Recombinant Mouse Alpha-Synuclein (SNCA)

Name: Recombinant Mouse Alpha-Synuclein (SNCA)
Brand: Beta LifeScience
SKU: BLC-03440P
Price: 946.4 USD
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: Antibody / cell therapy targets, Antibody therapeutic / adc target proteins, Recombinant proteins

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Product Overview

Description	Recombinant Mouse Alpha-Synuclein (SNCA) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	O55042
Target Symbol	SNCA
Synonyms	Snca; Syn; Alpha-synuclein; Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor; NACP
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	Tag-Free
Target Protein Sequence	MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPGSEAYEMPSEEGYQDYEPEA
Expression Range	1-140aa
Protein Length	Full Length
Mol. Weight	14.5 kDa
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	KEGG: mmu:20617 STRING: 10090.ENSMUSP00000109907 UniGene: Mm.17484
Tissue Specificity	Expressed in brain (at protein level). Highly expressed in presynaptic terminals in the central nervous system.

Gene Functions References

Taken together, these data suggest that PREP can enhance alpha-synuclein toxicity in vivo. PMID: 29367610
oligodendrocytes but not neurons transform misfolded alpha-Syn into a glial cytoplasmic inclusions-like strain, highlighting the fact that distinct alpha-Syn strains are generated by different intracellular milieus PMID: 29743672
Cardiolipin exposure on the outer mitochondrial membrane modulates alpha-synuclein in Parkinson's disease and cultured cardiomyocyte models. PMID: 29483518
A53T SNCA missense mutation caused impaired light entrainment of the circadian system in mice. PMID: 29865270
Induction of the Immunoproteasome Subunit Lmp7 Links Proteostasis and Immunity in alpha-Synuclein Aggregation Disorders PMID: 29759483
In this study, we assessed the spread of pathology following a localized induction of alphaS inclusions in the lumbar spinal cord following a unilateral injection in the sciatic nerve. Using this paradigm, we demonstrated the ability for alphaS inclusion spread and/or induction along neuroanatomical tracts within the CNS of two alphaS-overexpressing mouse models. PMID: 29976670
These results indicated that integrin CD11b mediates alpha-synuclein-induced NOX2 activation through a RhoA-dependent pathway. PMID: 29154191
High SNCA expression is associated with Parkinson's disease. PMID: 28923922
Snca regulates bone network homeostasis and ovariectomy-induced bone loss PMID: 27378017
These findings provide evidence for a novel mechanism underlying the protective effects of PINK1 against alpha-syn-induced neurodegeneration and highlight a novel therapeutic target for Parkinson's disease treatment. PMID: 28933786
study demonstrates that PLK-2 activity can rapidly change cellular alpha-synuclein levels in cell models and in mice brains, but this process does not require phosphorylation of S129. Instead, it operates via regulation of alpha-synuclein mRNA transcription in an open reading frame-dependent manner PMID: 28648742
the presented data link the Parkinson's disease-associated gene alpha-synuclein to the neuronal cell fate determinant TRIM32. PMID: 27339877
alpha-synuclein levels can be reduced in neurons without impairing (or improving) mitochondrial bioenergetics or distribution PMID: 28462393
Study shows that the age-dependent alpha-syn accumulation is correlated with an elevation of TRPC3 in the mitochondrial fractions isolated from monkey and mouse brains. In animal and cell models, alpha-syn overexpression was accompanied by an elevation of alpha-syn and TRPC3 in the mitochondrial fractions, and alpha-syn downregulation was associated with a reduction of the mitochondrial alpha-syn and TRPC3. PMID: 27904950
plasma concentrations of alpha-synuclein were significantly higher in exercising mice compared to control mice. Our results suggest that exercise may slow the progression of Parkinson's disease by preventing abnormal protein aggregation in brain PMID: 29272304
revealed a prominent modulating effect of alpha-synuclein on the developing DA neurons in substantia nigra (SN) which is the most affected region in PD patients. Yet, alpha-synuclein had no effect on the formation of DA neurons in ventral tegmental area which is much less susceptible to degeneration in PD patients. PMID: 29243900
These new mouse lines are invaluable for fast identification of cells with inactivation of Snca by Cre-recombination and represent useful tools for in vivo studies of alpha-synuclein function and dysfunction. PMID: 27838898
Retinal iron dyshomeostasis due to impaired or altered function of alpha-syn contributes to the visual symptoms associated with Parkinson disease. PMID: 27343690
Results obtained with immuno-spin trapping and immunoprecipitation experiments confirmed formation of alpha-synuclein radicals in dopaminergic neurons of maneb and paraquat exposed mice. PMID: 25952542
Study showed that intracerebral injection of synthetic alpha-synuclein fibrils into adult wild-type marmoset brains (caudate nucleus and/or putamen) resulted in spreading of abundant alpha-synuclein pathologies, which were positive for various antibodies to alpha-synuclein, including phospho Ser129-specific antibody, anti-ubiquitin and anti-p62 antibodies, at three months after injection. PMID: 28148299
Trehalose was also able to restore cell viability to control levels, but pre-formed fibrils (PFFs)still exhibited toxic effects on the cells. These data provide essential information regarding effects of trehalose on alphaSyn accumulation and neuronal survival on exposure to PFF PMID: 28068606
These results suggest that synucleins are important orchestrators of presynaptic terminal topography. PMID: 28052246
C57BL/6J-OlaHsd mice, a substrain of C57BL/6J carrying mutated alpha-synuclein and multimerin-1 genes, have an altered bone phenotype. PMID: 28266709
The findings of this study indicated a functional role of alpha-synuclein in early experimental autoimmune encephalomyelitis by increasing Th1 cell-mediated immune response. PMID: 27565429
synuclein is required for efficient maintenance of animal's balance and coordination in old age. PMID: 27614017
These data show that neurodegenerative processes associated with lysosomal dysfunction may be presynaptically initiated by a concomitant reduction in alpha-synuclein and CSPalpha levels at nerve terminals. PMID: 27881461
synuclein exerts dose-dependent effects on dilation of the exocytotic fusion pore. PMID: 28288128
Data suggest that endocytosis is the principal mechanism by which proteopathic alpha-synuclein aggregates are internalized in primary hippocampal neurons in culture; aggregates are rapidly trafficked along endosomal/lysosomal pathway, where most of the material remains for days as proposed in neurodegenerative synucleinopathies. PMID: 28611062
LRRK2 negatively regulates the clearance of alphaSYN accompanied by down-regulation of the endocytosis pathway; LRRK2 in microglia may function as the offending molecule responsible for neurodegeneration, in terms of down-regulation of alphaSYN clearance. PMID: 27903237
sideroflexin 3 (SFXN3) was found to be a mitochondrial protein localized to the inner mitochondrial membrane. PMID: 28049716
The ability of monomeric alpha-synuclein to enhance ATP synthase efficiency under physiological conditions may be of importance when alpha-synuclein undergoes the misfolding and aggregation PMID: 27733604
Rab7 accumulated in GCase deficient cells, supporting the notion that lysosomal recycling is impaired. Since recombinant GCase can reverse ALR impairment, we anticipate that strategies to restore GCase activity in the brains of both sporadic patients with PD and those with GBA1 mutations will improve autophagy lysosomal pathway, preventing the accumulation of a-synuclein and spread of pathology. PMID: 27378698
Study showed that apoptosis is an important form of cellular degeneration in lipopolysaccharide (LPS-sensitized hypoxic-ischemic (HI) injury in the immature brain. Loss of PINK1 can protect the immature brain against cell apoptosis induced by LPS-sensitized HI injury. Moreover, alpha-Syn plays a neuroprotective role in LPS-sensitized HI brain damage in PINK1-knockout neonatal mice PMID: 27742469
Genetic manipulation of sirtuin 2 levels in vitro and in vivo modulates the levels of alpha-synuclein acetylation, its aggregation, and autophagy. PMID: 28257421
These results indicate that fragmented amyloid-like aggregates of short alpha-syn fibrils are the key pathogenic seeds that trigger prion-like conversion. PMID: 27382062
In summary, we have combined multiple data sets to identify transcripts, which are strong candidates for being phenotypic modifiers, and demonstrated SNCA is a modifier of pathology in motor neuron disease. PMID: 28362802
In alpha-synuclein knock-out mice there was a decrease in neuronal glucose metabolism in cerebral cortex gray matter. PMID: 28039592
alpha-synuclein may have a varying modulating effect on the growth dynamics and the fate of populations of DA neurons. PMID: 27021360
In the olfactory bulb, globus pallidus and substantia nigra pars compacta, alpha-synuclein was expressed, but not in the cerebral cortex, subthalamic nucleus or thalamus. PMID: 26358191
identified alpha-synuclein as a new transcriptional target of p53 PMID: 26833254
High SNCA expression is associated with epilepsy. PMID: 26689812
Data suggest the produced mouse lines represent a set of useful tools for studies of alpha-synuclein normal function and the role of this protein in disease pathogenesis. PMID: 26564109
that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation PMID: 26378614
provides evidence for a novel interaction of alpha-synuclein and SOD1 that might be relevant for neurodegenerative diseases PMID: 26643113
It found that chromosome 1 harbors an expression quantitative trait locus that modulates Sncg expression in the mouse retina, and identified the prefoldin-2 (PFDN2) gene as the candidate upstream modulator of Sncg expression. PMID: 26663874
RNA virus-induced Asyn localizes to endoplasmic reticulum-derived membranes, modulates virus-induced endoplasmic reticulum stress signaling, and inhibits viral replication, growth, and injury in the central nervous system. PMID: 26719256
The response of CPLX1 and Foxp1 levels to SNCA deficiency supports the notion that these factors are regulated by altered physiological function of alpha-synuclein. PMID: 25112678
The pattern of expression and distribution of alpha-synuclein during the development of ciliary body and iris of mice, chick and fish data concluded that alpha-synuclein has important cellular function during eye development of studied animals. PMID: 25997379
Longitudinal Metabolomics Profiling of Parkinson's Disease-Related alpha-Synuclein A53T Transgenic Mice. PMID: 26317866
This would suggest that as complex I-deficient cells have already adapted to their mitochondrial defect, the subsequent toxic effects of alpha-synuclein are reduced. PMID: 26181201

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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.

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