Recombinant Alpha Synuclein

Recombinant Alpha Synuclein

Recombinant human alpha is perfect for use as a control substrate with in vitro conjugation. The reaction conditions should undergo optimization by specific applications. Most researchers recommend an initial concentration of the recombinant a-synuclein concentrate. The recombinant proteins provide breakthroughs in biomedical technology. The first observation of that case was in 1982 when the protein was contributive for the formation of recombinant human insulin.

The industry of this particular protein has undergone extreme growth since the first scientific observation. The US FDA currently has approvals for the usage of more than 130 proteins in the creation of a medicine. The total number of proteins used in the medicinal world is at 170 in a count worldwide. Stress Marq stocks some of the most widely used variations. The main applications of recombinant protein are in the following conditions:

  • Growth factors
  • Interleukins
  • Interferons
  • Tumor necrosis factors
  • Thrombolytic drugs
  • Diabetes
  • Dwarfism
  • Congestive heart failure
  • Multiple sclerosis
  • Anemia
  • Cerebral apoplexy
  • Neutropenia
  • Hepatitis
  • Asthma
  • Crohn’s disease
  • Cancer cases
  • Myocardial infarction

The function of recombinant proteins

  • They help in the regulation of releases of dopamine and its transportation.
  • It induces the fibrillation of protein tau
  • It reduces the responsiveness of apoptotic stimuli, which decreases the activation of caspase-3

The specificity of tissue

This aspect gains expression in the low concentration of all tissues except the liver. There is an intense concentration at the nerve terminals 

The making of recombinant alpha-synuclein

The process involves isolation of the relevant gene and cloning it into an expression vector. The most available recombinant proteins in therapeutic applications are from the human form. The most common expression is in yeast, animal cells, and bacteria. 

Most human genes have a complex structure. They have large introns and will require conversion to create the intron-free versions. The process involves converting mRNA into cDNA. The level of the equivalent t-RNA will depend on an organism’s biological structure. An organism with rare codons will have different amino acid arrays.

The expression vectors should have conditions that make up for the lacking regulatory regions. The necessary conditions are terminator sequences, ribosome-binding sites, and promoters. 

It is possible to alter the gene of a recombinant protein to create a more stable variation. Complete stabilization will, however, require removal of the PEST sequence and co-expression of the molecular chaperone.

Rapid production of the recombinant protein will aggregate the inclusion bodies. It is vital to use regulated expression vectors to control the production rate of the recombinant alpha-synuclein. Consider isolating the protein before forming a purification process that will work on the exported proteins.

Modification of recombinant proteins

Many of these proteins require some form of adjustment, such as glycosylation. This process is available in eukaryotic cells and may sometimes precede the application of insect cells, yeast, and mammalian culture systems. 


This process takes place on serine residues by CK1 that occurs on waste, which is distinct from residue that undergoes phosphorylation by specific kinases. The process is selective and extensive in specific lesions. Acetylation by Met-1 is perfect for the correct folding and formation of the native oligomeric system.


Recombinant Alpha Synuclein
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