Recombinant Proteins

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LBP
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SNCA 1-60 Human

Alpha Synuclein 1-60 Human Recombinant

Recombinant Human a-Synuclein 1-60, a truncated variant encompassing amino acids 1-60 and containing the N-terminal amphipathic domain, is produced in E. coli. This non-glycosylated polypeptide chain consists of 60 amino acids, resulting in a molecular weight of 6.1 kDa. The purification process involves proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9121
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SNCA Mouse

Alpha-Synuclein Mouse Recombinant

Recombinant Mouse SNCA, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 1-140. With a molecular weight of 14.4 kDa, this protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9909
Source
Escherichia Coli.
Appearance
A clear, colorless solution, sterile-filtered.

SNCA NACP112 Human

Alpha Synuclein NACP112 Human Recombinant

Recombinant Human a-Synuclein NACP112, an alternatively spliced (103-129) variant of a-Synuclein, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 112 amino acids, with a molecular weight of 11.3 kDa. It is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10015
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SNCB Human

Beta-Synuclein Human Recombinant

Recombinant Human beta-Synuclein, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 1-134. It has a molecular mass of 14.2 kDa. Note that its apparent size on SDS-PAGE may be slightly larger.
Shipped with Ice Packs
Cat. No.
BT10091
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SNCG Human

Gamma-Synuclein Human Recombinant

Recombinant human gamma-synuclein, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 127 amino acids with a molecular weight of 13.3 kDa. The protein's coding region was amplified via RT-PCR and cloned into an E. coli expression vector. Overexpression in E. coli was followed by purification using the protein's thermosolubility and standard column chromatography techniques, achieving apparent homogeneity.
Shipped with Ice Packs
Cat. No.
BT10165
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

SNCG Mouse

Gamma-Synuclein Mouse Recombinant

Recombinant SNCG protein produced in E. coli is a single, non-glycosylated polypeptide chain consisting of 146 amino acids (1-123 a.a.) with a molecular weight of 15.5 kDa. The protein includes a 23 amino acid His-tag fused at the N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT10230
Source
Escherichia Coli.
Appearance
A colorless solution that has been sterilized by filtration.

SNCA A30P/A53T Human

Alpha Synuclein A30P/A53T Human Recombinant

This product consists of a recombinant human A-Synuclein protein featuring the A30P/A53T double mutation associated with Parkinson's disease. Produced in E. coli, it exists as a single, non-glycosylated polypeptide chain composed of 140 amino acids, with a molecular weight of 14.5 kDa. Please note that its size on SDS-PAGE may appear larger. The purification of Recombinant Human a-Synuclein A30P/A53T is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9522
Source
Escherichia Coli.
Appearance
A clear, sterile-filtered solution.

SNCA A53T Human

Alpha Synuclein A53T Human Recombinant

Recombinant Human Alpha-Synuclein A53T, a Parkinson's disease-associated point mutant, is produced in E. coli. It is a single, non-glycosylated polypeptide chain composed of 140 amino acids, with a molecular weight of 14.4 kDa (note: it may appear larger on SDS-PAGE). The purification of Recombinant Human Alpha-Synuclein A53T is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9568
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

SNCA Delta-NAC Human

Alpha Synuclein Delta-NAC Human Recombinant

This product consists of a recombinant human alpha-synuclein protein with a deletion in the NAC region (amino acids 61-95), expressed in E. coli. It is a single, non-glycosylated polypeptide chain composed of 111 amino acids, resulting in a molecular weight of 11.9 kDa. A 6-amino acid linker is incorporated into the protein sequence. Despite its calculated molecular weight, the protein exhibits a higher apparent molecular size on SDS-PAGE. Purification of the recombinant human alpha-synuclein delta-NAC protein is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT9653
Source
Escherichia Coli.
Appearance
Clear, colorless solution that has been sterilized by filtration.

SNCA 1-95, Human

Alpha-Synuclein 1-95 Human Recombinant

Recombinant human SNCA, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 95 amino acids (1-95 a.a.). It has a molecular mass of 9.3kDa and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9195
Source
E.coli.
Appearance
Sterile Filtered colorless solution.
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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