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Merck
CN

GW22371F

Sigma-Aldrich

Anti-SNCB antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

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UNSPSC代码:
12352203
NACRES:
NA.41
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生物来源

chicken

偶联物

unconjugated

抗体形式

affinity isolated antibody

抗体产品类型

primary antibodies

克隆

polyclonal

表单

buffered aqueous solution

种属反应性

human

技术

western blot: suitable

NCBI登记号

UniProt登记号

运输

wet ice

储存温度

−20°C

靶向翻译后修饰

unmodified

基因信息

human ... SNCB(6620)

一般描述

SNCB (synuclein β) is a 134 amino acids protein, and is homologous to α-synuclein, which is composed of 140 amino acids. It has a putative molecular weight of 19kDa. It shares high homology to PNP14 (phosphoneuroprotein 14) found in bovines. It has a predominant expression in human brain, and is localized mainly to presynaptic nerve terminals. It is a member of synuclein proteins which are cytosolic in nature, and apart from β- and α-, also includes γ-synuclein.

免疫原

Immunogen Sequence: GI # 4507111, sequence 1-134
Recombinant β-synuclein

应用

Anti-SNCB antibody produced in chicken is suitable for western blotting analysis at a dilution of 1:500, for tissue or cell staining at a dilution of 1:200.

生化/生理作用

β-synuclein is associated with Parkinson disease along with other neurodegenerative disorders. The β-synuclein protein is highly homologous to the α-synuclein protein and both may be able to inhibit phospholipase D2 selectively. β-synuclein is also expressed in astrocytes. Both α-synuclein and β-synuclein are abundantly expressed in the central nervous system, but β-synuclein is absent in the pathological inclusions. It is thought to have a protective role during ageing. The reduction in this protein in brain cortex is linked to a subgroup of dementia, which contains Lewy bodies.

外形

Solution in phosphate buffered saline containing 0.02% sodium azide.

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储存分类代码

10 - Combustible liquids

WGK

WGK 1

闪点(°F)

Not applicable

闪点(°C)

Not applicable

个人防护装备

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

法规信息

新产品
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历史批次信息供参考:

分析证书(COA)

Lot/Batch Number

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Vasanthy Vigneswara et al.
PloS one, 8(4), e61442-e61442 (2013-05-01)
Abnormal α-synuclein aggregates are hallmarks of a number of neurodegenerative diseases. Alpha synuclein and β-synucleins are susceptible to post-translational modification as isoaspartate protein damage, which is regulated in vivo by the action of the repair enzyme protein L-isoaspartyl O-methyltransferase (PIMT).
C Lavedan et al.
Genomics, 54(1), 173-175 (1998-11-10)
The beta-synuclein protein is highly homologous to the alpha-synuclein protein for which two mutations were reported in some familial cases of Parkinson disease. It has been shown that both alpha- and beta-synucleins may be able to inhibit phospholipase D2 selectively.
R Jakes et al.
FEBS letters, 345(1), 27-32 (1994-05-23)
Two abundant proteins of 140 and 134 amino acids were purified and sequenced from human brain. They were identified through their reactivity on immunoblots with a partially characterised monoclonal antibody that recognises tau protein in a phosphorylation-dependent manner. The 140
K Tanji et al.
Neuroreport, 12(13), 2845-2848 (2001-10-06)
Although alpha- and beta-synucleins are expressed predominantly in presynaptic nerve terminals, recent studies have demonstrated that alpha-synuclein is also expressed in cultured astrocytes and oligodendrocytes. We determined whether beta-synuclein might be expressed in astrocytes. Beta-synuclein mRNA and protein were detected
Shahin Zibaee et al.
The Journal of biological chemistry, 285(49), 38555-38567 (2010-09-14)
Filamentous inclusions made of α-synuclein are found in nerve cells and glial cells in a number of human neurodegenerative diseases, including Parkinson disease, dementia with Lewy bodies, and multiple system atrophy. The assembly and spreading of these inclusions are likely

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