We are analyzing https://link.springer.com/article/10.1007/s12033-011-9463-x.

Title:
High-Yield Expression in Escherichia coli and Purification of Mouse Ubiquitin-Activating Enzyme E1 | Molecular Biotechnology
Description:
Research in the ubiquitin field requires large amounts of ubiquitin-activating enzyme (E1) for in vitro ubiquitination assays. Typically, the mammalian enzyme is either isolated from natural sources or produced recombinantly using baculovirus/insect cell protein expression systems. Escherichia coli is seldom used to produce mammalian E1 probably due to the instability and insolubility of this high-molecular mass protein. In this report, we show that 5–10 mg of histidine-tagged mouse E1 can be easily obtained from a 1 l E. coli culture. A low temperature during the protein induction step was found to be critical to obtain an active enzyme.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

Education
Science
Health & Fitness

Content Management System {📝}

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 {📈}

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.

check SE Ranking
check Ahrefs
check Similarweb
check Ubersuggest
check Semrush

How Does Link.springer.com Make Money? {💸}

We see no obvious way the site makes money.

Some websites aren't about earning revenue; they're built to connect communities or raise awareness. There are numerous motivations behind creating websites. This might be one of them. Link.springer.com has a revenue plan, but it's either invisible or we haven't found it.

Keywords {🔍}

article, google, scholar, cas, enzyme, journal, ubiquitinactivating, biological, chemistry, molecular, purification, coli, carvalho, ubiquitin, expression, escherichia, pinto, grou, ubiquitination, human, mammalian, cell, protein, supplementary, material, privacy, cookies, content, research, access, proteins, publish, search, mouse, jorge, azevedo, ubch, nature, biology, cloning, import, receptor, portugal, author, porto, data, information, log, october, rui,

Topics {✒️}

vitro ubiquitination assays atp-dependent proteolytic system e6ap ubiquitin-protein ligase high-molecular mass protein histidine-tagged mouse e1 human ubiquitin-activating enzyme month download article/chapter human anaphase-promoting complex grants ptdc/bia-bcm/64771/2006 processive brca1-directed ubiquitination high-yield expression ubch5/ubiquitin noncovalent complex clara sá-miranda & jorge related subjects rui vitorino ubiquitin-activating enzyme protein-ubiquitin conjugation high-level expression full article pdf privacy choices/manage cookies protein induction step protein kinase cdc2 fundo social europeu fumiaki yamao ubiquitin-chain formation recombinant e1 enzyme e1 enzyme specific escherichia coli universidade de aveiro author information authors 5-trisphosphate receptor ubiquitination atp·mg2+ binding �covalent affinity” purification peroxisomal import receptor european economic area single common protocol heat-stable polypeptide peroxisome biogenesis disorders poph-qren-tipologia 4 ubiquitin-mediated degradation conditions privacy policy check access molecular biology reports molecular life sciences instant access alphaherpesvirus icp0 family produce mammalian e1 soluble mammalian dsps accepting optional cookies pedro domingues

Schema {🗺️}

WebPage:
      mainEntity:
         headline:High-Yield Expression in Escherichia coli and Purification of Mouse Ubiquitin-Activating Enzyme E1
         description:Research in the ubiquitin field requires large amounts of ubiquitin-activating enzyme (E1) for in vitro ubiquitination assays. Typically, the mammalian enzyme is either isolated from natural sources or produced recombinantly using baculovirus/insect cell protein expression systems. Escherichia coli is seldom used to produce mammalian E1 probably due to the instability and insolubility of this high-molecular mass protein. In this report, we show that 5–10 mg of histidine-tagged mouse E1 can be easily obtained from a 1 l E. coli culture. A low temperature during the protein induction step was found to be critical to obtain an active enzyme.
         datePublished:2011-10-20T00:00:00Z
         dateModified:2011-10-20T00:00:00Z
         pageStart:254
         pageEnd:261
         sameAs:https://doi.org/10.1007/s12033-011-9463-x
         keywords:
            Ubiquitin-activating enzyme
            Purification
             Escherichia coli
            In vitro ubiquitination assays
            UBA1
            Biotechnology
            Biochemistry
            general
            Cell Biology
            Protein Science
            Biological Techniques
            Human Genetics
         image:
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig1_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig2_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig3_HTML.gif
            https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig4_HTML.gif
         isPartOf:
            name:Molecular Biotechnology
            issn:
               1559-0305
               1073-6085
            volumeNumber:51
            type:
               Periodical
               PublicationVolume
         publisher:
            name:Humana Press Inc
            logo:
               url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
               type:ImageObject
            type:Organization
         author:
               name:Andreia F. Carvalho
               affiliation:
                     name:Universidade do Porto
                     address:
                        name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Manuel P. Pinto
               affiliation:
                     name:Universidade do Porto
                     address:
                        name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Cláudia P. Grou
               affiliation:
                     name:Universidade do Porto
                     address:
                        name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Rui Vitorino
               affiliation:
                     name:Universidade de Aveiro
                     address:
                        name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Pedro Domingues
               affiliation:
                     name:Universidade de Aveiro
                     address:
                        name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Fumiaki Yamao
               affiliation:
                     name:National Institute of Genetics
                     address:
                        name:Division of Mutagenesis, National Institute of Genetics, Mishima, Japan
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Clara Sá-Miranda
               affiliation:
                     name:Universidade do Porto
                     address:
                        name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Jorge E. Azevedo
               affiliation:
                     name:Universidade do Porto
                     address:
                        name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
                     name:Universidade do Porto
                     address:
                        name:Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal
                        type:PostalAddress
                     type:Organization
               email:[email protected]
               type:Person
         isAccessibleForFree:
         hasPart:
            isAccessibleForFree:
            cssSelector:.main-content
            type:WebPageElement
         type:ScholarlyArticle
      context:https://schema.org
ScholarlyArticle:
      headline:High-Yield Expression in Escherichia coli and Purification of Mouse Ubiquitin-Activating Enzyme E1
      description:Research in the ubiquitin field requires large amounts of ubiquitin-activating enzyme (E1) for in vitro ubiquitination assays. Typically, the mammalian enzyme is either isolated from natural sources or produced recombinantly using baculovirus/insect cell protein expression systems. Escherichia coli is seldom used to produce mammalian E1 probably due to the instability and insolubility of this high-molecular mass protein. In this report, we show that 5–10 mg of histidine-tagged mouse E1 can be easily obtained from a 1 l E. coli culture. A low temperature during the protein induction step was found to be critical to obtain an active enzyme.
      datePublished:2011-10-20T00:00:00Z
      dateModified:2011-10-20T00:00:00Z
      pageStart:254
      pageEnd:261
      sameAs:https://doi.org/10.1007/s12033-011-9463-x
      keywords:
         Ubiquitin-activating enzyme
         Purification
          Escherichia coli
         In vitro ubiquitination assays
         UBA1
         Biotechnology
         Biochemistry
         general
         Cell Biology
         Protein Science
         Biological Techniques
         Human Genetics
      image:
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig1_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig2_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig3_HTML.gif
         https://media.springernature.com/lw1200/springer-static/image/art%3A10.1007%2Fs12033-011-9463-x/MediaObjects/12033_2011_9463_Fig4_HTML.gif
      isPartOf:
         name:Molecular Biotechnology
         issn:
            1559-0305
            1073-6085
         volumeNumber:51
         type:
            Periodical
            PublicationVolume
      publisher:
         name:Humana Press Inc
         logo:
            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:Andreia F. Carvalho
            affiliation:
                  name:Universidade do Porto
                  address:
                     name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Manuel P. Pinto
            affiliation:
                  name:Universidade do Porto
                  address:
                     name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Cláudia P. Grou
            affiliation:
                  name:Universidade do Porto
                  address:
                     name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Rui Vitorino
            affiliation:
                  name:Universidade de Aveiro
                  address:
                     name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Pedro Domingues
            affiliation:
                  name:Universidade de Aveiro
                  address:
                     name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Fumiaki Yamao
            affiliation:
                  name:National Institute of Genetics
                  address:
                     name:Division of Mutagenesis, National Institute of Genetics, Mishima, Japan
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Clara Sá-Miranda
            affiliation:
                  name:Universidade do Porto
                  address:
                     name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Jorge E. Azevedo
            affiliation:
                  name:Universidade do Porto
                  address:
                     name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
                  name:Universidade do Porto
                  address:
                     name:Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal
                     type:PostalAddress
                  type:Organization
            email:[email protected]
            type:Person
      isAccessibleForFree:
      hasPart:
         isAccessibleForFree:
         cssSelector:.main-content
         type:WebPageElement
["Periodical","PublicationVolume"]:
      name:Molecular Biotechnology
      issn:
         1559-0305
         1073-6085
      volumeNumber:51
Organization:
      name:Humana Press Inc
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:Universidade do Porto
      address:
         name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
         type:PostalAddress
      name:Universidade do Porto
      address:
         name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
         type:PostalAddress
      name:Universidade do Porto
      address:
         name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
         type:PostalAddress
      name:Universidade de Aveiro
      address:
         name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
         type:PostalAddress
      name:Universidade de Aveiro
      address:
         name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
         type:PostalAddress
      name:National Institute of Genetics
      address:
         name:Division of Mutagenesis, National Institute of Genetics, Mishima, Japan
         type:PostalAddress
      name:Universidade do Porto
      address:
         name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
         type:PostalAddress
      name:Universidade do Porto
      address:
         name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
         type:PostalAddress
      name:Universidade do Porto
      address:
         name:Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:Andreia F. Carvalho
      affiliation:
            name:Universidade do Porto
            address:
               name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
      name:Manuel P. Pinto
      affiliation:
            name:Universidade do Porto
            address:
               name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
      name:Cláudia P. Grou
      affiliation:
            name:Universidade do Porto
            address:
               name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
      name:Rui Vitorino
      affiliation:
            name:Universidade de Aveiro
            address:
               name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
               type:PostalAddress
            type:Organization
      name:Pedro Domingues
      affiliation:
            name:Universidade de Aveiro
            address:
               name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
               type:PostalAddress
            type:Organization
      name:Fumiaki Yamao
      affiliation:
            name:National Institute of Genetics
            address:
               name:Division of Mutagenesis, National Institute of Genetics, Mishima, Japan
               type:PostalAddress
            type:Organization
      name:Clara Sá-Miranda
      affiliation:
            name:Universidade do Porto
            address:
               name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
      name:Jorge E. Azevedo
      affiliation:
            name:Universidade do Porto
            address:
               name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
            name:Universidade do Porto
            address:
               name:Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
      name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
      name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
      name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
      name:Departamento de Química, Universidade de Aveiro, Aveiro, Portugal
      name:Division of Mutagenesis, National Institute of Genetics, Mishima, Japan
      name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
      name:Instituto de Biologia Molecular e Celular (IBMC), Universidade do Porto, Porto, Portugal
      name:Instituto de Ciências Biomédicas de Abel Salazar (ICBAS), Universidade do Porto, Porto, Portugal
WebPageElement:
      isAccessibleForFree:
      cssSelector:.main-content

External Links {🔗}(95)

Analytics and Tracking {📊}

Google Tag Manager

Libraries {📚}

Clipboard.js
Prism.js

CDN Services {📦}

Crossref

4.48s.

LINK . SPRINGER . COM {}