Production of recombinant human ameloblastin by a fully native purification pathway
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00558955" target="_blank" >RIV/61388963:_____/22:00558955 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11130/22:10444779
Result on the web
<a href="https://doi.org/10.1016/j.pep.2022.106133" target="_blank" >https://doi.org/10.1016/j.pep.2022.106133</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.pep.2022.106133" target="_blank" >10.1016/j.pep.2022.106133</a>
Alternative languages
Result language
angličtina
Original language name
Production of recombinant human ameloblastin by a fully native purification pathway
Original language description
Ameloblastin (Ambn) is an intrinsically disordered protein (IDP) with a specific function of forming heterogenous homooligomers. The oligomeric function is led through a specific sequence encoded by exon 5 of Ambn. Due to the IDP character of Ambn to form oligomers, protein purification is subject to many challenges. Human ameloblastin (AMBN) and its two isoforms, I and II have already been purified as a recombinant protein in a bacterial expression system and functionally characterized in vitro. However, here we present a new purification protocol for the production of native AMBN in its original formation as a homooligomeric heterogeneous IDP. The purification process consists of three chromatographic steps utilizing His-tag and Twin Strep-tag affinity chromatography, along with size exclusion and reverse affinity chromatography. The presented workflow offers the production of AMBN in sufficient yield for in vitro protein characterizations and can be used to produce both AMBN isoforms I and II.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
<a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Protein Expression and Purification
ISSN
1046-5928
e-ISSN
1096-0279
Volume of the periodical
198
Issue of the periodical within the volume
October
Country of publishing house
US - UNITED STATES
Number of pages
6
Pages from-to
106133
UT code for WoS article
000826774100001
EID of the result in the Scopus database
2-s2.0-85132738857