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Cleaving Glutathione S‐Transferase from a B‐cell Receptor Protein to Improve Interactions as seen in EMSAS
Author(s) -
Egbuchulam Angela,
Lares Monica
Publication year - 2018
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.2018.32.1_supplement.530.29
Subject(s) - aptamer , rna , receptor , glutathione , glutathione s transferase , chemistry , microbiology and biotechnology , biochemistry , biology , enzyme , gene
The purpose of my project is understanding the specific amino acid interactions for the B‐cell Receptor, BAFF‐R, protein interacting with a RNA aptamer. A RNA aptamer is a peptide that binds to a molecule of interest. We had to express our protein with a GST tag. We used different lab skills, such as gel shift assay, to investigate the interaction between the BAFF‐R and its RNA aptamer. However, the results were inconclusive as we saw an unexpected binding pattern. We hypothesize that cleaving the Glutathione S‐Transferase (GST) tag using thrombin will provide for our expected binding pattern in an EMSA. Support or Funding Information Funded by Office of Undergraduate Research in Sonoma State University. This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal .