抗体

抗alpha突触核蛋白

MBS500025

0.1毫升

235美元

单克隆

小鼠

未共轭

3H9

人类, 小鼠, 大鼠

免疫印迹, 免疫细胞化学

抗体

抗alpha突触核蛋白

alpha突触核蛋白

alpha-synuclein isoform NACP140; Alpha-synuclein; alpha-synuclein; synuclein alpha-140; non A-beta component of AD amyloid; synuclein, alpha (non A4 component of amyloid precursor); Non-A beta component of AD amyloid; Non-A4 component of amyloid precursor

SNCA

SNCA;SNCA;PD1;NACP;PARK1;PARK4;NACP;PARK1;NACP

SYUA_HUMAN

单克隆

IgG1

3H9

小鼠

人类, 小鼠, 大鼠

140

Specific for the ~15kDa alpha Synuclein protein.

Ascites fluid (Mouse ascites fluid.)

100微升液体。 含10 mM叠氮化钠

Store at -20 degree C in undiluted aliquots; stable for at least one year. Avoid freeze/thaw cycles.

免疫印迹(免疫印迹), 免疫荧光(IF)

Quality Control: Western blots performed on each lot. WB: 1:1,000. IF: 1:500

Antigen: Full length human alpha synuclein expressed in E. Coli. Immunogen Information: Full length human alpha synuclein expressed in E. Coli. Immunogen Species: Human

Reactivity Assumed Based on 100% Sequence Homology: Most mammals. Species Reactivity Note: The antibody has been directly tested for reactivity in human and rodent. It is expected that it will work on other mammal tissues. Biological Significance: Alpha-synuclein is a presynaptic neuronal protein that is thought to be involved in the formation of SNARE complexes. Most significantly, aggregated alpha-synuclein is one of the major components found in the Lewy bodies that occur in Parkinson's disease (PD) and other neurodegenerative disorders (Okochi et al., 2000). Early onset Parkinson's disease may be caused by a duplication or triplication of one of the alpha synuclein genes (Chartier-Harlin MC et al., 2004 and Singleton, AB et al., 2005). Alpha-synuclein is also found in the Lewy bodies of patients with diffuse Lewy body disease and inclusions in glial cells in the brains of patients with multiple system atrophy (MSA) and amyotrophic lateral sclerosis (ALS).

小鼠单克隆抗体

Okochi M, Walter J, Koyama A, Nakajo S, Baba M, Iwatsubo T, Meijer L, Kahle PJ, Haass C (2000) Constitutive phosphorylation of the Parkinson's disease associated alpha-synuclein. J Biol Chem Jan 7;275(1): 390-7. Chartier-Harlin, MC. et al. Alpha-synuclein locus duplication as a cause of familial Parkinson's disease. Lancet 364: 1167-1169 (2004). Singleton, AB et al. Alpha-synuclein locus triplication causes Parkinson's disease. Science 302: 841 (2003).

4507109

NP_000336.1

NM_000345.3

P37840

15

Alpha-synuclein Signaling Pathway 137913!!Alzheimer's Disease Pathway 83097!!Alzheimer's Disease Pathway 509!!Alzheimers Disease Pathway 672448!!Amyloids Pathway 366238!!Disease Pathway 530764!!EGFR1 Signaling Pathway 198782!!Parkin-Ubiquitin Proteasomal System Pathway 700638!!Parkinson's Disease Pathway 83098!!Parkinsons Disease Pathway 705377

Alpha-synuclein is a member of the synuclein family, which also includes beta- and gamma-synuclein. Synucleins are abundantly expressed in the brain and alpha- and beta-synuclein inhibit phospholipase D2 selectively. SNCA may serve to integrate presynaptic signaling and membrane trafficking. Defects in SNCA have been implicated in the pathogenesis of Parkinson disease. SNCA peptides are a major component of amyloid plaques in the brains of patients with Alzheimer's disease. Four alternatively spliced transcripts encoding two different isoforms have been identified for this gene. [provided by RefSeq, Mar 2009]

Function: May be involved in the regulation of dopamine release and transport. Induces fibrillization of microtubule-associated protein tau. Reduces neuronal responsiveness to various apoptotic stimuli, leading to a decreased caspase-3 activation. Subunit structure: Soluble monomer which can form filamentous aggregates. Interacts with UCHL1 . By similarity. Interacts with phospholipase D and histones. Ref.16 Ref.18. Subcellular location: Cytoplasm. Membrane. Nucleus. Cell junction synapse. Note: Membrane-bound in dopaminergic neurons. Ref.18 Ref.22. Tissue specificity: Expressed principally in brain but is also expressed in low concentrations in all tissues examined except in liver. Concentrated in presynaptic nerve terminals. Domain: The 'non A-beta component of Alzheimer disease amyloid plaque' domain (NAC domain) is involved in fibrils formation. The middle hydrophobic region forms the core of the filaments. The C-terminus may regulate aggregation and determine the diameter of the filaments. Ref.23. Post-translational modification: Phosphorylated, predominantly on serine residues. Phosphorylation by CK1 appears to occur on residues distinct from the residue phosphorylated by other kinases. Phosphorylation of Ser-129 is selective and extensive in synucleinopathy lesions. In vitro, phosphorylation at Ser-129 promoted insoluble fibril formation. Phosphorylated on Tyr-125 by a PTK2B-dependent pathway upon osmotic stress. Ref.13 Ref.14 Ref.15 Ref.17 Ref.21Hallmark lesions of neurodegenerative synucleinopathies contain alpha-synuclein that is modified by nitration of tyrosine residues and possibly by dityrosine cross-linking to generated stable oligomers.Ubiquitinated. The predominant conjugate is the diubiquitinated form . By similarity.Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure. Ref.26. Involvement in disease: Genetic alterations of SNCA resulting in aberrant polymerization into fibrils, are associated with several neurodegenerative diseases (synucleinopathies). SNCA fibrillar aggregates represent the major non A-beta component of Alzheimer disease amyloid plaque, and a major component of Lewy body inclusions. They are also found within Lewy body (LB)-like intraneuronal inclusions, glial inclusions and axonal spheroids in neurodegeneration with brain iron accumulation type 1.Parkinson disease 1 (PARK1) [MIM:168601]: A complex neurodegenerative disorder characterized by bradykinesia, resting tremor, muscular rigidity and postural instability. Additional features are characteristic postural abnormalities, dysautonomia, dystonic cramps, and dementia. The pathology of Parkinson disease involves the loss of dopaminergic neurons in the substantia nigra and the presence of Lewy bodies (intraneuronal accumulations of aggregated proteins), in surviving neurons in various areas of the brain. The disease is progressive and usually manifests after the age of 50 years, although early-onset cases (before 50 years) are known. The majority of the cases are sporadic suggesting a multifactorial etiology based on environmental and genetic factors. However, some patients present with a positive family history for the disease. Familial forms of the disease usually begin at earlier ages and are associated with atypical clinical features.Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.28 Ref.29 Ref.30 Ref.32 Ref.33Parkinson disease 4 (PARK4) [MIM:605543]: A complex neurodegenerative disorder with manifestations ranging from typical Parkinson disease to dementia with Lewy bodies. Clinical features include parkinsonian symptoms (resting tremor, rigidity, postural instability and bradykinesia), dementia, diffuse Lewy body pathology, autonomic dysfunction, hallucinations and paranoia.Note: The disease is caused by mutations affecting the gene represented in this entry.Dementia Lewy body (DLB) [MIM:127750]: A neurodegenerative disorder characterized by mental impairment leading to dementia, parkinsonism, fluctuating cognitive function, visual hallucinations, falls, syncopal episodes, and sensitivity to neuroleptic medication. Brainstem or cortical intraneuronal accumulations of aggregated proteins (Lewy bodies) are the only essential pathologic features. Patients may also have hippocampal and neocortical senile plaques, sometimes in sufficient number to fulfill the diagnostic criteria for Alzheimer disease.Note: The disease is caused by mutations affecting the gene represented in this entry. Sequence similarities: Belongs to the synuclein family.

0.1毫升

235美元