目录号 | 产品详情 | 靶点 | |
---|---|---|---|
T5S0658 | Autophagy | ||
Corynoxine 是从大叶钩藤中分离出的一种四环羟吲哚生物碱。它是一种自噬增强剂,可通过Akt/mTOR 途径促进 α-突触核蛋白的清除。 | |||
TN1140 | AMPK mTOR Autophagy | ||
Onjisaponin B 是从远志中提取的一种天然产物,可通过 AMPK-mTOR 信号通路诱导自噬,提高 NGF 水平并加速突变型亨廷顿蛋白和 A53T α±-突触核蛋白的清除,可研究帕金森病和亨廷顿病。 | |||
T7441 | Endogenous Metabolite | ||
Cuminaldehyde (Cuminal) 是一种具有抑制 α-突触核蛋白纤颤和细胞毒性作用的天然醛,是一种 Cuminum cyminum 的主要成分。它显示抗癌特性。 | |||
T76861 | Others | ||
Cinpanemab (BIIB054) 是一种新型人源单克隆抗体,对 α-突触核蛋白 1-10 位残基具有亲和力。Cinpanemab 可用于研究帕金森及其相关疾病。 | |||
T5S2357 | Antifungal | ||
Acetylcorynoline (O-Acetylcorynoline) 是提取自 Corydalis bungeana 中的一种主要生物碱成分,具有抗炎活性。 | |||
T63321 | Proteasome | ||
20S Proteasome activator 1 是一种 20S 蛋白酶激活剂,对胰蛋白酶样位点、胰凝乳蛋白酶样位点和半胱天冬酶位点的 IC50 分别为 0.3 μM、0.7 μM 和 1.8 μM。20S Proteasome activator 1 通过在细胞系统中翻译来防止致病性 α-synuclein A53T 突变体积累从而减少疾病发生的概率。20S Proteasome activator 1 可用于研究神经退行性疾病。 | |||
T72962 | |||
Sycosterol A 是一种α-synuclein(α-syn)甾醇抑制剂。 | |||
T13049 | Others | ||
Synucleozid is a potent the SNCA mRNA inhibitor that encodes α-synuclein protein (IC50=1.5 μM), has the potential for the investigation of Parkinson’s disease. | |||
T83726 | |||
Tat-βsyn-degron是一种降低α-synuclein表达的肽。其结构包括HIV-1 Tat质膜跨导域、与β-synuclein氨基酸36-45相对应的α-synuclein结合域βsyn,以及蛋白酶体定向域degron。在肽-蛋白结合实验中,Tat-βsyn-degron能够与重组α-synuclein结合,并在大鼠初级皮质神经元培养中降低α-synuclein水平,这一效应可以通过蛋白酶体抑制剂MG132阻止。体内研究显示,Tat-βsyn-degron (40 mg/kg)能够在过表达人类A53T突变体α-synuclein的M38转基因小鼠的大脑中降低α-synuclein水平,并且在黑质和脑桥中降低磷酸化α-synuclein水平,以及在通过α-synuclein预成纤维诱导的扩散性α-synuclein病理模型小鼠中减少神经炎症。此外,Tat-βsyn-degron (6 µmol/kg, i.p.)在MPTP诱导的帕金森病小鼠模型中,保护多巴胺能神经元,缓解运动缺陷。 | |||
T76889 | |||
Prasinezumab (PRX 002) 为针对聚集α-突触核蛋白 (α-synuclein) 的人源化IgG1单克隆抗体,展现在帕金森病研究中的应用潜力。 |
目录号 | 产品名/同用名 | 种属 | 表达系统 | ||
---|---|---|---|---|---|
TMPY-02512 | Alpha-Synuclein Protein, Human, Recombinant | Human | E. coli | ||
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). Besides, alpha-synuclein is an abundant component of Lewy bodies in sporadic Parkinson's disease and diffuse Lewy body disease.
|
|||||
TMPY-06460 | Alpha-Synuclein Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
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). Besides, alpha-synuclein is an abundant component of Lewy bodies in sporadic Parkinson's disease and diffuse Lewy body disease.
|
|||||
TMPY-06318 | Alpha-Synuclein Protein,Human,Recombinant (H50Q) | Human | E. coli | ||
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). Besides, alpha-synuclein is an abundant component of Lewy bodies in sporadic Parkinson's disease and diffuse Lewy body disease.
|
|||||
TMPJ-00683 | SNCA Protein, Mouse, Recombinant | Mouse | E. coli | ||
Alpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).
|
|||||
TMPJ-00684 | SNCA Protein, Mouse, Recombinant (His) | Mouse | E. coli | ||
Alpha-synuclein (Snca) belongs to a family of proteins including a-, b-, and g-synucleins. Alpha-synuclein has been found to be implicated in the pathophysiology of many neurodegenerative diseases, including Parkinson's disease (PD) and Alzheimer's disease. Manyneurodegenerative diseases has shown that alpha-synuclein accumulates in dystrophic neurites and in Lewy bodies. The function of alpha-synuclein is closely correlated with its three-dimensional structure, especially for proteins important in the pathogenesis of neurodegenerative diseases. Alpha-synuclein is a dynamic molecule whose secondary structure depends on the environment. For example, it has an unfolded random coil structure in aqueous solution, forms a-helical structure upon binding to acidic phospholipid vesicles, and forms insoluble fibrils with a high b-sheet content that resemble the filaments found in Lewy bodies. Also, alpha-synuclein was known to associate with 14-3-3 proteins including protein kinase C, BAD, and extracellular regulated kinase, and overexpression of alpha-synuclein could contribute to cell death in neurodegenerative diseases.
|
|||||
TMPJ-00023 | SNCA Protein, Human, Recombinant (His) | Human | E. coli | ||
Alpha-Synuclein (SNCA) is a member of the Synuclein family. SNCA is expressed principally in brain but also expressed in low concentrations in all tissues except liver. SNCA interacts with UCHL1, Phospholipase D and histones. SNCA can include beta- and gamma-synuclein. In addition, SNCA is an important regulatory component of vesicular transport in neuronal cells. It has been suggested that SNCA is related to the pathogenesis of Parkinson's Disease and neurodegenerative disorders. Defects in SNCA will lead to Dementia Lewy Body (DLB).
|
|||||
TMPH-02419 | Alpha-synuclein Protein, Cynomolgus, Recombinant (His & SUMO) | Cynomolgus | E. coli | ||
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.
|
|||||
TMPH-03238 | Alpha-synuclein Protein, Rat, Recombinant (GST) | Rat | E. coli | ||
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.
|
|||||
TMPH-02418 | Alpha-synuclein Protein, Cynomolgus, Recombinant (His) | Cynomolgus | Yeast | ||
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.
|
|||||
TMPH-03098 | Alpha-synuclein Protein, Pig, Recombinant (His & Myc) | Sus scrofa (Pig) | E. coli | ||
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.
|