FADD Antibody [P17H10] | Primary Antibodies

Application: Reactivity: Mouse

Usage Information

Dilution
WB1:1000 - 1:10000 IP1:30 IHC1:50 - 1:150 IF1:50 FCM1:40

Application
WB, IP, IHC, IF, FCM

Reactivity
Mouse

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW
23 kDa

Positive Control	Mouse kidney tissue; NIH/3T3 cells; RAW264.7 cells
Negative Control

Datasheet & SDS

Biological Description

Specificity
FADD Antibody [P17H10] detects endogenous levels of total FADD protein.

Clone
P17H10

Synonym(s)
Mort1, Fadd, FAS-associated death domain protein, FAS-associating death domain-containing protein, Mediator of receptor induced toxicity replace , with ;

Background
FADD, or Fas-Associated protein with Death Domain, is an adaptor protein that is ubiquitously expressed, with the highest levels found in the thymus and immune cells. It plays a central role in the extrinsic apoptosis pathway by linking death receptors such as Fas or CD95, TNFR1, and TRAIL-R1 or R2 to the activation of effector caspases. FADD consists of an N-terminal death effector domain, composed of six alpha-helices, which recruits procaspase-8 and procaspase-10 through homotypic DED-DED interactions, and a C-terminal death domain, also composed of six alpha-helices, that binds to the death domains of activated receptors. Key interaction surfaces are defined by charged residues that allow weak, conditional DD-DD contacts, facilitating the formation of oligomeric death-inducing signaling complex (DISC) networks when Fas receptors cluster. Upon ligand-induced receptor trimerization, the Fas death domain undergoes a conformational change that exposes FADD-binding sites, allowing FADD to assemble the DISC. Here, FADD's DED recruits and unmasks procaspase-8 and procaspase-10, enabling their dimerization, autocatalytic cleavage, and initiator caspase activation, which then propagates the apoptotic cascade through executioner caspases such as caspase-3, -6, and -7. FADD also regulates necroptosis through the RIPK1 and RIPK3 complex, influences T-cell proliferation through phosphorylation at serine residues 191 and 194, and participates in innate immune responses. FADD is essential for immune homeostasis, prevention of autoimmunity and lymphoproliferative disease, and the removal of damaged cells. Dysregulation of FADD, including overexpression, can promote tumorigenesis by shifting the balance toward anti-apoptotic signaling as seen in T-cell lymphomas and carcinomas, while FADD deficiency leads to embryonic lethality or severe immune dysfunction.

Background

FADD, or Fas-Associated protein with Death Domain, is an adaptor protein that is ubiquitously expressed, with the highest levels found in the thymus and immune cells. It plays a central role in the extrinsic apoptosis pathway by linking death receptors such as Fas or CD95, TNFR1, and TRAIL-R1 or R2 to the activation of effector caspases. FADD consists of an N-terminal death effector domain, composed of six alpha-helices, which recruits procaspase-8 and procaspase-10 through homotypic DED-DED interactions, and a C-terminal death domain, also composed of six alpha-helices, that binds to the death domains of activated receptors. Key interaction surfaces are defined by charged residues that allow weak, conditional DD-DD contacts, facilitating the formation of oligomeric death-inducing signaling complex (DISC) networks when Fas receptors cluster. Upon ligand-induced receptor trimerization, the Fas death domain undergoes a conformational change that exposes FADD-binding sites, allowing FADD to assemble the DISC. Here, FADD's DED recruits and unmasks procaspase-8 and procaspase-10, enabling their dimerization, autocatalytic cleavage, and initiator caspase activation, which then propagates the apoptotic cascade through executioner caspases such as caspase-3, -6, and -7. FADD also regulates necroptosis through the RIPK1 and RIPK3 complex, influences T-cell proliferation through phosphorylation at serine residues 191 and 194, and participates in innate immune responses. FADD is essential for immune homeostasis, prevention of autoimmunity and lymphoproliferative disease, and the removal of damaged cells. Dysregulation of FADD, including overexpression, can promote tumorigenesis by shifting the balance toward anti-apoptotic signaling as seen in T-cell lymphomas and carcinomas, while FADD deficiency leads to embryonic lethality or severe immune dysfunction.

References
https://pubmed.ncbi.nlm.nih.gov/19118384/ https://pubmed.ncbi.nlm.nih.gov/20935634/

Reference Table for Selecting PVDF Membrane Pore Size Specifications

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%