Recombinant human Alpha-Synuclein protein monomer
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Recombinant human Alpha-Synuclein protein monomer is a Human Full Length protein, in the 1 to 140 aa range, expressed in Escherichia coli, with >95%, < 0.1 EU/µg endotoxin level, suitable for SDS-PAGE, Mass Spec, HPLC.
View Alternative Names
NACP, PARK1, SNCA, Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant human Alpha-Synuclein protein monomer (AB254310)
SDS-PAGE analysis of ab254310.
- HPLC
Supplier Data
HPLC - Recombinant human Alpha-Synuclein protein monomer (AB254310)
Purity >95%.
The spectrum was recorded using a 1260 Infinity II HPLC system with DAD and a MabPac RP column (3.0x100 mm, 4 μm). 5 μL of purified protein was injected and the gradient run from 80 % water : TFA (99.9 : 0.1 v/v) and 20 % acetonitrile : water : TFA (90 : 9.9 : 0.1 v/v/v) to 20 % water : TFA (99.9 : 0.1 v/v) and 80 % acetonitrile : water : TFA (90 : 9.9 : 0.1 v/v/v) within 3 minutes followed by an isocratic step for another 3 min. Flow rate was 0.5 mL/min and the column compartment temperature was 50 °C.
Reactivity data
Product details
Alpha-Synuclein is expressed predominantly in the brain, where it is concentrated in presynaptic nerve terminals. The deposition of the abundant presynaptic brain protein alpha-synuclein as fibrillary aggregates in neurons or glial cells is a hallmark lesion in a subset of neurodegenerative disorders. These disorders include Parkinson's disease (PD), dementia with Lewy bodies (DLB) and multiple system atrophy, collectively referred to as synucleinopathies. Parkinson's disease (PD) is a common neurodegenerative disorder characterized by the progressive accumulation in selected neurons of protein inclusions containing alpha-synuclein and ubiquitin.
Collaborations
This antibody was developed with support from The Michael J. Fox Foundation.
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
The alpha-synuclein protein plays critical roles in neuronal activity. It contributes to neurotransmitter release regulation by acting in the formation and plasticity of the presynaptic neuronal network. Alpha-synuclein doesn't usually form parts of large protein complexes but it may associate transiently with membranes and vesicular structures. The protein's monomer form has also been observed in alpha lines and related neuronal processes operating alongside various cellular functions.
Pathways
Synaptic vesicle trafficking and dopamine neurotransmitter release are significant areas involving the alpha-synuclein protein. In these pathways alpha-synuclein interacts with other proteins like synaptophysin and protein monomer monomerizations are intrinsic to these processes. Altered function or aggregation of alpha-synuclein disrupts these pathways influencing broader neurological functions.
Specifications
Form
Lyophilized
Additional notes
Purity >95% by LC/MS.
General info
Function
The protein expressed by the SNCA gene is involved in various synaptic activities, including the regulation of synaptic vesicle trafficking and neurotransmitter release. As a monomer, it enhances synaptic vesicle exocytosis through vesicle priming, fusion, and dilation of exocytotic fusion pores. Mechanistically, it increases local Ca(2+) release, which is crucial for ATP-induced exocytosis. In its multimeric membrane-bound form, SNCA acts as a molecular chaperone, assisting in the folding of synaptic fusion components known as SNAREs at the presynaptic plasma membrane, in conjunction with cysteine string protein-alpha/DNAJC5, a function that is vital for maintaining normal SNARE-complex assembly during aging. Additionally, SNCA plays a role in dopamine neurotransmission regulation by associating with the dopamine transporter (DAT1) and modulating its activity. This supplementary information is collated from multiple sources and compiled automatically.
Sequence similarities
Belongs to the synuclein family.
Post-translational modifications
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.. Hallmark 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.. Acetylation at Met-1 seems to be important for proper folding and native oligomeric structure.
Target data
Product promise
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