
Lobbanási pont (C)
Not applicable
Analitikai tanúsítványok (COA)
Analitikai tanúsítványok (COA) keresése a termék sarzs-/tételszámának megadásával. A sarzs- és tételszámok a termék címkéjén találhatók, a „Lot” vagy „Batch” szavak után.
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Az Ön által nemrégiben megvásárolt termékekre vonatkozó dokumentumokat a Dokumentumtárban találja.
Dalila G Ordonez et al.
Neuron, 97(1), 108-124 (2017-12-19)
Genetics and neuropathology strongly link α-synuclein aggregation and neurotoxicity to the pathogenesis of Parkinson's disease and related α-synucleinopathies. Here we describe a new Drosophila model of α-synucleinopathy based on widespread expression of wild-type human α-synuclein, which shows robust neurodegeneration, early-onset
Rizwanul Haque et al.
Oncotarget, 11(6), 634-649 (2020-02-29)
Insulin-signalling is an important pathway in multiple cellular functions and organismal ageing across the taxa. A strong association of insulin-signalling with Parkinson's disease (PD) has been proposed but the exact nature of molecular events and genetic associations are yet to
Irene Hana Flønes et al.
Biomolecules, 12(6) (2022-06-25)
Idiopathic Parkinson's disease (iPD) is characterized by degeneration of the dopaminergic substantia nigra pars compacta (SNc), typically in the presence of Lewy pathology (LP) and mitochondrial respiratory complex I (CI) deficiency. LP is driven by α-synuclein aggregation, morphologically evolving from
Tomasz Brudek et al.
Journal of neurochemistry, 136(1), 172-185 (2015-10-16)
Together with Parkinson's disease (PD) and dementia with Lewy bodies, multiple system atrophy (MSA) is a member of a diverse group of neurodegenerative disorders termed α-synucleinopathies. Previously, it has been shown that α-synuclein, parkin, and synphilin-1 display disease-specific transcription patterns
Leping Sun et al.
Brain and behavior, 9(8), e01352-e01352 (2019-07-10)
Chaperone-mediated autophagy (CMA) is an autophagy-lysosome pathway (ALP) that is different from the other two lysosomal pathways, namely, macroautophagy and microautophagy, and can selectively degrade cytosolic proteins in lysosomes without vesicle formation. CMA activity declines in neurodegenerative diseases such as
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