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Merck

S3062

Sigma-Aldrich

Anti-α-Synuclein antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Szinonimák:

Anti-SNCA

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About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

IgG fraction of antiserum

antitest terméktípus

primary antibodies

klón

polyclonal

form

buffered aqueous solution

molekulatömeg

antigen 19 kDa

faj reaktivitás

rat, human

technika/technikák

immunohistochemistry (formalin-fixed, paraffin-embedded sections): 1:200 using formic acid treated sections of Alzheimer′s Disease brain
microarray: suitable
western blot: 1:1,000 using extract of rat brain homogenate

UniProt elérési szám

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... SNCA(6622)
rat ... Snca(29219)

Általános leírás

The synucleins are a family of soluble presynaptic proteins that are abundant in neurons and include α-synuclein, β-synuclein, and γ-synuclein. Human α-synuclein (also known as the non-amyloid component of plaques precursor protein or NACP) is a 140-amino acid polypeptide that is encoded by a gene on chromosome 4. It was originally isolated from plaques of Alzheimer′s disease (AD) brains as a 19 kDa protein precursor of the highly hydrophobic 35-amino acid peptide, nonamyloid component (NAC) of plaques. The NAC can self-aggregate into fibrils and induce aggregation of the β-amyloid peptide. α-Synuclein is highly abundant in presynaptic terminals, and is a major component of Lewy bodies (LBs). Pathogenic point mutations in the α-synuclein gene are linked to familial Parkinson′s disease (PD) in rare kindreds. However, most neurodegenerative disorders with LBs are associated with abnormal accumulation of wild-type, α-synuclein. α-Synuclein is expressed primarily in brain, but is also expressed in low levels in all tissues examined except liver.

Egyediség

Rabbit polyclonal anti-α-Synuclein antibody recognizes human and rat α-synuclein. Staining of α-synuclein in immunoblotting is specifically inhibited by the immunizing peptide

Immunogen

synthetic peptide corresponding to a sequence near the C-terminus of human α-synuclein (amino acids 111-132 with C-terminally added lysine) conjugated to KLH. This sequence is highly conserved (90% homology) in mouse and rat α-synuclein. This sequence has no homology with β- and γ-synuclein.

Alkalmazás

Rabbit polyclonal anti-α-Synuclein antibody is used to tag α-Synuclein for detection and quantitation by immunocytochemical and immunohistochemical (IHC) techniques, such as immunoblotting. It is also used as a probe to determine the presence and roles of α-Synuclein in plaques of Alzheimer′s disease (AD) brains.

Fizikai forma

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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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Tárolási osztály kódja

10 - Combustible liquids

WGK

WGK 3

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 ügyfelek ezeket is megtekintették

Extracellular truncated tau causes early presynaptic dysfunction associated with Alzheimer?s disease and other tauopathies
Florenzano F, et al.
Oncotarget, 8(39), 64745-64778 (2017)
Identification of a caspase-derived N-terminal tau fragment in cellular and animal Alzheimer's disease models
Corsetti V, et al.
Molecular and Cellular Neurosciences, 38(3), 381-392 (2008)
Lysosomal dysfunction in the brain of a mouse model with intraneuronal accumulation of carboxyl terminal fragments of the amyloid precursor protein
Kaur G, et al.
Molecular Psychiatry, 22(7), 981-981 (2017)
Geert Callewaert et al.
Frontiers in genetics, 11, 266-266 (2020-05-28)
The yeast Saccharomyces cerevisiae is a powerful model to study the molecular mechanisms underlying α-synuclein (α-syn) cytotoxicity. This is due to the high degree of conservation of cellular processes with higher eukaryotes and the fact that yeast does not endogenously
Clinical, Histological, and Immunohistochemical Findings in Inclusion Body Myositis
Camargo L, et al.
BioMed Research International, 2018 (2018)

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