Recombinant Proteins

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PARK2 Human

Parkinson Disease Protein 2 Human Recombinant

PARK2 Human Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 485 amino acids (1-465) and having a molecular mass of 53.8 kDa. PARK2 is fused to a 20 amino acid His-tag at N-terminus.
Shipped with Ice Packs
Cat. No.
BT2693
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PARK7 Human

Parkinson Disease Protein 7 Human Recombinant

PARK7 Human Recombinant fused to an N-terminal 36 aa His-Tag, produced in E.Coli is a single, non-glycosylated polypeptide chain (aa 1-189) containing 225 amino acids and having a molecular mass of 24 kDa.
Shipped with Ice Packs
Cat. No.
BT2743
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.

PARK7 Mouse

Parkinson Disease Protein 7 Mouse Recombinant

PARK7 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 212 amino acids (1-189 a.a) and having a molecular mass of 22.4kDa.
PARK7 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2800
Source
Escherichia Coli.
Appearance
Sterile Filtered colorless solution.
Definition and Classification

Parkinson Disease Protein, primarily known as α-synuclein, is a small protein that plays a crucial role in the pathogenesis of Parkinson’s disease (PD). It is classified under the family of synuclein proteins, which also includes β-synuclein and γ-synuclein. The abnormal aggregation of α-synuclein in the brain is a hallmark of Parkinson’s disease and other related neurodegenerative disorders, collectively termed synucleinopathies .

Biological Properties

Key Biological Properties: α-synuclein is a soluble, intrinsically disordered protein that can adopt multiple conformations. It is predominantly expressed in the brain, particularly in the presynaptic terminals of neurons .

Expression Patterns: The expression of α-synuclein is highest in the brain, but it is also found in other tissues such as the heart, muscles, and pancreas .

Tissue Distribution: Within the brain, α-synuclein is abundantly present in regions such as the substantia nigra, hippocampus, neocortex, and cerebellum .

Biological Functions

Primary Biological Functions: α-synuclein is involved in the regulation of synaptic vesicle trafficking and neurotransmitter release. It plays a role in maintaining synaptic function and plasticity .

Role in Immune Responses and Pathogen Recognition: Emerging evidence suggests that α-synuclein may have a role in the immune response, particularly in modulating neuroinflammation. It can interact with microglia, the resident immune cells of the brain, influencing their activation and response to pathogens .

Modes of Action

Mechanisms with Other Molecules and Cells: α-synuclein interacts with various cellular components, including lipids, proteins, and nucleic acids. It can bind to synaptic vesicles and membranes, influencing their dynamics .

Binding Partners: Key binding partners of α-synuclein include synaptobrevin-2, phospholipids, and other synaptic proteins .

Downstream Signaling Cascades: The aggregation of α-synuclein can trigger a cascade of events leading to cellular dysfunction and death. This includes the activation of stress responses, mitochondrial dysfunction, and impairment of protein degradation pathways .

Regulatory Mechanisms

Transcriptional Regulation: The expression of α-synuclein is regulated at the transcriptional level by various factors, including transcription factors and epigenetic modifications .

Post-Translational Modifications: α-synuclein undergoes several post-translational modifications, such as phosphorylation, ubiquitination, and nitration. These modifications can influence its aggregation propensity and toxicity .

Applications

Biomedical Research: α-synuclein is a critical target in Parkinson’s disease research. Understanding its biology and pathology is essential for developing therapeutic strategies .

Diagnostic Tools: Biomarkers based on α-synuclein levels in cerebrospinal fluid and blood are being explored for early diagnosis of Parkinson’s disease .

Therapeutic Strategies: Therapeutic approaches targeting α-synuclein include small molecules, antibodies, and gene therapies aimed at reducing its aggregation or enhancing its clearance .

Role in the Life Cycle

Development to Aging and Disease: α-synuclein plays a role throughout the life cycle, from development to aging. During development, it is involved in synaptic formation and function. In aging and disease, its aggregation and accumulation contribute to neurodegeneration and the progression of Parkinson’s disease .

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