Phospho-RIPK3 (Ser316) Antibody - #AF4508
Product: | Phospho-RIPK3 (Ser316) Antibody |
Catalog: | AF4508 |
Description: | Rabbit polyclonal antibody to Phospho-RIPK3 (Ser316) |
Application: | WB |
Reactivity: | Human |
Mol.Wt.: | 46-62kDa; 57kD(Calculated). |
Uniprot: | Q9Y572 |
RRID: | AB_2844557 |
Related Downloads
Protocols
Product Info
*The optimal dilutions should be determined by the end user.
*Tips:
WB: For western blot detection of denatured protein samples. IHC: For immunohistochemical detection of paraffin sections (IHC-p) or frozen sections (IHC-f) of tissue samples. IF/ICC: For immunofluorescence detection of cell samples. ELISA(peptide): For ELISA detection of antigenic peptide.
Cite Format: Affinity Biosciences Cat# AF4508, RRID:AB_2844557.
Fold/Unfold
Receptor interacting protein 3; Receptor interacting serine threonine kinase 3; Receptor interacting serine/threonine protein kinase 3; Receptor-interacting protein 3; Receptor-interacting serine/threonine-protein kinase 3; RIP 3; RIP like protein kinase 3; RIP-3; RIP-like protein kinase 3; RIPK 3; RIPK3; RIPK3_HUMAN;
Immunogens
Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. Isoform 3 is significantly increased in colon and lung cancers.
- Q9Y572 RIPK3_HUMAN:
- Protein BLAST With
- NCBI/
- ExPASy/
- Uniprot
MSCVKLWPSGAPAPLVSIEELENQELVGKGGFGTVFRAQHRKWGYDVAVKIVNSKAISREVKAMASLDNEFVLRLEGVIEKVNWDQDPKPALVTKFMENGSLSGLLQSQCPRPWPLLCRLLKEVVLGMFYLHDQNPVLLHRDLKPSNVLLDPELHVKLADFGLSTFQGGSQSGTGSGEPGGTLGYLAPELFVNVNRKASTASDVYSFGILMWAVLAGREVELPTEPSLVYEAVCNRQNRPSLAELPQAGPETPGLEGLKELMQLCWSSEPKDRPSFQECLPKTDEVFQMVENNMNAAVSTVKDFLSQLRSSNRRFSIPESGQGGTEMDGFRRTIENQHSRNDVMVSEWLNKLNLEEPPSSVPKKCPSLTKRSRAQEEQVPQAWTAGTSSDSMAQPPQTPETSTFRNQMPSPTSTGTPSPGPRGNQGAERQGMNWSCRTPEPNPVTGRPLVNIYNCSGVQVGDNNYLTMQQTTALPTWGLAPSGKGRGLQHPPPVGSQEGPKDPEAWSRPQGWYNHSGK
PTMs - Q9Y572 As Substrate
Site | PTM Type | Enzyme | Source |
---|---|---|---|
K5 | Ubiquitination | Uniprot | |
K55 | Ubiquitination | Uniprot | |
T182 | Phosphorylation | Uniprot | |
S199 | Phosphorylation | Q9Y572 (RIPK3) | Uniprot |
T224 | Phosphorylation | Uniprot | |
S227 | Phosphorylation | Q9Y572 (RIPK3) | Uniprot |
S241 | Phosphorylation | Uniprot | |
T252 | Phosphorylation | Uniprot | |
S299 | Phosphorylation | Uniprot | |
T300 | Phosphorylation | Uniprot | |
S316 | Phosphorylation | Uniprot | |
S320 | Phosphorylation | Uniprot | |
T325 | Phosphorylation | Uniprot | |
S339 | Phosphorylation | Uniprot | |
S359 | Phosphorylation | Uniprot | |
K363 | Ubiquitination | Uniprot | |
S372 | Phosphorylation | Uniprot | |
S410 | Phosphorylation | Uniprot | |
T412 | Phosphorylation | Uniprot | |
R486 | Methylation | Uniprot |
PTMs - Q9Y572 As Enzyme
Research Backgrounds
Essential for necroptosis, a programmed cell death process in response to death-inducing TNF-alpha family members. Upon induction of necrosis, RIPK3 interacts with, and phosphorylates RIPK1 and MLKL to form a necrosis-inducing complex. 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.
RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-199 plays a role in the necroptotic function of RIPK3. Phosphorylation at Ser-227 is required for binding MLKL. Phosphorylation at Thr-182 is important for its kinase activity, interaction with PELI1 and PELI1-mediated 'Lys-48'-linked polyubiquitination and for its ability to mediate TNF-induced necroptosis.
Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Polyubiquitinated with 'Lys-48'-linked chains by PELI1 leading to its subsequent proteasome-dependent degradation. Ubiquitinated by STUB1 leading to its subsequent proteasome-dependent degradation.
Cytoplasm>Cytosol. Cell membrane. Mitochondrion.
Highly expressed in the pancreas. Detected at lower levels in heart, placenta, lung and kidney. Isoform 3 is significantly increased in colon and lung cancers.
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. 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 with MLKL; the interaction is direct. Binds TRAF2 and is recruited to the TNFR-1 signaling complex. Interacts with PYGL, GLUL and GLUD1; these interactions result in activation of these metabolic enzymes. Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. Interacts with ARHGEF2. Interacts with PELI1 (via atypical FHA domain); the phosphorylated form at Thr-182 binds preferentially to PELI1. Interacts with BUB1B, TRAF2 and STUB1. Interacts with ZBP1 (By similarity).
Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.
Research Fields
· Cellular Processes > Cell growth and death > Necroptosis. (View pathway)
· Environmental Information Processing > Signal transduction > TNF signaling pathway. (View pathway)
· Organismal Systems > Immune system > NOD-like receptor signaling pathway. (View pathway)
· Organismal Systems > Immune system > Cytosolic DNA-sensing pathway. (View pathway)
Restrictive clause
Affinity Biosciences tests all products strictly. Citations are provided as a resource for additional applications that have not been validated by Affinity Biosciences. Please choose the appropriate format for each application and consult Materials and Methods sections for additional details about the use of any product in these publications.
For Research Use Only.
Not for use in diagnostic or therapeutic procedures. Not for resale. Not for distribution without written consent. Affinity Biosciences will not be held responsible for patent infringement or other violations that may occur with the use of our products. Affinity Biosciences, Affinity Biosciences Logo and all other trademarks are the property of Affinity Biosciences LTD.