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 Code
10 - Combustible liquids
WGK
WGK 1
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
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).
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
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
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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