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Merck
CN

GW22371F

Anti-SNCB antibody produced in chicken

affinity isolated antibody, buffered aqueous solution

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About This Item

NACRES:
NA.41
UNSPSC Code:
12352203
Conjugate:
unconjugated
Clone:
polyclonal
Application:
WB
Citations:
6
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biological source

chicken

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SNCB(6620)

General description

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.

Immunogen

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

Application

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.

Biochem/physiol Actions

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.

Physical form

Solution in phosphate buffered saline containing 0.02% sodium azide.

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Storage Class

10 - Combustible liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

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

Regulatory Information

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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).
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
Katrin Beyer et al.
Brain : a journal of neurology, 133(Pt 12), 3724-3733 (2010-10-21)
Lewy body diseases include dementia with Lewy bodies and Parkinson's disease. Whereas dementia with Lewy bodies and Parkinson's disease can be distinguished as separate clinical entities, the pathological picture is very often identical. α-synuclein aggregation is a key event in
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.
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

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