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LINK . SPRINGER . COM {}

  1. Analyzed Page
  2. Matching Content Categories
  3. CMS
  4. Monthly Traffic Estimate
  5. How Does Link.springer.com Make Money
  6. Keywords
  7. Topics
  8. Schema
  9. External Links
  10. Analytics And Tracking
  11. Libraries
  12. CDN Services

We are analyzing https://link.springer.com/article/10.1007/s00253-020-10402-8.

Title:
Fusion tags to enhance heterologous protein expression | Applied Microbiology and Biotechnology
Description:
Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system. Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {πŸ“š}

  • Education
  • Science
  • Food & Drink

Content Management System {πŸ“}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {πŸ“ˆ}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 5,000,019 visitors per month in the current month.
However, some sources were not loaded, we suggest to reload the page to get complete results.

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How Does Link.springer.com Make Money? {πŸ’Έ}

We see no obvious way the site makes money.

Earning money isn't the goal of every website; some are designed to offer support or promote social causes. People have different reasons for creating websites. This might be one such reason. Link.springer.com might be cashing in, but we can't detect the method they're using.

Keywords {πŸ”}

article, google, scholar, pubmed, cas, protein, expression, coli, escherichia, fusion, proteins, central, purification, biotechnol, recombinant, httpsdoiorgs, microbiol, tag, cell, heterologous, httpsdoiorg, tags, soluble, production, kim, peptide, solubility, expr, purif, httpsdoiorgjpep, human, factories, lee, biochem, biol, wang, system, chapter, microb, appl, technology, mol, zhang, inclusion, methods, prokaryotic, nguyen, sci, membrane, domain,

Topics {βœ’οΈ}

rescuing aggregation-prone proteins organic solvent-tolerant Ξ²-fructofuranosidase crispr/cas9-mediated genome engineering channel-forming trans-membrane domain month download article/chapter seung pil pack hexahistidine-tagged maltose-binding protein internally-duplicated carbonic anhydrase inclusion body formation baculovirus/insect cell systems bacterial cell-free systems enhancing protein expression cell-free expression systems hehehe-tagged affibody molecule article applied microbiology peptide guided auto-secretion sumo fusion tag sep tag enhances optimized npro-based method g-protein-coupled receptors hexa-lysine tag disulfide bond-dependent proteins n-terminal fusion tags data-driven designed tags signal peptide-dependent proteins clostridium cellulovorans endoglucanase-xylanase single-chain variable fragment column-free protein purification full article pdf bacterial inclusion bodies fusion tag article ki heterologous protein secretion protein disulfide isomerase heterologous protein expression membrane protein expression nguyen tkm protein-coupled receptor privacy choices/manage cookies membrane protein architects membrane-integrating protein maltose binding protein maltose-binding protein cellulose-binding domain cellulose binding domain de souza em recombinant protein expression heterologous protein overexpression antimicrobial peptide mediated ribonuclease s-peptide

Schema {πŸ—ΊοΈ}

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         headline:Fusion tags to enhance heterologous protein expression
         description:Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system. Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.
         datePublished:2020-01-28T00:00:00Z
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      headline:Fusion tags to enhance heterologous protein expression
      description:Escherichia coli is the most widely used heterologous protein expression system. However, this system remains a challenge due to the low solubility of proteins, insufficient yield, and inclusion body formation. Numerous approaches have sought to address these issues. The use of a fusion tag is one of the most powerful strategies for obtaining large amounts of heterologous protein in E. coli expression system. Here, recent advances in fusion tags that increase the expression of proteins are reviewed. In addition, proposed concepts for designing peptide tags to increase protein expression are discussed.
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External Links {πŸ”—}(553)

Analytics and Tracking {πŸ“Š}

  • Google Tag Manager

Libraries {πŸ“š}

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CDN Services {πŸ“¦}

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