Phospho-FADD (Ser194) Antibody
(Synonyms: Mort1, Fadd, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity)Phospho-FADD (Ser194) Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to Phospho-FADD (Ser194).
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Host:
Rabbit
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Isotype:
IgG
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Application:
WB, IHC-P
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Reactivity :
Human, Mouse, Rat
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Formulation:
Supplied in PBS (pH 7.4), containing 30% glycerol, 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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IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|---|
| Dilution Ratio | 1:1000-2000 | 1:100-200 |
Product Details
Phospho-FADD (Ser194) Antibody is a Rabbit-derived and non-conjugated IgG Polyclonal antibody, targeting to Phospho-FADD (Ser194).
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Host Rabbit
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Clonality Polyclonal
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Species ReactivityHuman, Mouse, Rat
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Observed Molecular WeightObserved band size: 28 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: 23 kDa
Synthetic phosphopeptide corresponding to residues surrounding S194 of human FADD protein.
Endogenous
affinity purified.
Non-conjugated
Phosphorylated
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in PBS (pH 7.4), containing 30% glycerol, 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
FADD is an Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation. Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis. Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling[1][2][3][4][5][6][7][8][9].
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Subcellular Localization
Cytoplasm
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Expression
Tissue_Specificity: Expressed in a wide variety of tissues, except for peripheral blood mononuclear leukocytes. -
Isoforms & Post-Translational Modification
Phospho-FADD has an amino acid length of 208, molecular weight is 23279 Da.
(Microbial infection) Glycosylated at Arg-117 by enteropathogenic E.coli protein NleB1, C.rodentium protein NleB and S.typhimurium protein Ssek1: arginine GlcNAcylation prevents recruitment of caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. -
Subunit
Can self-associate.
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SwissProt ID
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Synonyms
Mort1, Fadd, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity
Documentation
References
[1]. Carrington PE, et al. The structure of FADD and its mode of interaction with procaspase-8. Mol Cell. 2006 Jun 9;22(5):599-610. [Content Brief]
[2]. Scott FL, et al. The Fas-FADD death domain complex structure unravels signalling by receptor clustering. Nature. 2009 Feb 19;457(7232):1019-22. [Content Brief]
[3]. Wang L, et al. The Fas-FADD death domain complex structure reveals the basis of DISC assembly and disease mutations. Nat Struct Mol Biol. 2010 Nov;17(11):1324-9. [Content Brief]
[4]. Li S, et al. Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains. Nature. 2013 Sep 12;501(7466):242-6. [Content Brief]
[5]. Pearson JS, et al. A type III effector antagonizes death receptor signalling during bacterial gut infection. Nature. 2013 Sep 12;501(7466):247-51. [Content Brief]
[6]. Chinnaiyan AM, et al. FADD, a novel death domain-containing protein, interacts with the death domain of Fas and initiates apoptosis. Cell. 1995 May 19;81(4):505-12. [Content Brief]
[7]. Medema JP, et al. FLICE is activated by association with the CD95 death-inducing signaling complex (DISC). EMBO J. 1997 May 15;16(10):2794-804. [Content Brief]
[8]. Bolze A, et al. Whole-exome-sequencing-based discovery of human FADD deficiency. Am J Hum Genet. 2010 Dec 10;87(6):873-81. [Content Brief]
[9]. Ma Z, et al. DDX24 negatively regulates cytosolic RNA-mediated innate immune signaling. PLoS Pathog. 2013 Oct;9(10):e1003721. [Content Brief]
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