SNCA Human

Alpha Synuclein Human Recombinant
Cat. No.
BT9839
Source
Escherichia Coli.
Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Appearance
Sterile filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
Prospec's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
Shipped with Ice Packs
In Stock

Description

a-Synuclein Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain of 140 amino acids having a molecular mass of 14.4kDa (Real molecular weight on SDS-PAGE will be shift up). 
The Recombinant Human a-Synuclein is purified by proprietary chromatographic techniques.

Product Specs

Introduction
Alpha-synuclein (a-synuclein), a 140-amino acid neuronal protein, plays a role in Parkinson's disease and related neurodegenerative disorders. This protein exhibits heat resistance, an extended unfolded structure with random coils, and potential involvement in vesicular transport regulation. Studies indicate its chaperone activity, which is influenced by the C-terminal acidic tail (amino acids 96-140).
Description
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.
Physical Appearance
Clear, colorless solution that has been sterilized by filtration.
Formulation
The protein solution (1 mg/ml) is supplied in a buffer containing 20 mM Tris-HCl (pH 7.5), 0.1 M NaCl, and 1 mM MgCl2.
Stability
For short-term storage (up to 2-4 weeks), the product can be stored at 4°C. For extended storage, it is recommended to freeze the protein at -20°C. Adding a carrier protein such as HSA or BSA (0.1%) can further enhance stability during long-term storage. Avoid repeated freezing and thawing.
Purity
The purity is determined to be greater than 95.0% using SDS-PAGE analysis.
Synonyms
Alpha-synuclein, Non-A beta component of AD amyloid, Non-A4 component of amyloid precursor, NACP, PD1, PARK1, PARK4, MGC110988, a-Synuclein, SNCA.
Source
Escherichia Coli.
Amino Acid Sequence

MDVFMKGLSK AKEGVVAAAE KTKQGVAEAA GKTKEGVLYV GSKTKEGVVH GVATVAEKTK EQVTNVGGAV VTGVTAVAQK TVEGAGSIAA ATGFVKKDQL GKNEEGAPQE GILEDMPVDP DNEAYEMPSE EGYQDYEPEA.

Product Science Overview

Structural Characteristics

Alpha-synuclein exists in at least two structural isoforms:

  1. Helix-rich, membrane-bound form: Both the N- and C-terminal regions of alpha-synuclein are tightly associated with membranes.
  2. Disordered, cytosolic form: This form is found in the cytosol and lacks a defined structure .
Biological Functions

Alpha-synuclein is involved in several critical biological processes:

  • Synaptic Function: It plays a role in the regulation of synaptic vesicle trafficking and neurotransmitter release.
  • Mitochondrial Function: It is highly expressed in the mitochondria of various brain regions, including the olfactory bulb, hippocampus, striatum, and thalamus .
Pathological Implications

Alpha-synuclein is a major component of Lewy bodies, which are pathological hallmarks of several neurodegenerative diseases, collectively known as synucleinopathies. These include:

  • Parkinson’s Disease (PD): Characterized by the accumulation of alpha-synuclein aggregates in the brain.
  • Dementia with Lewy Bodies (DLB): Involves the presence of Lewy bodies in the cortex.
  • Multiple System Atrophy (MSA): Features widespread alpha-synuclein pathology .
Recombinant Alpha Synuclein

Recombinant human alpha-synuclein is produced using DNA sequences encoding the mature form of the protein. This recombinant protein is often used in research to study its structure, function, and role in disease. It is typically expressed in E. coli and purified for experimental use .

Research and Clinical Relevance

Alpha-synuclein’s role in neurodegenerative diseases makes it a significant target for research. Understanding its interactions with other proteins, such as amyloid-beta (Aβ) and tau, is crucial for developing therapeutic strategies for diseases like Alzheimer’s and Parkinson’s .

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