Rabbit anti-Mouse, Rat RIP3 Polyclonal Antibody | anti-RIP3 antibody

Phospho-RIP3 (Thr231/Ser232) Antibody

Cat. Num. AAA9612968

• Gene Names: Ripk3; Rip3; AW107945; 2610528K09Rik
• Reactivity: Mouse, Rat
• Applications: ELISA
• Purity: The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
• Synonyms: RIP3; Polyclonal Antibody; Phospho-RIP3 (Thr231/Ser232) Antibody; anti-RIP3 antibody

• Host: Rabbit
• Reactivity: Mouse, Rat
• Clonality: Polyclonal
• Isotype: Rabbit IgG
• Specificity: Phospho-RIP3 (Thr231/Ser232) Antibody detects endogenous levels of RIP3 only when phosphorylated at Thr231/Ser232.; Tissue Specificity: Expressed in embryo and in adult spleen, liver, testis, heart, brain and lung.
• Purity/Purification: The antibody is from purified rabbit serum by affinity purification via sequential chromatography on phospho-peptide and non-phospho-peptide affinity columns.
• Form/Format: Liquid. Rabbit IgG in phosphate buffered saline, pH7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
• Concentration: 1mg/ml (varies by lot)

• Applicable Applications for anti-RIP3 antibody: Peptide ELISA (EIA)
• Application Notes: Peptide ELISA: 1:20,000-1:40,000
• Immunogen: A synthesized peptide derived from mouse RIP3 around the phosphorylation site of Thr231/Ser232.
• Conjugation: Unconjugated
• Fragment: Fab fragment
• Post Translational Modifications: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (By similarity). Autophosphorylated following interaction with ZBP1. Phosphorylation of Ser-204 plays a role in the necroptotic function of RIPK3 (By similarity). Autophosphorylates at Thr-231 and Ser-232 following activation by ZBP1: phosphorylation at these sites is a hallmark of necroptosis and is required for binding MLKL. Phosphorylation at Thr-187 is important for its kinase activity, interaction with PELI1 and for its ability to mediate TNF-induced necroptosis (By similarity).Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent degradation.
• Subunit Structure: Interacts (via RIP homotypic interaction motif) with RIPK1 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necrosis-inducing complex. Interacts with MLKL; the interaction is direct and triggers necroptosis. Interacts with ZBP1 (via RIP homotypic interaction motif); interaction with ZBP1 activates RIPK3, triggering necroptosis. Upon TNF-induced necrosis, the RIPK1-RIPK3 dimer further interacts with PGAM5 and MLKL; the formation of this complex leads to PGAM5 phosphorylation and increase in PGAM5 phosphatase activity (By similarity). Binds TRAF2 and is recruited to the TNFR-1 signaling complex (By similarity). Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4 (By similarity). Interacts with ARHGEF2 (By similarity). Interacts with PELI1 (via atypical FHA domain); the phosphorylated form at Thr-187 binds preferentially to PELI1. Interacts with BUB1B, TRAF2 and STUB1 (By similarity). Interacts with CASP6 (By similarity). (Microbial infection) Interacts (via RIP homotypic interaction motif) with murid herpesvirus protein RIR1; this interaction disrupts RIP3-RIP1 interactions characteristic of TNF-alpha induced necroptosis, thereby suppressing this death pathway.
• Similarity: The RIP homotypic interaction motif (RHIM) mediates interaction with the RHIM motif of RIPK1. Both motifs form a hetero-amyloid serpentine fold, stabilized by hydrophobic packing and featuring an unusual Cys-Ser ladder of alternating Ser (from RIPK1) and Cys (from RIPK3).Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
• Subcellular Location: Cytoplasm>Cytosol. Nucleus.; Note: Mainly cytoplasmic (PubMed:32200799, PubMed:32296175). Present in the nucleus in response to influenza A virus (IAV) infection (PubMed:32200799).
• Preparation and Storage: Store at -20 degree C. Stable for 12 months from date of receipt.

Related Product Information for anti-RIP3 antibody

Serine/threonine-protein kinase that activates necroptosis and apoptosis, two parallel forms of cell death. Necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members, is triggered by RIPK3 following activation by ZBP1. Activated RIPK3 forms a necrosis-inducing complex and mediates phosphorylation of MLKL, promoting MLKL localization to the plasma membrane and execution of programmed necrosis characterized by calcium influx and plasma membrane damage. In addition to TNF-induced necroptosis, necroptosis can also take place in the nucleus in response to orthomyxoviruses infection: following ZBP1 activation, which senses double-stranded Z-RNA structures, nuclear RIPK3 catalyzes phosphorylation and activation of MLKL, promoting disruption of the nuclear envelope and leakage of cellular DNA into the cytosol. Also regulates apoptosis: apoptosis depends on RIPK1, FADD and CASP8, and is independent of MLKL and RIPK3 kinase activity. Phosphorylates RIPK1: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (By similarity). In some cell types, also able to restrict viral replication by promoting cell death-independent responses. In response to flavivirus infection in neurons, promotes a cell death-independent pathway that restricts viral replication: together with ZBP1, promotes a death-independent transcriptional program that modifies the cellular metabolism via up-regulation expression of the enzyme ACOD1/IRG1 and production of the metabolite itaconate. Itaconate inhibits the activity of succinate dehydrogenase, generating a metabolic state in neurons that suppresses replication of viral genomes. RIPK3 binds to and enhances the activity of three metabolic enzymes: GLUL, GLUD1, and PYGL (By similarity). These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production (By similarity).

NCBI and Uniprot Product Information

• NCBI GI #: 6063101
• NCBI GeneID: 56532
• UniProt Accession #: Q9QZL0; Q3U3Z9; Q8K2Y2; G3X8V8
• NCBI Official Full Name: receptor interacting protein 3
• NCBI Official Synonym Full Names: receptor-interacting serine-threonine kinase 3
• NCBI Official Symbol: Ripk3
• NCBI Official Synonym Symbols: Rip3; AW107945; 2610528K09Rik
• NCBI Protein Information: receptor-interacting serine/threonine-protein kinase 3; RIP-3; mRIP3; RIP-like protein kinase 3; receptor interacting protein 3; receptor-interacting protein 3
• UniProt Protein Name: Receptor-interacting serine/threonine-protein kinase 3
• Protein Family: Putative zinc metalloprotease
• UniProt Gene Name: Ripk3
• UniProt Synonym Gene Names: Rip3; RIP-3; mRIP3
• UniProt Entry Name: RIPK3_MOUSE

Uniprot Description

RIPK3: Promotes apoptosis. Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family. Binds TRAF2 and RIPK1 and is recruited to the TNFR-1 signaling complex. 3 isoforms of the human protein are produced by alternative splicing.

Protein type: EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); Protein kinase, TKL; Kinase, protein; TKL group; RIPK family

Cellular Component: mitochondrion; membrane; cytoplasm; plasma membrane; intracellular; cytosol

Molecular Function: transferase activity; NF-kappaB-inducing kinase activity; identical protein binding; protein serine/threonine kinase activity; protein binding; transferase activity, transferring phosphorus-containing groups; protein complex binding; nucleotide binding; kinase activity; ATP binding; protein kinase activity

Biological Process: spleen development; regulation of activated T cell proliferation; I-kappaB kinase/NF-kappaB cascade; viral reproduction; thymus development; protein heterooligomerization; protein amino acid autophosphorylation; T cell differentiation in the thymus; programmed cell death; positive regulation of transferase activity; lymph node development; protein amino acid phosphorylation; activation of NF-kappaB transcription factor; regulation of T cell mediated cytotoxicity; regulation of adaptive immune response; regulation of interferon-gamma production; activation of protein kinase activity; T cell homeostasis; positive regulation of ligase activity; phosphorylation; protein homooligomerization; positive regulation of oxidoreductase activity