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alpha synuclein r peptide synuclein

Published October Oct 17, 2026 9:21 PM

In the specialized field of neurodegenerative research, the study of alpha-synuclein has become a cornerstone for understanding the molecular mechanisms underlying various neuropathies. As a Human Alpha-Synuclein (Wild Type) 1 mg – recombinant protein for Parkinson's disease and amyloid research, supplied in high purity for laboratory use. resea by TT Ali · 2025 · Cited by 3 — Both peptides reduce αSyn fibril and oligomer formation in vitro and significantly suppress αSyn aggregation and cytotoxicity in yeast and human H4 cells. rcher frequently sourcing high- Alpha-Synuclein (α-Synuclein) is a presynaptic protein found to be a major component of Parkinson's Disease (PD) aggregates. quality reagents, I have found that navigating the nuances of alpha synuclein r peptide and related This protein cycles between a free, partially unfolded form and a helical, membrane-bound form. alpha -Synuclein can aggregate in vivo and in vitro. recombinant materials is essential for consistent experimental outcomes.

Defining the Protein and Its Biological Significance

Alpha-Synuclein (α-Synuclein) is a presynaptic protein found to be a major component of Parkinson's Disease (PD) aggregates. It is encoded by the SNCA gene, located on chromosome 4p21, and is Apr 12, 2021 — Recent work by Jin and colleagues explored the use of a Tat-βsyn-degron peptide to bind alpha-synuclein and induce its proteasomal degradation specifically. processed as a 140 amino acid (aa) protein with a theoretical molecular weight of approximately 14 kD.

Under normal physiological conditions, alpha-synuclein is a soluble protein that plays several roles in synaptic activity, such as the regulation of synaptic vesicle trafficking and subsequent neurotransmitter release. However, its tendency to cycle between a free, partially unfolded form and a helical, membrane-bound form makes it a focal point in amyloid research. When misfolded, it aggregates to form filamentous inclusions, specifically Lewy bodies and Lewy neurites, which are a major component of Lewy bodies in the affected neurons in Parkinson's disease.

Reagents and Experimental Models

For those looking to order Human Alpha Synuclein Monomers (SPR-316) or similar variants, quality control is paramount. rPeptide offers a large selection of Beta Amyloids, Taus, Synucleins, Calmodulins, Custom Products, and more, which are widely utilized in in vitro and in vivo models.

When conducting research, one must distinguish between different forms of the protein:

* Monomers: Recombinant human Alpha-Synuclein protein monomer (1 to 140 aa) is typically expressed in *Escherichia coli* and provided with >95% purity.

* Preformed Fibrils: The preformed fibrils of α-synuclein serve as a critical model for the pathogenic form of α-synuclein in numerous neuropathies, allowing researchers to simulate aggregation pathways in a controlled environment.

* Truncated Variants: Specialized research often requires fragments such as Alpha-Synuclein, 61-140, or Alpha-Synuclein, 1-60, to isolate specific binding domains.

Peptide-Based Approaches and Therapeutic Potential

The current efforts made in the development of peptides and their mimetics are among the most exciting frontiers in this domain. Scientists are investigating how a specific peptide can be designed to inhibit the formation of alpha-synuclein aggregates.

For instance, the Tat-βsyn-degron peptide has been documented as a successful tool for inducing the proteasomal degradation of the protein. By utilizing a targeting peptide-ba Alpha-Synuclein (Wild Type) (1.0 mg) Human, Recombinant sed system, researchers have demonstrated the specific knockdown of α-synuclein, effectively reducing its levels in cell cultures and animal models. Furthermo Apr 12, 2021 — Recent work by Jin and colleagues explored the use of a Tat-βsyn-degron peptide to bind alpha-synuclein and induce its proteasomal degradation specifically. re, novel biomimetic peptides are being chemically conjugated to target these aggregates directly, representing a promising strategy for modulating the protein's pathological behavior.

Conclusion: Best Practices for Selection

When selecting a recombinant protein for Parkinson's disease and amyloid research, it is vital to source materials from reputable providers like rPeptide to ensure the integrity of your study. Whether you are working with wild-type human alpha synuclein or specialized fragments, understanding the structural dynamics of this alpha-synuclein (α-synuclein) molecule is the first step toward reproducible results. As the scientific community continues to refine these peptide-based approaches, the precision of our experimental models will undoubtedly improve, leading to a deeper understanding of these complex biological processes.

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