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dc.contributor.advisorPollock, R.
dc.contributor.authorBornfleth, Lorelei
dc.date.accessioned2020-08-13T14:55:26Z
dc.date.available2020-08-13T14:55:26Z
dc.date.issued2003-01-01 0:00
dc.identifier.urihttps://scholar.oxy.edu/handle/20.500.12711/487
dc.description.abstractAlthough the exact molecular mechanism is not known, b cell differentiation is a process tightly regulated by cell-surface receptors. In our research we sought to examine the physical structure of the b cell receptor (BCR) within a transgenic model, in order to gain insight into this differentiation process. In this work we use mice and murine hybridoma-cell-lines that express the HUG-heavy chain within their antibodies.The HUG-gene is a chimeric transgene that encodes the constant region of the human g-class heavy chain and a dansyl-specific murine variable region. We are interested in finding out whether HUG can substitute for the μ-heavy chain in the BCR and to examine whether HUG associates with the same proteins as μ in the BCR. To this end, we immunoprecipitated Igb, a known component of the pre-BCR and BCR, from bone marrow and spleen cells obtained from mice of different genetic backgrounds. Immunoprecipitation and Western blot analysis allowed us to examine whether HUG and/or μ associate with Igb.
dc.description.sponsorshipHoward Hughes Medical Institute
dc.titlePhysical Associations of the b Cell Receptor within a Transgenic Model: Insight into Light Chain Rearrangement
dc.typearticle
dc.abstract.formathtml
dc.description.departmentbio
dc.source.issueurc_student
dc.source.issueurc_student
dc.identifier.legacyhttps://scholar.oxy.edu/urc_student/1015
dc.source.statuspublished


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