General Information | |
Product | RIPK1 Antibody Affinity Purified |
Description | Affinity Purified Receptor-interacting Serine/Threonine-protein kinase 1 |
Verified Applications | ELISA, IMM, WB |
Host | Rabbit |
Species Cross Reactivity | Human |
Immunogen | Synthetic peptide taken within aino acid region 620-670 on human Receptor-interacting Serine/Threonine-protein kinase 1 protein. |
Accession # | NCBI: NP_003795.2 |
Physical Properties | |
Quantity | 100 µg |
Volume | 200 µl |
Concentration | 0.55 µg/µl in antibody stabilization buffer |
Form | Affinity Purified |
Clonality | Polyclonal |
Determinant | C-epitope |
Storage | -20⁰C for long term storage |
Application Protocol |
DB | 1:10,000 |
ELISA | 1:10,000 |
Immunoprecipitation | 1:150 |
Western Blot | 1:500 |
Protein |
Uniprot # | Q13546 |
Overview | Serine-threonine kinase which transduces inflammatory and cell-death signals (programmed necrosis) following death receptors ligation, activation of pathogen recognition receptors (PRRs), and DNA damage. Upon activation of TNFR1 by the TNF-alpha family cytokines, TRADD and TRAF2 are recruited to the receptor. Phosphorylates DAB2IP at "Ser-728" in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Ubiquitination by TRAF2 via "Lys-63"-link chains acts as a critical enhancer of communication with downstream signal transducers in the mitogen-activated protein kinase pathway and the NF-kappa-B pathway, which in turn mediate downstream events including the activation of genes encoding inflammatory molecules. Polyubiquitinated protein binds to IKBKG/NEMO, the regulatory subunit of the IKK complex, a critical event for NF-kappa-B activation. Interaction with other cellular RHIM-containing adapters initiates gene activation and cell death. RIPK1 and RIPK3 association, in particular, forms a necrosis-inducing complex. |
Molecular Function | ATP binding; Death domain binding; Identical protein binding; Protein complex binding; Protein kinase activity; protein serine/threonine kinase activity; Ubiquitin protein ligase binding |
Subcellular Location | Cytoplasm |
Structure | Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif). 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. Interacts (via the death domain) with TNFRSF6 (via the death domain) and TRADD (via the death domain). Is recruited by TRADD to TNFRSF1A in a TNF-dependent process. Binds RNF216, EGFR, IKBKG, TRAF1, TRAF2 and TRAF3. Interacts with BNLF1. Interacts with SQSTM1 upon TNF-alpha stimulation. May interact with MAVS/IPS1. Interacts with ZFAND5. Interacts with RBCK1 (By similarity). Interacts with ZBP1 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Upon TNF-induced necrosis, forms in complex with PGAM5, RIPK3 and MLKL. Interacts (via kinase domain) with DAB2IP (via Ras-GAP domain); the interaction occurs in a TNF-alpha-dependent manner. Interacts with ARHGEF2. Interacts (via protein kinase domain) with RFFL; involved in RIPK1 ubiquitination. Interacts with RNF34; involved in RIPK1 ubiquitination. |
Alternative Nomenclature | Cell death protein RIP antibody Receptor (TNFRSF) interacting serine threonine kinase 1 antibody Receptor-interacting protein 1 antibody Serine threonine protein kinase RIP antibody |
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