GW22371F
Anti-SNCB antibody produced in chicken
affinity isolated antibody, buffered aqueous solution
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
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.
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_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)
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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).
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
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
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
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.
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