Rageia Elfageih

Rageia Elfageih

Laboratory Technician
Visiting address: Alfred Nobels Allé 8, plan 7, 14152 Huddinge
Postal address: H7 Medicin, Huddinge, H7 CIM Norrby-Teglund, 171 77 Stockholm

About me

  • Doctor of biochemistry sciences with experience in basic, medical, and 

  • clinical biochemistry and molecular biology with more than nine years of 
  • research and teaching experience. Knowledgeable in pharmaceutical sciences,  
  • with a particular interest in drug discovery and drug design. I'm 
  • interested in continuing career development in academic scientific researchto apply biochemistry, molecular biology, biotechnology, and project 
  • management knowledge and skills. Curiosity and enthusiasm to solve male 
  • infertility issues, particularly childhood cancer survivors who experienced 
  • oncological diseases and are subjected to gonadotoxic therapy such as 
  • chemotherapy and radiotherapy. Multitasking with the ability to lead and 
  • manage projects independently and with others. Other people describe me as 
  • helpful, problem solver, creative, taking challenges, and 
  • supportive. *https://orcid.org/0000-0003-0506-1470* [1]
    2015-2021: Ph.D. in Biochemistry- Stockholm University.
    2004-2009: Master's degree in Biochemistry- University of Benghazi- Libya.
    1999-2003: Bachelors in Pharmaceutical Sciences- University of 
  • Benghazi-Libya.


  • 2021-2023 I was working with development of a high-quality in vitro human testicular tissue culture approach. The clinical 

  • significance of this study is to preserve the fertility of the childhood 
  • cancer survivors who experienced various cancer therapeutic regimens. 
  • Moreover, it might help childhood cancer survivors who cryopreserved a 
  • testicular tissue before starting gonadotoxic therapies to restore their 
  • fertility by using their tissue samples in the future and thereby enhancing 
  • these patients' quality of life. 
  • https://nordfertil.org/


  • 2015-2021 PhD studies was focusing on Production and folding of proteins in the periplasm of 

  • Escherichia coli. These studies have aimed at developing strategies to enhance recombinant protein production yields in the periplasm, to better understand what happens when a protein is produced in the periplasm, and to shed light on the protein folding process in the periplasm. It has been shown that evolving translation initiation regions (TIRs) can enhance periplasmic protein production yields of a variety of proteins. Furthermore, it has been shown that the protein translocation machinery can adapt for enhanced periplasmic recombinant protein production. Force profile analysis was used to study cotranslational folding of the periplasmic disulfide-bond containing protein alkaline phosphatase (PhoA) in the periplasm. It was shown that folding-induced forces can be transmitted via the nascent chain from the periplasm to the peptidyl transferase center in the ribosome and that PhoA appears to fold co translationally via disulfide-stabilized folding intermediates. Finally, the S. pneumoniae neuraminidases NanA, NanB, and NanC were produced in E. coli and subsequently isolated. The activity of these neuraminidases was monitored at different pH as well as their oligomeric state was studied. https://www.diva-portal.org/smash/record.jsf?pid=diva2%3A1539920&
  • dswid=7356


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