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SAB1404387

Sigma-Aldrich

Monoclonal Anti-SNCB antibody produced in mouse

clone 3G6, purified immunoglobulin, buffered aqueous solution

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3G6, monoclonal

form

buffered aqueous solution

mol wt

antigen ~40.85 kDa

species reactivity

human

technique(s)

capture ELISA: suitable
immunofluorescence: suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

isotype

IgG2aκ

NCBI accession no.

BC002902

UniProt accession no.

Q16143

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... SNCB(6620)

General description

β-Synuclein (SNCB) is present in the presynaptic neuron terminal. It comprises an imperfect KTKEGV sequence at the N-terminus as well as highly acidic and intrinsically disordered regions. SNCB shares sequence similarity with α-synuclein. The SNCB gene is mapped to human chromosome 5q35.2.

Immunogen

SNCB (AAH02902, 1 a.a. ~ 134 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
MDVFMKGLSMAKEGVVAAAEKTKQGVTEAAEKTKEGVLYVGSKTREGVVQGVASVAEKTKEQASHLGGAVFSGAGNIAAATGLVKREEFPTDLKPEEVAQEAAEEPLIEPLMEPEGESYEDPPQEEYQEYEPEA

Biochem/physiol Actions

β-Synuclein (SNCB) may delay the α- synuclein (αS) fibril formation and inhibit its aggregation. SNCB and αS interact with lipid vesicles to form a high degree of α-helical structure. SNCB is implicated in Dementia with Lewy bodies (DLB), a neurodegenerative dementia.

Physical form

Solution in phosphate buffered saline, pH 7.4

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Storage Class Code

10 - Combustible liquids

WGK

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable

Certificates of Analysis (COA)

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James W P Brown et al.
Scientific reports, 6, 36010-36010 (2016-11-04)
α-Synuclein is an intrinsically disordered protein that is associated with the pathogenesis of Parkinson's disease through the processes involved in the formation of amyloid fibrils. α and β-synuclein are homologous proteins found at comparable levels in presynaptic terminals but β-synuclein
Tracey Evans et al.
Brain research, 1681, 1-13 (2017-12-27)
Dementia with Lewy bodies (DLB) is the second most prevalent neurodegenerative dementia, where an accumulation of aggregated fibrillar alpha-synuclein in neurons of limbic and forebrain regions of the brain leads to visual hallucination, cognitive impairment of a fluctuating nature and
Andres Jerez et al.
Journal of clinical oncology : official journal of the American Society of Clinical Oncology, 30(12), 1343-1349 (2012-03-01)
Interstitial deletions of chromosome 5q are common in acute myeloid leukemia (AML) and myelodysplastic syndromes (MDS), pointing toward the pathogenic role of this region in disease phenotype and clonal evolution. The higher level of resolution of single-nucleotide polymorphism array (SNP-A)
Gina M Moriarty et al.
The Journal of biological chemistry, 292(39), 16368-16379 (2017-07-16)
α-Synuclein (αS) is the primary protein associated with Parkinson's disease, and it undergoes aggregation from its intrinsically disordered monomeric form to a cross-β fibrillar form. The closely related homolog β-synuclein (βS) is essentially fibril-resistant under cytoplasmic physiological conditions. Toxic gain-of-function

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