Receptor-interacting protein kinase 1 (RIPK1) is a critical regulator of apoptosis, necroptosis, and inflammation. It functions as a kinase and scaffolding protein, mediating signaling pathways downstream of death receptors like TNFR1 . Biotin-conjugated RIPK1 antibodies enhance detection sensitivity by enabling streptavidin-based amplification in assays such as Western blot (WB), ELISA, and immunohistochemistry (IHC). These antibodies are essential for studying RIPK1’s role in immune regulation, autoimmunity, and cancer .
Bioss : Detects RIPK1 at ~76 kDa in human, mouse, and rat lysates. Optimal dilution: 1:300–5000.
Novus : Validated for human, mouse, and rat samples. Positive controls include K562 and HeLa lysates .
Bioss : IHC-P and IHC-F validated in mouse/rat tissues. Dilution: 1:200–400 (IHC-P), 1:100–500 (IHC-F).
Novus : Compatible with paraffin-embedded sections using PFA fixation .
RIPK1 is essential for suppressing both apoptosis (via FADD/Caspase-8) and necroptosis (via RIPK3/MLKL) in regulatory T (T-reg) cells. Mice lacking RIPK1 in T-reg cells exhibit fatal autoimmunity due to excessive cell death, highlighting the need for precise RIPK1 detection .
RIPK1 inhibitors (e.g., Necrostatin-34) block necroptosis by stabilizing an inactive RIPK1 conformation. Biotin-conjugated antibodies enable monitoring of RIPK1 activation states in drug development studies .