Recombinant Human alpha-Synuclein / SNCA Protein

Beta LifeScience SKU/CAT #: BLPSN-0168

Recombinant Human alpha-Synuclein / SNCA Protein

Beta LifeScience SKU/CAT #: BLPSN-0168
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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
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

  1. Results provide evidence of the role of SNCA in opiate dependence PMID: 21309955
  2. 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
  3. 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
  4. 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
  5. [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
  6. Age-related accumulation of neuromelanin might induce alpha-synuclein over-expression and thereby make dopamine neurons more vulnerable to injuries. PMID: 21461961
  7. 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
  8. 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
  9. Our result strongly indicates that Parkinson's disease, induced by alpha-SYN mutation, is evoked by deregulation of the AKT-signaling cascade. PMID: 21474915
  10. 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
  11. Our results imply that CSF alpha-synuclein is currently unsuitable as biomarker to differentiate between PD and AP. PMID: 21236518
  12. [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
  13. 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
  14. 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
  15. 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
  16. Patients with multiple system atrophy may have a cerebrospinal fluid environment particularly favorable for alpha-synuclein fibril formation. PMID: 21215793
  17. 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
  18. an association of the two SNPs in 4q22/SNCA with the age of onset of Parkinson's disease PMID: 21044948
  19. Findings suggest that alpha-synuclein pathology is associated with Tar DNA-binding protein-43 accumulation in Lewy body disease. PMID: 20669025
  20. 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
  21. 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
  22. 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
  23. 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
  24. Synphilin-1 inhibits alpha-synuclein degradation by the proteasome. PMID: 21103907
  25. 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
  26. 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
  27. 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
  28. 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
  29. Single-nucleotide polymorphisms in SNCA (rs356219; P = 5.5 x 10(-4) ) is significantly associated with Parkinson's disease PMID: 21425343
  30. 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
  31. evidence that alpha-synuclein is a cellular ferrireductase, responsible for reducing iron (III) to bio available iron (II) PMID: 21249223
  32. 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
  33. mechanistic insights on the role alpha-synuclein in modulating neurodegenerative phenotypes by regulation of Akt-mediated cell survival signaling in vivo PMID: 21304957
  34. 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
  35. 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
  36. REVIEW: alpha-Synuclein in Parkinson disease and other neurodegenerative disorders PMID: 21342025
  37. 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
  38. 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
  39. SNCA locus duplication carriers: from genetics to Parkinson disease phenotypes PMID: 21412942
  40. Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination PMID: 21466165
  41. analysis of the mechanism of membrane permeabilization by oligomeric alpha-synuclein PMID: 21179192
  42. 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
  43. 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
  44. Coordination features and affinity of the Cu(2)+ site in the alpha-synuclein protein of Parkinson's disease PMID: 21319811
  45. This study confirms the association between PD and both SNCA SNPs and the H1 MAPT haplotype. PMID: 21391235
  46. 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
  47. 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
  48. 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
  49. Data suggest that mutations in alpha-synuclein may impair specific functional domains, leaving others intact. PMID: 21272100
  50. 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.

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