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SNCA Protein, Mouse, Recombinant (His)

Catalog No. TMPJ-00684
Synonyms: Snca, Non-A β component of AD amyloid, Non-A4 component of amyloid precursor, α-synuclein, Alpha-synuclein, Non-A beta component of AD amyloid, NACP

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.

All products from TargetMol are for Research Use Only. Not for Human or Veterinary or Therapeutic Use.
SNCA Protein, Mouse, Recombinant (His)
Pack Size Availability Price/USD Quantity
10 μg 5 days $ 184.00
50 μg 5 days $ 545.00
500 μg 5 days $ 1,900.00
1 mg 5 days $ 2,730.00
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Biological Description
Technical Params
Product Properties
Description 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.
Species Mouse
Expression System E. coli
Tag N-6His
Accession Number O55042
Synonyms Snca, Non-A β component of AD amyloid, Non-A4 component of amyloid precursor, α-synuclein, Alpha-synuclein, Non-A beta component of AD amyloid, NACP
Amino Acid Met1-Ala140
Construction Recombinant Mouse Alpha-Synuclein is produced by our E.coli expression system and the target gene encoding Met1-Ala140 is expressed with a 6His tag at the N-terminus.
Protein Purity Greater than 95% as determined by reducing SDS-PAGE. (QC verified)
Molecular Weight 18 KDa, reducing conditions
Endotoxin Less than 0.1 ng/µg (1 EU/µg) as determined by LAL test.
Formulation Lyophilized from a 0.2 μm filtered solution of 20mM PB, 150mM NaCl, pH 7.4.
Reconstitution Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. 
Stability & Storage

Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months.
Shipping

The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature listed below.
Research Background 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.

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Keywords

SNCA Protein, Mouse, Recombinant (His) Non-A b component of AD amyloid Snca Non-A β component of AD amyloid Non-A4 component of amyloid precursor α-synuclein Alpha-synuclein Non-A beta component of AD amyloid NACP a-synuclein recombinant recombinant-proteins proteins protein

 

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