Recombinant Human Alpha-Synuclein (SNCA) Protein (GST)

Name: Recombinant Human Alpha-Synuclein (SNCA) Protein (GST)
Brand: Beta LifeScience
SKU: BLC-03593P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, High-quality recombinant proteins

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Product Overview

Description	Recombinant Human Alpha-Synuclein (SNCA) Protein (GST) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	P37840
Target Symbol	SNCA
Synonyms	Alpha synuclein ; Alpha-synuclein; Alpha-synuclein; isoform NACP140 ; alphaSYN; MGC105443; MGC110988; MGC127560; MGC64356; NACP; Non A beta component of AD amyloid ; Non A4 component of amyloid; Non A4 component of amyloid precursor ; Non-A beta component of AD amyloid; Non-A-beta component of alzheimers disease amyloid ; precursor of; Non-A4 component of amyloid precursor; Non-A4 component of amyloid; precursor of; OTTHUMP00000218549; OTTHUMP00000218551; OTTHUMP00000218552; OTTHUMP00000218553; OTTHUMP00000218554; PARK 1; PARK 4; PARK1; PARK4; Parkinson disease (autosomal dominant; Lewy body) 4; Parkinson disease familial 1; SNCA; Snca synuclein; Snca synuclein; alpha (non A4 component of amyloid precursor); SYN; Synuclein alpha ; Synuclein alpha 140; Synuclein; alpha (non A4 component of amyloid precursor); SYUA_HUMAN
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-GST
Target Protein Sequence	MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVATVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGSIAAATGFVKKDQLGKNEEGAPQEGILEDMPVDPDNEAYEMPSEEGYQDYEPE
Expression Range	1-139AA
Protein Length	Partial
Mol. Weight	41.4kDa
Research Area	Neuroscience
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

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: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.