MSSVKLWLNGASSISLVGSEELENLGFVGKGGFGAVFRARHTAWNLDVAVKIVNSKKISREVKAMVNLRHENVLLLLGVTENLEWDYVYGPALVTGFMENGSLSGLLQPSCPRPWPLLCRLLEEVVLGMCYLHSLNPSLLHRDLKPSNVLLDPELHAKLADFGLSTFQGGSQSGSGSGSRDSGGTLAYLAPELLDNDGKASKASDVYSFGVLVWTVLAGREAEVVDKTSLIRGAVCNRQRRPPLTELPPDSPETPGLEGLKELMTHCWSSEPKDRPSFQDCESKTNNVYILVQDKVDAAVSKVKHYLSQYRSSDTKLSARESSQKGTEVDCPRETIVYEMLDRLHLEEPSGSVPERLTSLTERRGKEASFGHATPAGTSSDTLAGTPQIPHTLPSRGTTPRPAFTETPGPDPQRNQGDGRNSNPWYTWNAPNPMTGLQSIVLNNCSEVQIGQHNCMSVQPRTAFPKKEPAQFGRGRGW
Note: The complete
sequence may include tag sequence, target protein sequence, linker sequence and extra sequence that is
translated with the protein sequence for the purpose(s) of secretion, stability, solubility, etc.
If the exact amino acid sequence of this recombinant protein is critical to your application,
please explicitly request the full and complete sequence of this protein before ordering.
Mol. Weight
56.1
Protein Length
Full Length
Tag Info
N-terminal 10xHis-tagged and C-terminal Myc-tagged
The tag type will be determined during production process. If you have specified tag type, please tell us and we will develop the specified tag preferentially.
Buffer
Tris-based buffer,50% glycerol
Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
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. 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. These metabolic enzymes may eventually stimulate the tricarboxylic acid cycle and oxidative phosphorylation, which could result in enhanced ROS production.
Gene References into Functions
Data found another important signaling pathway of RIP3 in the nucleus in the neuronal programmed necrosis induced by cerebral ischemia/reperfusion (I/R) injury. The formation of a RIP3-AIF complex and its nuclear translocation are critical to ischemic neuronal DNA degradation and programmed necrosis.PMID:27377128
RIPK1/RIPK3/MLKL-mediated necroptosis may play an important role in nucleus pulposus (NP) cell death induced by continuous mechanical stress. Treatment strategies which aim to regulate necroptosis may prove beneficial, by both reducing NP cells death and slowing IVD degeneration.PMID:28289909
Shikonin induces glioma cell necroptosis in vitro by reactive oxygen species overproduction and promoting RIP1/RIP3 necrosome formation.PMID:28816233
High receptor-interacting protein 3 expression is associated with Chronic Kidney Disease Progression.PMID:27281190
The levels of receptor-interacting serine/threonine protein kinase 1 (RIP1) and RIP3 in osteocytes were significantly increased at 8 weeks after ovariectomy.PMID:26985994
RIP3-induced activation of CaMKII, via phosphorylation or oxidation or both, triggers opening of the mitochondrial permeability transition pore and myocardial necroptosis.PMID:26726877
These results indicated that necroptosis mediated by RIP1 and RIP3 participates in the loss of renal cells of subtotal nephrectomised rats.PMID:25907058
RIP3-dependent necroptosis modulates post-ischaemic adverse remodelling in a mouse model of myocardial infarctionPMID:24920296
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Subcellular Location
Cytoplasm, cytosol. Nucleus.
Protein Families
Protein kinase superfamily, TKL Ser/Thr protein kinase family