Rabbit polyclonal primary
RIP3 Rabbit Polyclonal Antibody (ER1901-27)
Synthetic peptide within mouse rip3 aa 403-426.
Mouse lung tissue, A549, PANC-1, rat kidney tissue, rat pancreas tissue, mouse colon tissue, mouse pancreas tissue.
Store at +4C after thawing. Aliquot store at -20C. Avoid repeated freeze / thaw cycles.
1*PBS (pH7.4), 0.2% BSA, 50% Glycerol. Preservative: 0.05% Sodium Azide.
Peptide affinity purified.
Receptor interacting protein 3 antibody; Receptor interacting serine threonine kinase 3 antibody; Receptor interacting serine/threonine protein kinase 3 antibody; Receptor-interacting protein 3 antibody; Receptor-interacting serine/threonine-protein kinase 3 antibody; RIP 3 antibody; RIP like protein kinase 3 antibody; RIP-3 antibody; RIP-like protein kinase 3 antibody; RIPK 3 antibody; RIPK3 antibody; RIPK3_HUMAN antibody
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. Isoform 3 is significantly increased in colon and lung cancers.
RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-199 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-227 is required for binding MLKL. Phosphorylation at Thr-182 is important for its kinase activity, interaction with PELI1 and PELI1-mediated 'Lys-48'-linked polyubiquitination and for its ability to mediate TNF-induced necroptosis.; Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Polyubiquitinated with 'Lys-48'-linked chains by PELI1 leading to its subsequent proteasome-dependent degradation. Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent degradation.
Cytoplasm. Membrane. Mitochondrion.
The product of this gene is a member of the receptor-interacting protein (RIP) family of serine/threonine protein kinases, and contains a C-terminal domain unique from other RIP family members. The encoded protein is predominantly localized to the cytoplasm, and can undergo nucleocytoplasmic shuttling dependent on novel nuclear localization and export signals. Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production.