Rel B is part of the NFκB complex and forms heterodimeric complexes with p50 (NFKB1) and p52 (NFKB2). The homodimeric complexes of Rel B alone do not show DNA-binding activity. IHC analysis has shown that Rel B expression correlated with dendritic cell activation. NFκB-inducing kinase NIK is required for osteoclastogenesis in response to pathologic stimuli and overexpression of Rel B rescues differentiation of mouse NIK -/- osteoclast precursors. Rel B is required for RANKL-induced osteoclastogenesis in vitro and for TNF -induced bone resorption in vivo. This indicates that the alternative NFκB pathway, via Rel B, plays an essential and unique role in RANKL signaling toward osteoclast development.
Proceedings of the National Academy of Sciences of the United States of America, 105(10), 3897-3902 (2008-03-07)
NF-kappaB inducing kinase (NIK) is required for osteoclastogenesis in response to pathologic stimuli, and its loss leads to functional blockade of both alternative and classical NF-kappaB caused by cytoplasmic retention by p100. We now show that deletion of p100 restores
RelB belongs to the family of Rel-related proteins, dimers of which determine NF-kappa B activity. The murine RelB protein has been reported to be a dimerizing partner in kappa B-binding complexes which are capable of transactivation. On the other hand
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