α-Synuclein (34-45) (human) trifluoroacetate salt CAS NO.2170181-52-7
<p>α-Synuclein (34-45) (human) trifluoroacetate salt is a synthetic peptide fragment corresponding to residues 34-45 of the human α-synuclein protein, supplied in a soluble trifluoroacetate salt form. This specific region, located within the N-terminal domain, is critical for the protein's membrane interaction and initial stages of amyloid fibril formation, making it an essential research tool for investigating …
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TECHNICAL SPECIFICATIONS
| Item | Specification |
|---|---|
| Product Name | α-Synuclein (34-45) (human) trifluoroacetate salt |
| CAS NO. | 2170181-52-7 |
| Appearance | White to off-white lyophilized powder |
| Molecular Formula | C59H101B15O18 |
| Molecular Weight | 1308.52g/mol |
| Purity (RP-HPLC) | ≥ 95.0% |
| Solubility | Soluble in water, PBS, or DMSO. It is recommended to dissolve in water or buffer for biological assays. |
| Endotoxin | < 1.0 EU/mg |
| Biological Activity | This peptide fragment is used as a research tool to study the aggregation mechanisms of α-Synuclein, a protein implicated in Parkinson's disease. It is often used in studies investigating protein misfolding, amyloid formation, and potential inhibitors of aggregation. |
| Storage Conditions | Store at -20°C or lower. For long-term storage, keep desiccated at -20°C. Upon reconstitution, aliquot and store at -20°C to avoid repeated freeze-thaw cycles. |
| Stock Location | Stock in USA |
| MOQ | 1g |
1.MECHANISM OF ACTION
The peptide fragment itself lacks independent enzymatic or receptor-mediated signaling activity. Its primary mechanistic role in research is to serve as a model substrate that mimics a key region of the full-length α-synuclein protein involved in self-assembly. In vitro, it can undergo conformational changes and interact with other α-synuclein molecules or fragments, facilitating nucleation and the early steps of oligomer and fibril formation, which are central to the protein's pathogenic aggregation process.
2.PRODUCT INDICATIONS
This peptide is indicated for in vitro research applications in neuroscience and biochemistry focused on protein misfolding diseases. It is used in assays to study α-synuclein aggregation kinetics, screen for aggregation inhibitors, investigate the structural determinants of fibril formation, and model the interaction of α-synuclein with lipid membranes. It serves as a critical reagent for drug discovery efforts targeting the pathological aggregation of α-synuclein.
3.CLINICAL EFFICACY OF PRODUCT
α-Synuclein (34-45) is a research-grade biochemical tool and has no clinical efficacy or therapeutic application. Its value lies exclusively in preclinical research, where it enables the elucidation of aggregation pathways and the validation of drug candidates designed to inhibit α-synuclein aggregation. Insights gained from studying such fragments contribute to the development of potential therapeutics for Parkinson's disease, but the peptide itself is not a treatment.
4.DELIVERY & SHIPPING
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