Recombinant Proteins

p53
LBP
CEA
HLA
TCL
TTC
NPM
MAF
Bax
BID

SNCA Mouse

Alpha-Synuclein Mouse Recombinant

SNCA Recombinant Mouse produced in E.Coli is a single, non-glycosylated polypeptide chain containing 140 amino acids (1-140 a.a.) and having a molecular mass of 14.4 kDa. The SNCA is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT9909
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SNCA NACP112 Human

Alpha Synuclein NACP112 Human Recombinant

A-Synuclein NACP112 Human Recombinant which is an alternatively spliced (103-129) form of a-Synuclein, produced in E.Coli is a single, non-glycosylated polypeptide chain of 112 amino acids having a molecular mass of 11.3kDa. The Recombinant Human a-Synuclein NACP112 is purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10015
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SNCB Human

Beta-Synuclein Human Recombinant

Recombinant Human b-Synuclein produced in E.Coli is a single, non-glycosylated polypeptide chain (1-134 a.a) having a molecular mass of 14.2kDa (molecular size on SDS-PAGE will appear higher).
Shipped with Ice Packs
Cat. No.
BT10091
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SNCG Human

Gamma-Synuclein Human Recombinant

g-Synuclein Human Recombinant produced in E.Coli is a single,non-glycosylated polypeptide chain containing 127 amino acids and having a molecular mass of 13,300 Dalton.
The protein coding region of g-synuclein was amplified by RT-PCR and cloned into an E.coli expression vector. g-synuclein was overexpressed in E. coli and purified to apparent homogeneity by taking advantage of the thermosolubility of the protein and by using conventional column chromatography techniques.
Shipped with Ice Packs
Cat. No.
BT10165
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

SNCG Mouse

Gamma-Synuclein Mouse Recombinant

SNCG Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 146 amino acids (1-123 a.a) and having a molecular mass of 15.5kDa.
SNCG is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT10230
Source
Escherichia 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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