
Cell-free expression systems allow for the in-vitro synthesis of a protein using only the cellular machinery required for transcription and translation, enabling quick manufacture of small amounts of functional proteins without the need for transfection and cell culture. Traditional cell-free expression methods use crude cell extracts derived from rabbit reticulocytes, wheat germ, or Escherichia coli to drive protein translation. Other approaches use coupled translation and transcriptions systems using reconstituted ribosomes and RNA polymerase components purified from E. coli. The proteins that carry out transcription/translation are his-tagged, allowing for easy purification of translated proteins in their native state. The reaction is also more well-defined and void of nucleases and proteases that may be present in crude extracts. Cell-free expression systems can be used for the production of functional virions, expression of active mammalian proteins with post-translational modifications, generating protein arrays, and expression of mutant or truncated proteins. Visit the supplier page for more product information.
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