NFκB was originally identified as a factor that binds to the immunoglobulin kappa light chain enhancer in B cells. It was subsequently found in non-B cells in an inactive cytoplasmic form consisting of NFκB bound to IkB. NFκB was originally identified as a heterodimeric DNA binding protein complex consisting of p65 (RelA) and p50 (NFκB1) subunits. Other identified subunits include p52 (NFκB2), c-Rel, and RelB. The p65, cRel, and RelB subunits are responsible for transactivation. The p50 and p52 subunits possess DNA binding activity but limited ability to transactivate. p52 has been reported to form transcriptionally active heterodimers with the NFκB subunit p65, similar to p50/p65 heterodimers. The heterodimers of p52/p65 and p50/p65 are regulated by physical inactivation in the cytoplasm by an inhibitor called IkB-a. IkB-a binds to the p65 subunit, preventing nuclear localization and DNA binding. Low levels of p52 and p50 homodimers can also exist in cells.
Immunogen
NFKB2 antibody was raised against a peptide near the N-Terminus of NFKB2 (Human).
Key Feature
Clonality
Polyclonal
Host Species
Rabbit
Tested Applications
ELISAIFIHCIPWB
NFKB2 antibody can be used in ELISA, and immunohistochemistry starting at 20 μg/mL.:
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