Recombinant Proteins

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LBP
CEA
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SNCA 61-140 Human

Alpha Synuclein 61-140 Human Recombinant

Recombinant Human A-Synuclein 61-140, produced in E. coli, is a truncated form of the alpha-synuclein protein, encompassing amino acids 61-140. This non-glycosylated polypeptide chain consists of 81 amino acids, resulting in a molecular weight of 8.4 kDa. However, its apparent size on SDS-PAGE may appear larger due to an additional methionine residue at the N-terminus. Purification of this recombinant protein is achieved through proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT9284
Source
Escherichia Coli.
Appearance
A clear, sterile solution without any color.

SNCA 96-140 Human

Alpha Synuclein 96-140 Human Recombinant

This product consists of the amino acids 96-140 of the human alpha-synuclein protein, produced in E. coli. It is a single, non-glycosylated polypeptide chain of 46 amino acids with a molecular weight of 5.2 kDa. An additional methionine residue is present at the N-terminus. Purification of this recombinant human alpha-synuclein 96-140 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9368
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SNCA A30P Human

Alpha Synuclein A30P Human Recombinant

Recombinant Human α-Synuclein A30P, a Parkinson's disease-associated point mutant, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 140 amino acids with a molecular weight of 14.4 kDa. Note that its apparent size on SDS-PAGE might be higher. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9430
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

SNCA E46K, Human

Alpha-Synuclein E46K Human Recombinant

Recombinant human SNCA E46K, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 140 amino acids (1-140a.a.). It has a molecular mass of 14.4 kDa. SNCA undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9751
Source
E.coli.
Appearance
A colorless solution that has been sterilized by filtration.

SNCA Human

Alpha Synuclein Human Recombinant

Recombinant Human a-Synuclein, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 140 amino acids. It has a molecular mass of 14.4 kDa. Note: The actual molecular weight observed on SDS-PAGE might be higher. The protein undergoes purification using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9839
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.
Definition and Classification

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 .

Biological Properties

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 .

Biological Functions

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 .

Modes of Action

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 .

Regulatory Mechanisms

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 .

Applications

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 .

Role in the Life Cycle

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 .

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