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Recombinant Rat Alpha-synuclein (Snca)

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  • 中文名稱：
    大鼠Snca重組蛋白
  • 貨號：
    CSB-EP021912RAe0
  • 規(guī)格：
    ￥1836
  • 促銷：
    現(xiàn)貨重組蛋白特價促銷
  • 圖片：
    • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • 其他：

產(chǎn)品詳情

  • 純度：
    Greater than 90% as determined by SDS-PAGE.
  • 基因名：
    Snca
  • Uniprot No.：
  • 別名：
    Snca; Alpha-synuclein
  • 種屬：
    Rattus norvegicus (Rat)
  • 蛋白長度：
    Full Length
  • 來源：
    E.coli
  • 分子量：
    41.5kDa
  • 表達區(qū)域：
    1-140aa
  • 氨基酸序列
    MDVFMKGLSKAKEGVVAAAEKTKQGVAEAAGKTKEGVLYVGSKTKEGVVHGVTTVAEKTKEQVTNVGGAVVTGVTAVAQKTVEGAGNIAAATGFVKKDQMGKGEEGYPQEGILEDMPVDPSSEAYEMPSEEGYQDYEPEA
    Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
  • 蛋白標(biāo)簽：
    N-terminal GST-tagged
  • 產(chǎn)品提供形式：
    Liquid or Lyophilized powder
    Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
  • 緩沖液：
    Tris-based buffer,50% glycerol
  • 儲存條件：
    Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
  • 保質(zhì)期：
    The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
    Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
  • 貨期：
    3-7 business days
  • 注意事項：
    Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
  • Datasheet & COA：
    Please contact us to get it.

產(chǎn)品評價

靶點詳情

  • 功能：
    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.
  • 基因功能參考文獻：
    1. Calcium binds to the C terminus of alpha-synuclein, therewith increasing its lipid-binding capacity. Using CEST-NMR, we reveal that alpha-synuclein interacts with isolated synaptic vesicles with two regions, the N terminus, already known from studies on SUVs, and additionally via its C terminus, which is regulated by the binding of calcium. PMID: 29459792
    2. alphasynuclein induces apoptosis of astrocytes by causing dysfunction of the endoplasmic reticulumGolgi compartment. PMID: 29749529
    3. induces the clustering of synaptic vesicles by double-anchor mechanism PMID: 27640673
    4. The results suggest that Zn caused Ubiquitin proteasome system impairment, resulting in alpha-synuclein aggregation subsequently leading to dopaminergic neurodegeneration, and that Zn-induced Parkinsonism exhibited positive L-Dopa response similar to sporadic PD. PMID: 29198021
    5. FKBP12 contributes to alpha-synuclein toxicity by regulating the calcineurin-dependent phosphoproteome. PMID: 29229832
    6. Exposure to the Functional Bacterial Amyloid Protein Curli Enhances Alpha-Synuclein Aggregation in Aged Fischer 344 Rats and Caenorhabditis elegans PMID: 27708338
    7. E46K alpha-synuclein pathological mutation causes cell-autonomous toxicity without altering protein turnover or aggregation. PMID: 28900007
    8. 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
    9. Using single-molecule microscopy and photo-bleaching approaches, the authors most frequently found 70 alpha-synuclein-green fluorescent fusion proteins per vesicle. Although this number is high enough to modulate physical membrane properties, it is also strikingly similar to the number of synaptobrevins, a putative interaction partner of alpha-synuclein, per vesicle. PMID: 27477055
    10. TMEM175 deficiency impairs lysosomal and mitochondrial function and increases alpha-synuclein aggregation. PMID: 28193887
    11. we documented that ceftriaxone interacts with alpha-synuclein inhibiting its pathological aggregation and that a cyclical treatment with this molecule in a patient with adult-onset Alexander's disease halted, and partly reversed, the progression of neurodegeneration, suggests the possibility of a chaperone-like effect of ceftriaxone on protein involved in specific neurodegenerative diseases. PMID: 27133445
    12. The findings of this study confirm that alpha-synuclein interacts with membranes to affect Ca(2+) signalling in a structure-specific manner and the oligomeric beta-sheet-rich alpha-synuclein species ultimately leads to Ca(2+) dysregulation and Ca(2+)-dependent cell death. PMID: 26989132
    13. alpha-synuclein plays a crucial role in motor and sensory function regulation, in which, the underlying mechanism may be linked to the regulation of apoptosis associated with apoptotic gene (Bax, Bcl2) and neurotrophic factors expression (NGF, BDNF and NT3). PMID: 26822976
    14. the unaltered SNCA levels observed following ZSCAN21 down-regulation in the rat brain, possibly due to compensatory mechanisms, imply that ZSCAN21 is not a master regulator of SNCA in vivo. PMID: 26907683
    15. that loss of glucocerebrosidase function may contribute to SNCA accumulation through inhibition of autophagy via PPP2A inactivation PMID: 26378614
    16. We conclude that alphaSyn overexpression impairs neurite outgrowth and augments axonal degeneration, whereas axonal vesicle transport and autophagy are severely altered. PMID: 26158517
    17. The destabilization of physiological tetramers by PD-causing missense mutations and the neurotoxicity and inclusions induced by markedly decreasing tetramers suggest that decreased alpha-helical tetramers and increased unfolded monomers initiate pathogenesis. PMID: 26076669
    18. Results show that hydrostatic pressure is associated with a transition from monomeric to higher order alpha-synuclein aggregates and that increased pressure reduces the level of PLCbeta1 and the amount of alpha-synuclein/PLCbeta1 complexes. PMID: 26434717
    19. The data suggest that a-syn is involved in the regulation of synaptic plasticity in the ENS during early postnatal life and adult age. PMID: 25896939
    20. Mitochondrial impairment disturbs the autophagic flux and leads to the accumulation of exogenously applied alpha-synuclein PMID: 26212128
    21. the major toxic role of SNCA is related to its extracellular species and further supports a protective role of intracellular SNCA aggregation PMID: 25484190
    22. comparison between two types of alpha-synuclein showed that A53T mutated alpha-synuclein was more effective to establish a Parkinson disease (PD) model, and the model based A53T mutated alpha-synuclein was a suitable model for early-onset PD PMID: 26192120
    23. LRRK2 inhibition alleviates alpha-synuclein gene-induced neurodegeneration in the rat Parkinson's disease model. PMID: 26078453
    24. Cx3cl1 overexpression suppresses alpha-synuclein-mediated neurodegeneration. PMID: 25195598
    25. alpha-synuclein knockdown is neuroprotective in the rotenone model of PD and indicates that endogenous alpha-synuclein contributes to the specific vulnerability of dopaminergic neurons to systemic mitochondrial inhibition PMID: 26075822
    26. shed light on the potential roles of mutant alpha-synuclein in the pathogenesis of Parkinson's disease PMID: 24833599
    27. suggest that the N terminus of alpha-Syn is essential for the regulation of mitochondrial membrane permeability PMID: 25446002
    28. In the neuronal plasma membrane, alpha-synuclein caused synaptotoxic failure associated with a decrease in membrane proteins. PMID: 25669123
    29. a tight link between the intracellular level of alpha-synuclein and maturation capacity of primary oligodendrocyte progenitor cells PMID: 25019582
    30. These results suggest alpha-synuclein as a pathological link between chronic effects of traumatic brain injury and Parkinson's disease. PMID: 25251017
    31. It impairs maturation of oligodendrocyte progenitors thereby contributing to multiple system atrophy. PMID: 24698767
    32. CHIP can mediate the degradation of alpha synuclein aggregates in vivo PMID: 24664141
    33. extracellular ASN is involved in GSK-3beta-dependent Tau hyperphosphorylation, which leads to microtubule destabilization PMID: 24722055
    34. Results indicate the critical involvement of PAR2-NF-kappaB signaling in the upregulation of alpha-synuclein and motor dysfunction in the rodent model of Parkinsons disease. PMID: 24747612
    35. S-Nitrosylating protein disulphide isomerase plays a significant role in neurological disorders related to alpha-syn aggregation. PMID: 25090657
    36. LRRK2 expression in the wild-type rat midbrain remained undetected under nonpathological conditions, LRRK2 became highly expressed in iNOS-positive myeloid cells in the substantia nigra in response to alpha-synuclein overexpression or LPS exposures PMID: 24927544
    37. onjisaponin B was able to induce autophagy and accelerate both the removal of mutant huntingtin and A53T alpha-synuclein, which are highly associated with Huntington disease and Parkinson disease, respectively PMID: 24248062
    38. Changes in alpha-synuclein expression with age, including a baseline of accumulating synucleinopathies in the healthy aging submucosal plexus PMID: 23809578
    39. Our data show that changes in the S129 residue of alpha-synuclein influence the rate of pathology and neurodegeneration PMID: 23567651
    40. Extracellular alpha-synuclein induces calpain-dependent overactivation of cyclin-dependent kinase 5 in vitro. PMID: 23954626
    41. Inhibition of Nrf2/HO-1 leads to more alpha-syn aggregation and greater toxicity induced by iron, creating a vicious cycle of iron accumulation, alpha-syn aggregation and HO-1 disruption in PD. PMID: 23454680
    42. VDAC1 has a role in alpha-synuclein-induced dopaminergic neuron toxicity in rats PMID: 23291291
    43. Results suggest that macrophages play an active phagocytotic role in removing alpha-SYNC aggregates that accumulate with age in the neural circuitry of the gut. PMID: 23441091
    44. Accumulation of aggregated alpha-synuclein is triggered in substantia nigra in response to environmental toxins later in life. PMID: 23567316
    45. Exophagy, with or without expression of TPPP, may be an important physiological mechanism for unconventional secretion of alpha-synuclein from dopaminergic neurons. PMID: 23629650
    46. TFEB is a key player in the induction of alpha-synuclein-induced toxicity and Parkinson disease pathogenesis PMID: 23610405
    47. Our study is the first to evidence that enteric neurons are capable of secreting alpha-synuclein, thereby providing new insights into the role of the enteric nervous system in the pathophysiology of Parkinson disease. PMID: 23278133
    48. This study demonistrated that Deletion in exon 5 of the SNCA gene and exposure to rotenone leads to oligomerization of alpha-synuclein and toxicity to PC12 cells. PMID: 23128054
    49. Large alpha-Syn oligomers preferentially bind to the N-terminal domain of a vesicular SNARE protein, synaptobrevin-2, which blocks SNARE-mediated lipid mixing by preventing SNARE complex formation. PMID: 23431141
    50. Primary oligodendrocytes from rat brain and oligodendroglial cell lines take-up neuronal-secreted or exogenously added synuclein alpha from their conditioning medium. PMID: 23077527

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  • 亞細胞定位：
    Cytoplasm. Membrane. Nucleus. Cell junction, synapse. Secreted.
  • 蛋白家族：
    Synuclein family
  • 組織特異性：
    Found only in brain (hippocampus, brainstem and cortex). Specifically expressed in neuronal cell bodies and synapses.
  • 數(shù)據(jù)庫鏈接：

    KEGG: rno:29219

    UniGene: Rn.1827