Recombinant Human alpha-Synuclein / SNCA Protein

Name: Recombinant Human alpha-Synuclein / SNCA Protein
Brand: Beta LifeScience
SKU: BLPSN-0168
Availability: InStock

Collections: Other recombinant proteins, Recombinant proteins

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Product Overview

Tag	N/A
Host Species	Human
Accession	P37840
Synonym	NACP, PARK1, PARK4, PD1
Background	Alpha-Synuclein (alpha-Syn), also known as NACP or SNCA, exists as at least two structural isoforms: one is helix-rich, membrane-bound form that both the N- and C-terminal regions of alpha-synuclein are tightly associated with membranes and the other is disordered, cytosolic form. Synuclein is found predominantly in the presynaptic termini, in both free or membrane-bound forms. SNCA is extensively localized in nucleus of neurons. It has been shown that alpha-Synuclein was highly expressed in the mitochondria in olfactory bulb, hippocampus, striatum, and thalamus, where the cytosolic alpha-Synuclein was also rich. Normally the unstructured soluble type of alpha-synuclein can aggregate to form insoluble fibrils in pathological conditions characterized by Lewy bodies, such as Parkinson's disease, dementia with Lewy bodies and multiple system atrophy. SNCA abnormality and mitochondrial deficiency are two major changes in the brain of patients with Parkinson's disease (PD). In addition, alpha-synuclein is an abundant component of Lewy bodies in sporadic Parkinson's disease and diffuse Lewy body disease.
Description	A DNA sequence encoding the mature form of human SNCA isoform 1 (P37840-1) (Met 1-Ala 140) was expressed and purified.
Source	E.coli
Predicted N Terminal	Met 1
AA Sequence	Met 1-Ala 140
Molecular Weight	The recombinant human SNCA consisting of 140 a.a. and has a calculated molecular mass of 14.5 kDa. It migrates as an approximately 19 kDa band in SDS-PAGE under reducing conditions.
Purity	>97% as determined by SDS-PAGE
Endotoxin	Please contact us for more information.
Bioactivity	Please contact us for detailed information
Formulation	Lyophilized from sterile PBS, pH 7.4.
Stability	The recombinant proteins are stable for up to 1 year from date of receipt at -70°C.
Usage	For Research Use Only
Storage	Store the protein under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.

Target Details

Target Function	Neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. Participates as a monomer in synaptic vesicle exocytosis by enhancing vesicle priming, fusion and dilation of exocytotic fusion pores. Mechanistically, acts by increasing local Ca(2+) release from microdomains which is essential for the enhancement of ATP-induced exocytosis. Acts also as a molecular chaperone in its multimeric membrane-bound state, assisting in the folding of synaptic fusion components called SNAREs (Soluble NSF Attachment Protein REceptors) at presynaptic plasma membrane in conjunction with cysteine string protein-alpha/DNAJC5. This chaperone activity is important to sustain normal SNARE-complex assembly during aging. Plays also a role in the regulation of the dopamine neurotransmission by associating with the dopamine transporter (DAT1) and thereby modulating its activity.
Subcellular Location	Cytoplasm. Membrane. Nucleus. Cell junction, synapse. Secreted.
Protein Families	Synuclein family
Database References	HGNC: 11138 OMIM: 127750 KEGG: hsa:6622 STRING: 9606.ENSP00000338345 UniGene: Hs.21374
Associated Diseases	Parkinson disease 1, autosomal dominant (PARK1); Parkinson disease 4, autosomal dominant (PARK4); Dementia Lewy body (DLB)
Tissue Specificity	Highly expressed in presynaptic terminals in the central nervous system. Expressed principally in brain.

Gene Functions References

Results provide evidence of the role of SNCA in opiate dependence PMID: 21309955
The molecular basis and clinical relevance of statistically decreased alphaSyn pathology in schizophrenic brain versus aged controls is unknown and needs further elucidation as will be necessary for its incidence and relevance in chronic affective disorders. PMID: 19198857
Elevated levels of insoluble alpha-Syn seen in brains of patients with Parkinson's and dementia are higher than that of Parkinson brains, for insoluble and insoluble/soluble alpha-Syn, respectively, with a highly significant difference between the two groups. PMID: 20599975
Data suggest that the key molecular scaffold most effective in inhibiting and destabilizing self-assembly by alphaS requires: (i) aromatic elements for binding to the alphaS monomer/oligomer and (ii) vicinal hydroxyl groups present on a single phenyl ring. PMID: 21443877
[review] The role of alpha-syn is summarized in synaptic vesicle recycling, neurotransmitter synthesis and release and synaptic plasticity, as well as the possible relevance between the loss of normal alpha-syn functions in disease conditions. PMID: 21167933
Age-related accumulation of neuromelanin might induce alpha-synuclein over-expression and thereby make dopamine neurons more vulnerable to injuries. PMID: 21461961
alpha-Synuclein function in promoting cell proliferation is associated with its microtubule assembly activity with the functional domain localized in its carboxyl-terminal part. PMID: 21331461
Association ofalpha-synuclein with Rab attachment receptor protein and soluble sensitive factor attachment receptors (SNAREs) highlights a key role for membrane transport defects in alpha-synuclein-mediated pathology. PMID: 21439320
Our result strongly indicates that Parkinson's disease, induced by alpha-SYN mutation, is evoked by deregulation of the AKT-signaling cascade. PMID: 21474915
Genetic mutations in the alpha-synuclein gene can lead to Parkinson's disease, but even in these patients, age-dependent physiological changes or environmental exposures appear to be involved in disease presentation. PMID: 21238487
Our results imply that CSF alpha-synuclein is currently unsuitable as biomarker to differentiate between PD and AP. PMID: 21236518
[review] Presynaptic function is implicated in the function/dysfunction of alpha-synuclein, the first gene shown to contribute to Parkinson's disease (PD), in this review of genetic models of PD. PMID: 20969957
In the Caucasian patient-control series examined, risk for Parkinson disease is influenced by variation in SNCA and tau proteins but not glycogen synthase kinase (GSK)beta3. PMID: 21159074
Overexpression of alpha-Syn transgene alters dopamine efflux and dopamine D2 receptor modulation of corticostriatal glutamate release at a young age in mice. PMID: 21488084
An artificial microRNA-embedded human SNCA silencing vector is expressed lacks toxicity in rat PC12 cells in which rat SNCA is not silenced and has reduced toxicity in human SH-SY5Y cells in which hSNCA is silenced. PMID: 21338582
Patients with multiple system atrophy may have a cerebrospinal fluid environment particularly favorable for alpha-synuclein fibril formation. PMID: 21215793
Iron up-regulates alpha-synuclein and induces aggregation through the predicted iron responsive element (IRE) in the 5'-untranslated region (UTR) of human alpha-synuclein mRNA. PMID: 20383623
an association of the two SNPs in 4q22/SNCA with the age of onset of Parkinson's disease PMID: 21044948
Findings suggest that alpha-synuclein pathology is associated with Tar DNA-binding protein-43 accumulation in Lewy body disease. PMID: 20669025
Attenuation of nigral SNCA pathology and dopaminergic neurodegeneration by inhibition of NADPH oxidase and iNOS supports a causative relation between inflammation-mediated SNCA pathologic alterations and chronic dopaminergic neurodegeneration. PMID: 21245015
Data describe spontaneous accumulation of hyperphosphorylated tau in striata of a mouse model of Parkinsonism, which overexpresses human a-Synuclein under the PDGF promoter. PMID: 21453448
Direct replication of single nucleotide polymorphisms (SNPs) within SNCA and BST1 confirmed these two genes to be associated with the Parkinson's Disease in the Netherlands. PMID: 21248740
Transgenic alpha-synuclein localizes to the mitochondrial membranes under conditions of proteasomal inhibitory stress; this localization coincides with selective age-related mitochondrial complex I inhibition. PMID: 20887775
Synphilin-1 inhibits alpha-synuclein degradation by the proteasome. PMID: 21103907
From crystal structures of fusions between maltose-binding protein and four segments of alpha-synuclein, the study traces a virtual model of the first 72 residues of alpha -synuclein. PMID: 21462277
In transgenic mice, the norepinephrine systems may be more vulnerable than dopamine systems to toxic effects of aberrant alpha-synuclein; this is in line with the major damage to the noradrenaline system that occurs in patients with Parkinson's disease. PMID: 19152986
In patients diagnosed with dementia with Lewy bodies, lower cerebrospinal fluid alpha-synuclein levels may perhaps be associated with lower cognitive performance, in comparison to patients who are diagnosed with Alzheimer's disease. PMID: 20847452
A novel function for BAG5 as a modulator of CHIP E3 ubiquitin ligase activity with implications for CHIP-mediated regulation of alpha-syn oligomerization. PMID: 21358815
Single-nucleotide polymorphisms in SNCA (rs356219; P = 5.5 x 10(-4) ) is significantly associated with Parkinson's disease PMID: 21425343
alpha-Synuclein thus exerts a primary and direct effect on the morphology of an organelle long implicated in the pathogenesis of Parkinson disease. PMID: 21489994
evidence that alpha-synuclein is a cellular ferrireductase, responsible for reducing iron (III) to bio available iron (II) PMID: 21249223
study found a significant association between the NACP-Rep1 length polymorphism and Beck Depression Inventory (BDI) score; analysis revealed no further association between the In4 polymorphism or between the mRNA expression of SNCA and the BDI score PMID: 21271299
mechanistic insights on the role alpha-synuclein in modulating neurodegenerative phenotypes by regulation of Akt-mediated cell survival signaling in vivo PMID: 21304957
overexpression of alpha-syn may cause mitochondrial defects in dopaminergic neurons of the substantia nigra through an association with adenylate translocator and activation of mitochondria-dependent cell death pathways PMID: 21310263
data demonstrate an elevated state of tauopathy in striata of the A53T alpha-Syn mutant mice, suggesting that tauopathy is a common feature of synucleinopathies PMID: 21445308
REVIEW: alpha-Synuclein in Parkinson disease and other neurodegenerative disorders PMID: 21342025
Data suggest that membrane lipid modification in oligodendroglial cells containing SUMO-1 promotes the formation of alpha-synuclein inclusion bodies resembling protein aggregates in neurodegenerative disease. PMID: 20725866
Data suggest that low SMN levels are associated with significantly lower alpha-synuclein expression, and that alpha-synuclein may be a genetic modifier or biomarker of spinal muscular atrophy. PMID: 20640532
SNCA locus duplication carriers: from genetics to Parkinson disease phenotypes PMID: 21412942
Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination PMID: 21466165
analysis of the mechanism of membrane permeabilization by oligomeric alpha-synuclein PMID: 21179192
the relation between membrane physical properties and AS binding affinity and dynamics that presumably define protein localization in vivo and, thereby, the role of AS in the physiopathology of Parkinson disease. PMID: 21330368
MMP3 digestion of alpha-synuclein in DA neurons plays a pivotal role in the progression of Parkinson disease through modulation of alpha-synuclein in aggregation, Lewy body formation, and neurotoxicity PMID: 21330369
Coordination features and affinity of the Cu(2)+ site in the alpha-synuclein protein of Parkinson's disease PMID: 21319811
This study confirms the association between PD and both SNCA SNPs and the H1 MAPT haplotype. PMID: 21391235
In this work Cu(ii) coordination to peptide fragments encompassing residues 45-55 of synuclein alpha has been exhaustively characterized, including systems containing the inherited mutations E46K and A53T, as model peptides of the His-50 site. PMID: 21212878
results support the hypothesis that WT and A53T alpha-synuclein has an important role in the initiation and maintenance of inflammation in Parkinson's disease PMID: 21255620
The combined data indicate that the A30P mutation does not cause changes in the number, location and overall arrangement of beta-strands in amyloid fibrils of alpha-synuclein. PMID: 21280130
Data suggest that mutations in alpha-synuclein may impair specific functional domains, leaving others intact. PMID: 21272100
Single locus analysis showed that G/G SNCA and H1/H1 MAPT risk genotypes were over-represented in patients with Parkinson disease compared with controls PMID: 21054681

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