Recombinant Proteins
Product List
SNCA 1-60 Human
Alpha Synuclein 1-60 Human Recombinant
A-Synuclein 1-60 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 1-60 and contains the N-terminal amphipathic domain, produced in E.Coli is a single, non-glycosylated polypeptide chain of 60 amino acids having a molecular mass of 6.1kDa. The Recombinant Human a-Synuclein 1-60 is purified by proprietary chromatographic techniques.
SNCA 1-95, Human
Alpha-Synuclein 1-95 Human Recombinant
SNCA Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 95 amino acids (1-95 a.a.) and having a molecular mass of 9.3kDa.
SNCA is purified by proprietary chromatographic techniques.
SNCA 61-140 Human
Alpha Synuclein 61-140 Human Recombinant
A-Synuclein 61-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 61-140 , produced in E.Coli is a single, non-glycosylated polypeptide chain of 81 amino acids having a molecular mass of 8.4kDa (molecular size on SDS-PAGE will appear higher), with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 61-140 is purified by proprietary chromatographic techniques.
SNCA 96-140 Human
Alpha Synuclein 96-140 Human Recombinant
A-Synuclein 96-140 Human Recombinant which is a deletion mutant of the a-synuclein amino acids 96-140, produced in E.Coli is a single, non-glycosylated polypeptide chain of 46 amino acids having a molecular mass of 5.2kDa, with an additional Met attached at the N-terminus. The Recombinant Human a-Synuclein 96-140 is purified by proprietary chromatographic techniques.
SNCA A30P Human
Alpha Synuclein A30P Human Recombinant
A-Synuclein A30P Human Recombinant which is a Parkinson’s disease-related point mutant, produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (molecular size on SDS-PAGE will appear higher). The Recombinant Human a-Synuclein A30P is purified by proprietary chromatographic techniques.
SNCA A30P/A53T Human
Alpha Synuclein A30P/A53T Human Recombinant
SNCA A53T Human
Alpha Synuclein A53T Human Recombinant
SNCA Delta-NAC Human
Alpha Synuclein Delta-NAC Human Recombinant
A-Synuclein Delta-NAC Human Recombinant which is a deletion mutant of the a-synuclein that lacks the NAC region (amino acid 61-95), produced in E.Coli is a single, non-glycosylated polypeptide chain of 111 amino acids having a molecular mass of 11.9kDa (molecular size on SDS-PAGE will appear higher), with 6 amino acids added as a linker. The Recombinant Human a-Synuclein Delta-NAC is purified by proprietary chromatographic techniques.
SNCA E46K, Human
Alpha-Synuclein E46K Human Recombinant
SNCA E46K Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140a.a.) and having a molecular mass of 14.4kDa.
SNCA is purified by proprietary chromatographic techniques.
SNCA Human
Alpha Synuclein Human Recombinant
The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques.
Introduction
Synucleins are a family of soluble proteins predominantly found in vertebrates. They are primarily expressed in neural tissue and certain tumors. The family includes three members: alpha-synuclein, beta-synuclein, and gamma-synuclein. The name “synuclein” is derived from their initial discovery in the synapses and nuclei of neurons . Alpha-synuclein is the most studied member due to its association with neurodegenerative diseases such as Parkinson’s disease .
Key Biological Properties: Alpha-synuclein is a small protein composed of 140 amino acids. It is known for its ability to adopt various conformational states, which is crucial for its function and aggregation properties .
Expression Patterns: Alpha-synuclein is abundantly expressed in the brain, particularly in the neocortex, hippocampus, substantia nigra, thalamus, and cerebellum . It is also present in the peripheral nervous system, muscle, liver, heart, lungs, kidney, hematopoietic cells of the bone marrow, and circulating blood cells .
Tissue Distribution: While alpha-synuclein is most abundant in neural tissues, smaller amounts are found in the heart, muscle, and other tissues . Beta-synuclein is primarily located at presynaptic terminals in the central nervous system, and gamma-synuclein is mainly expressed in the peripheral nervous system, ocular, and adipose tissues .
Primary Biological Functions: Alpha-synuclein plays a critical role in regulating synaptic vesicle trafficking and neurotransmitter release . It is involved in neurotransmission, calcium homeostasis, mitochondrial function, and gene regulation .
Role in Immune Responses and Pathogen Recognition: Although the primary focus has been on its role in the nervous system, recent studies suggest that alpha-synuclein may also play a role in immune responses and pathogen recognition. However, more research is needed to fully understand these functions .
Mechanisms with Other Molecules and Cells: Alpha-synuclein interacts with phospholipids and proteins within presynaptic terminals. It binds to phospholipids of the plasma membrane via its N-terminus domain and to synaptobrevin-2 via its C-terminus domain, which is crucial during synaptic activity .
Binding Partners and Downstream Signaling Cascades: Alpha-synuclein functions as a molecular chaperone in the formation of SNARE complexes, which are essential for synaptic vesicle fusion and neurotransmitter release . It also interacts with other proteins and lipids, influencing various signaling pathways .
Transcriptional Regulation: The expression of alpha-synuclein is controlled by several mechanisms, including transcriptional regulation. It binds to DNA and histones, participating in epigenetic regulatory functions that control specific gene transcription .
Post-Translational Modifications: Alpha-synuclein undergoes various post-translational modifications, such as phosphorylation, ubiquitination, and acetylation, which regulate its function and aggregation properties .
Biomedical Research: Alpha-synuclein is extensively studied in the context of neurodegenerative diseases, particularly Parkinson’s disease. Understanding its role in these diseases can lead to the development of new therapeutic strategies .
Diagnostic Tools: Alpha-synuclein can serve as a biomarker for the early diagnosis of neurodegenerative diseases. Techniques such as real-time quaking-induced conversion (RT-QuIC) and protein misfolding cyclic amplification (PMCA) are used to detect pathological alpha-synuclein in peripheral tissues .
Therapeutic Strategies: Targeting alpha-synuclein aggregation and its interactions with other molecules is a promising approach for developing disease-modifying therapies for Parkinson’s disease and other synucleinopathies .
Development to Aging and Disease: Alpha-synuclein plays a role throughout the life cycle, from development to aging. During development, it is involved in synaptic formation and plasticity. In aging and disease, its aggregation into Lewy bodies is a hallmark of neurodegenerative diseases such as Parkinson’s disease and dementia with Lewy bodies .
