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  • Product Name
    RIPK1 Antibody
  • Catalog No.
  • RRID
  • Source
  • Application
  • Reactivity
    Human, Mouse, Rat
  • Prediction
    Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken
  • UniProt
  • Mol.Wt
  • Concentration
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Product Information

Alternative Names:Expand▼

Cell death protein RIP; FLJ39204; OTTHUMP00000039163; Receptor (TNFRSF) interacting serine threonine kinase 1; receptor interacting protein 1; Receptor interacting protein; Receptor interacting protein kinase 1; Receptor interacting serine threonine protein kinase 1; Receptor TNFRSF interacting serine threonine kinase 1; Receptor-interacting protein 1; Receptor-interacting serine/threonine-protein kinase 1; Rinp; RIP 1; RIP; Rip-1; RIP1; RIPK 1; Ripk1; RIPK1_HUMAN; Serine threonine protein kinase RIP; Serine/threonine-protein kinase RIP;


WB 1:500-1:2000, ELISA(peptide) 1:20000-1:40000
*The optimal dilutions should be determined by the end user.


Human, Mouse, Rat

Predicted Reactivity:

Pig, Bovine, Horse, Sheep, Rabbit, Dog, Chicken






The antiserum was purified by peptide affinity chromatography using SulfoLink™ Coupling Resin (Thermo Fisher Scientific).


RIPK1 Antibody detects endogenous levels of total RIPK1.


Please cite this product as: Affinity Biosciences Cat# AF7877, RRID:AB_2844241.





Storage Condition and Buffer:

Rabbit IgG in phosphate buffered saline , pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.Store at -20 °C.Stable for 12 months from date of receipt.

Immunogen Information in 3D


A synthesized peptide derived from human RIPK1, corresponding to a region within the internal amino acids.


>>Visit The Human Protein Atlas

Gene ID:

Gene Name:


Molecular Weight:

Observed Mol.Wt.: 76kD.
Predicted Mol.Wt.: 76kDa(Calculated)..

Subcellular Location:



Research Background


Serine-threonine kinase which is a key regulator of both cell death and cell survival. Exhibits kinase activity-dependent functions that trigger cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival. Initiates ripoptocide which describes cell death that is dependent on RIPK1, be it apoptosis or necroptosis. 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-kB pathway (By similarity). Specific conditions can however activate RIPK1, and its kinase activity then regulates assembly of two death-inducing complexes, namely complex IIa (RIPK1-FADD-CASP8) and the complex IIb (RIPK1-RIPK3-MLKL) and these complexes respectively drive apoptosis or necroptosis, a regulated form of necrosis. During embryonic development suppresses apoptosis and necroptosis and prevents the interaction of TRADD with FADD thereby limiting aberrant activation of CASP8 (By similarity). Phosphorylates DAB2IP at 'Ser-728' in a TNF- alpha-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Required for ZBP1-induced NF-kappaB activation and activation of NF-kappaB by DNA damage and IR (By similarity).

Post-translational Modifications:

Proteolytically cleaved by CASP8 at Asp-324. Cleavage is crucial for limiting apoptosis and necroptosis during embryonic development (By similarity). Cleavage abolishes NF-kappa-B activation and enhances the interaction of TRADD with FADD.

RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylation of Ser-161 by RIPK3 is necessary for the formation of the necroptosis-inducing complex. Phosphorylation at Ser-25 represses its kinase activity and consequently prevents TNF-mediated RIPK1-dependent cell death. Phosphorylated at Ser-320 by MAP3K7 which requires prior ubiquitination with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 (By similarity). This phosphorylation positively regulates RIPK1 interaction with RIPK3 to promote necroptosis but negatively regulates RIPK1 kinase activity and its interaction with FADD to mediate apoptosis (By similarity).

Ubiquitinated with 'Lys-11'-, 'Lys-48'-, 'Lys-63'- and linear-linked type ubiquitin Ref.33). Polyubiquitination with 'Lys-63'-linked chains by TRAF2 induces association with the IKK complex. Deubiquitination of 'Lys-63'-linked chains and polyubiquitination with 'Lys-48'-linked chains by TNFAIP3 leads to RIPK1 proteasomal degradation and consequently down-regulates TNF-alpha-induced NFkappa-B signaling. 'Lys-48'-linked polyubiquitination by RFFL or RNF34 also promotes proteasomal degradation and negatively regulates TNF-alpha-induced NF-kappa-B signaling Ref.33). Linear polyubiquitinated; the head-to-tail linear polyubiquitination ('Met-1'-linked) is mediated by the LUBAC complex and decreases protein kinase activity. Deubiquitination of linear polyubiquitin by CYLD promotes the kinase activity (By similarity). Polyubiquitinated with 'Lys-48' and 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2, leading to activation of NF-kappa-B. Ubiquitinated with 'Lys-63'-linked chains by PELI1. Ubiquitination at Lys-377 with 'Lys-63'-linked chains by BIRC2/c-IAP1 and BIRC3/c-IAP2 is essential for its phosphorylation at Ser-320 mediated by MAP3K7 (By similarity). This ubiquitination is required for NF-kB activation, suppresses RIPK1 kinase activity and plays a critical role in preventing cell death during embryonic development (By similarity).

Subcellular Location:

Cytoplasm. Cell membrane.

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte

Subunit Structure:

Homodimer. Interacts (via RIP homotypic interaction motif) with RIPK3 (via RIP homotypic interaction motif); this interaction induces RIPK1 phosphorylation and formation of a RIPK1-RIPK3 necroptosis-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 (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. Interacts with ZBP1 (By similarity). Interacts with BIRC2/c-IAP1, BIRC3/c-IAP2 and XIAP/BIRC4. 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 (Ref.33). Interacts with TICAM1 and this interaction is enhanced in the presence of WDFY1. Interacts with PELI1. Interacts (via death domain) with CRADD (via death domain); the interaction is direct. Component of complex IIa composed of at least RIPK1, FADD and CASP8 (By similarity). Interacts with MAP3K7, CFLAR, CASP8, FADD and NEMO (By similarity).

(Microbial infection) Interacts with mumps virus protein SH; this interaction inhibits downstream NF-kappa-B pathway activation.

(Microbial infection) Interacts with Murid herpesvirus 1 protein RIR1.


The death domain mediates dimerization and activation of its kinase activity during necroptosis and apoptosis (PubMed:29440439). It engages other DD-containing proteins as well as a central (intermediate) region important for NF-kB activation and RHIM-dependent signaling (PubMed:10356400).

Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family.

Research Fields

Research Fields:

· Cellular Processes > Cell growth and death > Apoptosis.(View pathway)
· Cellular Processes > Cell growth and death > Necroptosis.(View pathway)
· Environmental Information Processing > Signal transduction > NF-kappa B signaling pathway.(View pathway)
· Environmental Information Processing > Signal transduction > TNF signaling pathway.(View pathway)
· Human Diseases > Infectious diseases: Viral > Hepatitis C.
· Human Diseases > Infectious diseases: Viral > Epstein-Barr virus infection.
· Organismal Systems > Immune system > Toll-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > NOD-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > RIG-I-like receptor signaling pathway.(View pathway)
· Organismal Systems > Immune system > Cytosolic DNA-sensing pathway.(View pathway)

Reference Citations:

1). Liu L;Liang L;Yang C;Zhou Y;Chen Y; et al. Extracellular vesicles of Fusobacterium nucleatum compromise intestinal barrier through targeting RIPK1-mediated cell death pathway. Gut Microbes Jan-Dec 2021;13(1):1-20. (PubMed: 33769187) [IF=7.740]

2). Yang W et al. Transient Inhibition of mTORC1 Signaling Ameliorates Irradiation-Induced Liver Damage. Front Physiol 2019 Mar 20;10:228 (PubMed: 30984007) [IF=3.367]

3). et al. Endoplasmic Reticulum Associated Degradation (ERAD) Deficiency Promotes Mitochondrial Dysfunction and Transcriptional Rewiring in Human Hepatic Cells.

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Catalog Number :

(Blocking peptide available as AF7877-BP)

Price/Size :

Tips: For modified antibodies, we provide modified peptides(0.5mg) and non-modified peptides(0.5mg).

Function :

Blocking peptides are peptides that bind specifically to the target antibody and block antibody binding. These peptide usually contains the epitope recognized by the antibody. Antibodies bound to the blocking peptide no longer bind to the epitope on the target protein. This mechanism is useful when non-specific binding is an issue, for example, in Western blotting (immunoblot) and immunohistochemistry (IHC). By comparing the staining from the blocked antibody versus the antibody alone, one can see which staining is specific; Specific binding will be absent from the western blot or immunostaining performed with the neutralized antibody.

Format and storage :

Synthetic peptide was lyophilized with 100% acetonitrile and is supplied as a powder. Reconstitute with 0.1 ml DI water for a final concentration of 10 mg/ml.The purity is >90%,tested by HPLC and MS.Storage Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.

Precautions :

This product is for research use only. Not for use in diagnostic or therapeutic procedures.

High similarity Medium similarity Low similarity No similarity
Q13546 as Substrate
Site PTM Type Enzyme
S6 Phosphorylation
K13 Ubiquitination
S14 Phosphorylation Q13546 (RIPK1)
S15 Phosphorylation Q13546 (RIPK1)
S20 Phosphorylation Q13546 (RIPK1)
S25 Phosphorylation
S32 Phosphorylation
T38 Phosphorylation
K49 Ubiquitination
K105 Ubiquitination
K115 Ubiquitination
K137 Ubiquitination
K140 Ubiquitination
K153 Ubiquitination
S161 Phosphorylation Q13546 (RIPK1)
K163 Ubiquitination
S166 Phosphorylation Q13546 (RIPK1)
K167 Ubiquitination
K184 Ubiquitination
K185 Ubiquitination
K284 Ubiquitination
S296 Phosphorylation
K302 Ubiquitination
S303 Phosphorylation
K306 Ubiquitination
S309 Phosphorylation
K316 Ubiquitination
S320 Phosphorylation
S330 Phosphorylation
S331 Phosphorylation
S333 Phosphorylation
T337 Phosphorylation
S346 Phosphorylation
K377 Ubiquitination
Y384 Phosphorylation
Y387 Phosphorylation
S389 Phosphorylation
S416 Phosphorylation
Y426 Phosphorylation
Y463 Phosphorylation
Y469 Phosphorylation
S470 Phosphorylation
S471 Phosphorylation
R477 Methylation
T483 Phosphorylation
R487 Methylation
Y490 Phosphorylation
K530 Acetylation
K571 Ubiquitination
K585 Ubiquitination
K596 Ubiquitination
K604 Ubiquitination
S610 Phosphorylation
K627 Ubiquitination
K642 Acetylation
K642 Ubiquitination
K648 Acetylation
S664 Phosphorylation
Q13546 as PTM Enzyme
Substrate Site Source
Q13233 (MAP3K1) S970 Uniprot
Q13546 (RIPK1) S14 Uniprot
Q13546 (RIPK1) S15 Uniprot
Q13546 (RIPK1) S20 Uniprot
Q13546 (RIPK1) S161 Uniprot
Q13546 (RIPK1) S166 Uniprot
Q5VWQ8 (DAB2IP) S728 Uniprot
IMPORTANT: For western blots, incubate membrane with diluted antibody in 5% w/v milk , 1X TBS, 0.1% Tween®20 at 4°C with gentle shaking, overnight.

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