Product Name :
α-Synuclein (61-75) (TFA)
Description:
α-Synuclein (61-75) TFA is the 61-75 fragment of α-Synuclein. α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve terminals. α-Synuclein is a potential biomarker for Parkinson’s disease (PD).
CAS:
Molecular Weight:
Formula:
Chemical Name:
alpha-Synuclein (61-75) (TFA)
Smiles :
InChiKey:
InChi :
Purity:
≥98% (or refer to the Certificate of Analysis)
Shipping Condition:
Shipped under ambient temperature as non-hazardous chemical or refer to Certificate of Analysis
Storage Condition :
Dry, dark and -20 oC for 1 year or refer to the Certificate of Analysis.
Shelf Life:
≥12 months if stored properly.
Stock Solution Storage:
0 – 4 oC for 1 month or refer to the Certificate of Analysis.Phosphatidylserine Akt
Additional information:
α-Synuclein (61-75) TFA is the 61-75 fragment of α-Synuclein. α-Synuclein is an abundant neuronal protein that is highly enriched in presynaptic nerve terminals. α-Synuclein is a potential biomarker for Parkinson’s disease (PD).|Product information|Chemical Name: alpha-Synuclein (61-75) (TFA)|Technical Data|Appearance: Solid Power|Purity: ≥98% (or refer to the Certificate of Analysis)|Shipping Condition: Shipped under ambient temperature as non-hazardous chemical or refer to Certificate of Analysis|Storage Condition: Dry, dark and -20 oC for 1 year or refer to the Certificate of Analysis.|Shelf Life: ≥12 months if stored properly.|Stock Solution Storage: 0 – 4 oC for 1 month or refer to the Certificate of Analysis.|Drug Formulation: To be determined|HS Tariff Code: 382200|How to use|In Vitro:|Lewy bodies containing α-synuclein are a neuropathological hallmark of PD, and missense mutations in α-Synuclein (A30P, E46K, H50Q, G51D, A53E, A53T), as well as α-Synuclein gene duplications and triplications, appear to cause PD.Soticlestat web Moreover, polymorphisms in regulatory elements of the α-Synuclein gene predispose individuals to PD and are linked to an early onset of the disease.PMID:32156637 The non-Aβ-amyloid component (NAC) region of α-synuclein is relatively hydrophobic and aggregation-prone in human α-Synuclein but not in mouse α-Synuclein nor in the corresponding homologous region of human β-synuclein. Yet, β-synuclein is more homologous to α-Synuclein in the N-terminal sequences (74%) than γ-synuclein (67%).|Products are for research use only. Not for human use.|