Alexa Fluor™ 488-Labeled Human Alpha-synuclein Protein, Tag Free

AIDD‑Ready
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ALN-HA113-200ug
$840.00
In Stock - Delivery in 2-3 business days
ALN-HA113-1mg
$3,150.00
In Stock - Delivery in 2-3 business days
ALN-HA113
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Synonyms

NACP, PARK1, PARK4, PD1

Source

Alexa Fluor 488-Labeled Human Alpha-synuclein Protein, Tag Free (ALN-HA113) is expressed from E. coli cells. It contains AA Met 1 - Ala 140 (Accession # P37840-1). It is the Alexa Fluor™ 488 labeled form of Human Alpha-Synuclein, Tag Free (Cat. No. ALN-H5214).

Predicted N-terminus: Met 1

Molecular Characterization

This protein carries no "tag".

The protein has a calculated MW of 14.5 kDa. The protein migrates as 15-17 kDa when calibrated against Star Ribbon Pre-stained Protein Marker under reducing (R) condition (SDS-PAGE).

Conjugate

AF488

Excitation Wavelength: 488 nm

Emission Wavelength: 517 nm

Labeling

The primary amines in the side chains of lysine residues and the N-terminus of the protein are conjugated with AF488 using standard chemical labeling method. The residual AF488 is removed by molecular sieve treatment during purification process.

Purity

>90% as determined by SDS-PAGE.

Formulation

Supplied as 0.2 μm filtered solution in PBS, pH7.4, 0.03% Proclin300 with trehalose as protectant.

Contact us for customized product form or formulation.

Shipping and Storage

This product is supplied and shipped on dry ice.

Please protect from light and avoid repeated freeze-thaw cycles.

This product is stable after storage at:
  • The product MUST be stored at -70°C or lower upon receipt;
  • -70°C for 3 months under sterile conditions.

バックグランド

Alpha-synuclein is a neuronal protein that plays several roles in synaptic activity such as regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. It 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. Abnormalities in alpha-synuclein are implicated in the pathogenesis of Parkinson's disease (PD). Alpha-synuclein is present in Lewy-bodies, the neuropathological hallmark of PD, and the protein and its aggregation have been widely linked to neurotoxic pathways that ultimately lead to neurodegeneration.