Recombinant human RIP protein (Active) is a Human Fragment protein, in the 1 to 327 aa range, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
>90% SDS-PAGE
Baculovirus infected Sf9 cells
GST tag N-Terminus
SDS-PAGE, FuncS
Yes
M Q P D M S L N V I K M K S S D F L E S A E L D S G G F G K V S L C F H R T Q G L M I M K T V Y K G P N C I E H N E A L L E E A K M M N R L R H S R V V K L L G V I I E E G K Y S L V M E Y M E K G N L M H V L K A E M S T P L S V K G R I I L E I I E G M C Y L H G K G V I H K D L K P E N I L V D N D F H I K I A D L G L A S F K M W S K L N N E E H N E L R E V D G T A K K N G G T L Y Y M A P E H L N D V N A K P T E K S D V Y S F A V V L W A I F A N K E P Y E N A I C E Q Q L I M C I K S G N R P D V D D I T E Y C P R E I I S L M K L C W E A N P E A R P T F P G I E E K F R P F Y L S Q L E E S V E E D V K S L K K E Y S N E N A V V K R M Q S L Q L D C V A
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
Application FuncS | Reactivity Reacts | Dilution info - | Notes - |
Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:15310755, PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity).
RIP, RIP1, RIPK1, RIP1, RIP, Receptor-interacting serine/threonine-protein kinase 1, Cell death protein RIP, Receptor-interacting protein 1, RIP-1
Recombinant human RIP protein (Active) is a Human Fragment protein, in the 1 to 327 aa range, expressed in Baculovirus infected Sf9, with >90% purity and suitable for SDS-PAGE, FuncS.
>90% SDS-PAGE
Baculovirus infected Sf9 cells
GST tag N-Terminus
SDS-PAGE, FuncS
Yes
The specific activity of ab268942 was 9 nmol/min/mg in a kinase assay using MBP protein as substrate.
No
Human
pH: 7.5
Constituents: 25% Glycerol (glycerin, glycerine), 0.87% Sodium chloride, 0.79% Tris HCl, 0.31% Glutathione, 0.004% (R*,R*)-1,4-Dimercaptobutan-2,3-diol, 0.003% EDTA, 0.002% PMSF
M Q P D M S L N V I K M K S S D F L E S A E L D S G G F G K V S L C F H R T Q G L M I M K T V Y K G P N C I E H N E A L L E E A K M M N R L R H S R V V K L L G V I I E E G K Y S L V M E Y M E K G N L M H V L K A E M S T P L S V K G R I I L E I I E G M C Y L H G K G V I H K D L K P E N I L V D N D F H I K I A D L G L A S F K M W S K L N N E E H N E L R E V D G T A K K N G G T L Y Y M A P E H L N D V N A K P T E K S D V Y S F A V V L W A I F A N K E P Y E N A I C E Q Q L I M C I K S G N R P D V D D I T E Y C P R E I I S L M K L C W E A N P E A R P T F P G I E E K F R P F Y L S Q L E E S V E E D V K S L K K E Y S N E N A V V K R M Q S L Q L D C V A
Fragment
1 to 327
Recombinant
GST tag N-Terminus
Liquid
Affinity purified.
Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways (PubMed:17703191, PubMed:24144979, PubMed:31827280, PubMed:31827281, PubMed:32657447, PubMed:35831301). Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival (PubMed:11101870, PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Has kinase-independent scaffold functions: upon binding of TNF to TNFR1, RIPK1 is recruited to the TNF-R1 signaling complex (TNF-RSC also known as complex I) where it acts as a scaffold protein promoting cell survival, in part, by activating the canonical NF-kappa-B pathway (By similarity). Kinase activity is essential to regulate necroptosis and apoptosis, two parallel forms of cell death: upon activation of its protein kinase activity, regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8), which drives apoptosis, and the complex IIb (RIPK1-RIPK3-MLKL), which drives necroptosis (By similarity). RIPK1 is required to limit CASP8-dependent TNFR1-induced apoptosis (By similarity). In normal conditions, RIPK1 acts as an inhibitor of RIPK3-dependent necroptosis, a process mediated by RIPK3 component of complex IIb, which catalyzes phosphorylation of MLKL upon induction by ZBP1 (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis (PubMed:19524512, PubMed:19524513, PubMed:29440439, PubMed:30988283). Required to inhibit apoptosis and necroptosis during embryonic development: acts by preventing the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). In addition to apoptosis and necroptosis, also involved in inflammatory response by promoting transcriptional production of pro-inflammatory cytokines, such as interleukin-6 (IL6) (PubMed:31827280, PubMed:31827281). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation (PubMed:19524513). Phosphorylates DAB2IP at 'Ser-728' in a TNF-alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade (PubMed:15310755, PubMed:17389591). Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity).
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
(Microbial infection) Proteolytically cleaved by S.flexneri OspD3 within the RIP homotypic interaction motif (RHIM), leading to its degradation and inhibition of necroptosis.
Dry Ice
-80°C
-80°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This product is an active protein and may elicit a biological response in vivo, handle with caution.
This supplementary information is collated from multiple sources and compiled automatically.
RIP also known as Receptor-Interacting Protein or RIPK1 is a serine/threonine-protein kinase with a mass of approximately 74 kDa. It plays an important role in cell death and survival signaling pathways. RIP is expressed ubiquitously across various tissues indicating its importance in many cellular functions. The protein contains a kinase domain an intermediate domain for protein-protein interactions and a death domain which facilitates its involvement in apoptotic signaling processes.
Receptor-Interacting Protein Kinase 1 (RIPK1) participates in regulating both necroptosis and apoptosis distinguishing itself as an important mediator in cell death mechanisms. As part of the necrosome complex which includes RIPK3 and MLKL RIPK1 functions in necroptosis—a programmed form of necrosis. This characteristic involvement shows its dual role in maintaining cell fate decisions making it an integral part of immune response and inflammation control.
RIPK1 strongly associates with the TNF signaling pathway and NF-kB pathway. Its interaction with TNF receptor 1 (TNFR1) and consequent involvement with TRADD and TRAF2 mediates the signal transduction necessary for the activation of NF-kB leading to transcription of genes involved in survival and inflammation. This connection illustrates its capability to switch between promoting cell survival through NF-kB and facilitating cell death via necroptosis or apoptosis depending on cellular context and cues.
RIPK1 plays a significant role in conditions such as inflammatory diseases and neurodegenerative disorders. Its overactivation results in excessive cell death implicated in inflammatory conditions; necrostatin a necroptosis inhibitor targets RIPK1 to potentially mitigate this damage. Furthermore RIPK1's dysregulation links to Alzheimer's disease where it can interact with components like RIPK3 to exacerbate neurodegenerative processes. This relationship underlines the potential of targeting RIPK1 therapeutically to manage inflammation and neurodegeneration.
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The specific activity of ab268942 was 9 nmol/min/mg in a kinase assay using MBP protein as substrate.
SDS-PAGE analysis of ab268942.
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