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AB89242

Recombinant Human FADD protein

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Recombinant Human FADD protein is a Human Full Length protein, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.

View Alternative Names

MORT1, GIG3, FADD, FAS-associated death domain protein, FAS-associating death domain-containing protein, Growth-inhibiting gene 3 protein, Mediator of receptor induced toxicity

1 Images
SDS-PAGE - Recombinant Human FADD protein (AB89242)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human FADD protein (AB89242)

SDS-PAGE analysis of ab89242 (3 μg) under reducing conditions and visualized by coomassie blue stain.

Key facts

Purity

>85% SDS-PAGE

Expression system

Escherichia coli

Tags

Tag free

Applications

SDS-PAGE

applications

Biologically active

No

Accession

Q13158

Animal free

No

Carrier free

No

Species

Human

Storage buffer

pH: 8 Constituents: 10% Glycerol (glycerin, glycerine), 0.316% Tris HCl

storage-buffer

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Reactivity data

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }
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Sequence info

[{"sequence":"","proteinLength":"Full Length","predictedMolecularWeight":null,"actualMolecularWeight":null,"aminoAcidEnd":0,"aminoAcidStart":0,"nature":"Recombinant","expressionSystem":null,"accessionNumber":"Q13158","tags":[]}]
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Properties and storage information

Shipped at conditions
Blue Ice
Appropriate short-term storage conditions
-20°C
Appropriate long-term storage conditions
-20°C
Aliquoting information
Upon delivery aliquot
Storage information
Avoid freeze / thaw cycle
False
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Supplementary information

This supplementary information is collated from multiple sources and compiled automatically.

FADD also known as Fas-Associated protein with Death Domain is an adaptor molecule with a molecular weight of approximately 23 kDa. It plays a critical role in the transmission of apoptotic signals. FADD is widely expressed in various tissues particularly in the thymus and immune system cells. This protein serves as a bridge linking death receptors like Fas and TNFR-1 with caspase activation pathways.
Biological function summary

FADD is essential in apoptosis where it assists in the assembly of the death-inducing signaling complex (DISC). Upon receptor activation FADD recruits procaspase-8 or -10 to DISC promoting their autocatalytic cleavage and activation. This leads to the subsequent cascade that results in cell apoptosis. FADD also plays a role in necroptosis and is involved in the immune response regulation highlighting its multifunctional nature in cellular processes.

Pathways

FADD integrates into the apoptotic and necroptotic pathways. In the apoptotic pathway it interacts closely with Fas a death receptor to promote caspase-8 activation. Additionally in the necroptotic pathway FADD associates with RIP1 and RIP3 contributing to an alternative form of programmed cell death. These interactions underline its significant role in controlling cell fate decisions.

Aberrations in FADD function are associated with cancer and autoimmune diseases. Overexpression or mutation of FADD can lead to unchecked cell proliferation or defective apoptosis contributing to cancer development. In autoimmune disorders improper regulation of FADD may disrupt immune tolerance and lead to systemic inflammation. Key proteins involved in these disease processes include caspase-8 and RIPK1 which interact with FADD in regulating cell death and survival mechanisms.
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Specifications

Form

Liquid

Additional notes

ab89242 is purified using conventional chromatography techniques.

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General info

Function

Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed : 16762833, PubMed : 19118384, PubMed : 20935634, PubMed : 23955153, PubMed : 24025841, PubMed : 7538907, PubMed : 9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed : 16762833, PubMed : 19118384, PubMed : 20935634, PubMed : 7538907, PubMed : 9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed : 16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed : 21109225).

Post-translational modifications

(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.

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Product protocols

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Target data

Apoptotic adapter molecule that recruits caspases CASP8 or CASP10 to the activated FAS/CD95 or TNFRSF1A/TNFR-1 receptors (PubMed : 16762833, PubMed : 19118384, PubMed : 20935634, PubMed : 23955153, PubMed : 24025841, PubMed : 7538907, PubMed : 9184224). The resulting aggregate called the death-inducing signaling complex (DISC) performs CASP8 proteolytic activation (PubMed : 16762833, PubMed : 19118384, PubMed : 20935634, PubMed : 7538907, PubMed : 9184224). Active CASP8 initiates the subsequent cascade of caspases mediating apoptosis (PubMed : 16762833). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (PubMed : 21109225).
See full target information FADD
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