Cleaved-RIP (Asp324) Antibody (YA9983)
(Synonyms: RIP, RIP1, RIPK1, Receptor-interacting serine/threonine-protein kinase 1, Cell death protein RIP, Receptor-interacting protein 1, RIP-1)Cleaved-RIP (Asp324) Antibody (YA9983) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to Cleaved-RIP (Asp324).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 50% glycerol, 0.05% BSA and 0.01% sodium azide.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
WB
WB: Western Blot
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|---|---|
| Dilution Ratio | 1:1000-2000 |
Product Details
Cleaved-RIP (Asp324) Antibody (YA9983) is a Rabbit-derived and non-conjugated IgG Monoclonal, Recombinant antibody, targeting to Cleaved-RIP (Asp324).
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Host Rabbit
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Clonality Monoclonal,Recombinant
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 44 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 75 kDa
Synthetic peptide encompassing a sequence human Cleaved-RIPK1.
Endogenous
affinity purified.
Non-conjugated
Cleaved
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 50% glycerol, 0.05% BSA and 0.01% sodium azide.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
Cleaved-RIP is a Serine-threonine kinase which is a key regulator of TNF-mediated apoptosis, necroptosis and inflammatory pathways. Exhibits kinase activity-dependent functions that regulate cell death and kinase-independent scaffold functions regulating inflammatory signaling and cell survival. 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. Inhibits RIPK3-mediated necroptosis via FADD-mediated recruitment of CASP8, which cleaves RIPK1 and limits TNF-induced necroptosis. 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). Phosphorylates RIPK3: RIPK1 and RIPK3 undergo reciprocal auto- and trans-phosphorylation. Phosphorylates DAB2IP at 'Ser-728' in a TNF-dependent manner, and thereby activates the MAP3K5-JNK apoptotic cascade. Required for ZBP1-induced NF-kappa-B activation in response to DNA damage (By similarity)[1][2][3][4][5][6][7][8][9][10][11][12][13].
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Subcellular Localization
Cytoplasm; Cell membrane
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Isoforms & Post-Translational Modification
Cleaved-RIP has 2 isoforms, Q13546-1: amino acid length is 671, molecular weight is 75931 Da (predicted); Q13546-2: amino acid length is 625, molecular weight is 70733 Da (predicted).(Microbial infection) Proteolytically cleaved by S.flexneri OspD3 within the RIP homotypic interaction motif (RHIM), leading to its degradation and inhibition of necroptosis
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Subunit
Homodimer.
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SwissProt ID
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Synonyms
RIP, RIP1, RIPK1, Receptor-interacting serine/threonine-protein kinase 1, Cell death protein RIP, Receptor-interacting protein 1, RIP-1
Documentation
References
[1]. Shembade N, et al. Essential role for TAX1BP1 in the termination of TNF-alpha-, IL-1- and LPS-mediated NF-kappaB and JNK signaling. EMBO J. 2007 Sep 5;26(17):3910-22. [Content Brief]
[2]. Zaman MM, et al. Ubiquitination-deubiquitination by the TRIM27-USP7 complex regulates tumor necrosis factor alpha-induced apoptosis. Mol Cell Biol. 2013 Dec;33(24):4971-84. [Content Brief]
[3]. Tao P, et al. A dominant autoinflammatory disease caused by non-cleavable variants of RIPK1. Nature. 2020 Jan;577(7788):109-114. [Content Brief]
[4]. Lalaoui N, et al. Mutations that prevent caspase cleavage of RIPK1 cause autoinflammatory disease. Nature. 2020 Jan;577(7788):103-108. [Content Brief]
[5]. Ashida H, et al. A unique bacterial tactic to circumvent the cell death crosstalk induced by blockade of caspase-8. EMBO J. 2020 Sep 1;39(17):e104469. [Content Brief]
[6]. Hou B, et al. Grb2 interacts with necrosome components and is involved in rasfonin-induced necroptosis. Cell Death Discov. 2022 Jul 13;8(1):319. [Content Brief]
[7]. Holler N, et al. Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule. Nat Immunol. 2000 Dec;1(6):489-95. [Content Brief]
[8]. He S, et al. Receptor interacting protein kinase-3 determines cellular necrotic response to TNF-alpha. Cell. 2009 Jun 12;137(6):1100-11. [Content Brief]
[9]. Cho YS, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell. 2009 Jun 12;137(6):1112-23. [Content Brief]
[10]. Meng H, et al. Death-domain dimerization-mediated activation of RIPK1 controls necroptosis and RIPK1-dependent apoptosis. Proc Natl Acad Sci U S A. 2018 Feb 27;115(9):E2001-E2009. [Content Brief]
[11]. Dondelinger Y, et al. Serine 25 phosphorylation inhibits RIPK1 kinase-dependent cell death in models of infection and inflammation. Nat Commun. 2019 Apr 15;10(1):1729. [Content Brief]
[12]. Zhang H, et al. AIP1/DAB2IP, a novel member of the Ras-GAP family, transduces TRAF2-induced ASK1-JNK activation. J Biol Chem. 2004 Oct 22;279(43):44955-65. [Content Brief]
[13]. Zhang H, et al. RIP1-mediated AIP1 phosphorylation at a 14-3-3-binding site is critical for tumor necrosis factor-induced ASK1-JNK/p38 activation. J Biol Chem. 2007 May 18;282(20):14788-96. [Content Brief]
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