MW 259.33 Da, Purity >99%. Potent, specific necroptosis inhibitor (EC50 = 490 nM). Selective allosteric inhibitor of death domain receptor-associated adaptor kinase RIP1 in vitro (EC50 = 182 nM). Caspase independent, programmed necrosis pathway.
4311-88-0
> 99%
Solid
259.33 Da
C13H13N3OS
2828334
Synthetic
Cell death protein RIP, FLJ39204, OTTHUMP00000039163, RIPK1_HUMAN, Receptor (TNFRSF) interacting serine threonine kinase 1, Receptor TNFRSF interacting serine threonine kinase 1, Receptor interacting protein, Receptor interacting protein kinase 1, Receptor interacting serine threonine protein kinase 1, Receptor-interacting protein 1, Receptor-interacting serine/threonine-protein kinase 1, Rinp, Rip-1, Serine threonine protein kinase RIP, Serine/threonine-protein kinase RIP
MW 259.33 Da, Purity >99%. Potent, specific necroptosis inhibitor (EC50 = 490 nM). Selective allosteric inhibitor of death domain receptor-associated adaptor kinase RIP1 in vitro (EC50 = 182 nM). Caspase independent, programmed necrosis pathway.
4311-88-0
> 99%
Solid
259.33 Da
C13H13N3OS
2828334
Synthetic
Soluble in ethanol to 50 mM. Soluble in DMSO to 100 mM.
5-(1H-indol-3-ylmethyl)-3-methyl-2-thioxo-4-Imidazolidinone
Potent, specific necroptosis inhibitor (EC50 = 490 nM). Selective allosteric inhibitor of death domain receptor-associated adaptor kinase RIP1 in vitro (EC50 = 182 nM). Caspase independent, programmed necrosis pathway.
CN1C(=O)C(NC1=S)CC2=CNC3=CC=CC=C32
InChI=1S/C13H13N3OS/c1-16-12(17)11(15-13(16)18)6-8-7-14-10-5-3-2-4-9(8)10/h2-5,7,11,14H,6H2,1H3,(H,15,18)
TXUWMXQFNYDOEZ-UHFFFAOYSA-N
5-(1H-indol-3-ylmethyl)-3-methyl-2-sulfanylideneimidazolidin-4-one
Ambient - Can Ship with Ice
-20°C
-20°C
Store under desiccating conditions, The product can be stored for up to 12 months
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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2D chemical structure image of ab141053, Necrostatin-1, necroptosis inhibitor
Necroptosis exists in PDLSCs.
TEM, a representative normal cell (the cell had a long fusiform, cell membrane structure was complete, the nucleus was round, nucleolus was obvious and center), b representative necroptosis cell (cell membrane ruptured, organelle disappeared, chromatin consolidated and agglutinated, presenting necrotic ultrastructural characteristics), c representative necrosis cell after Nec-1 inhibited (the cell membrane was intact, and the chromatin structure returned to normal).
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