Render Target: STATIC
Render Timestamp: 2024-10-21T09:39:04.491Z
Commit: 4d55b15f5e0754a7adc0cf65b75f728b5d0d4ec3
XML generation date: 2024-08-01 15:25:22.332
Product last modified at: 2024-10-18T14:15:14.039Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

FADD Antibody #2782

Filter:
  • WB

    Supporting Data

    REACTIVITY H
    SENSITIVITY Endogenous
    MW (kDa) 28
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • H-Human 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    FADD Antibody detects endogenous levels of human FADD protein.

    Species Reactivity:

    Human

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser194 of human FADD. Antibodies are purified by protein A and peptide affinity chromatography.

    Background

    Fas-associated death domain (FADD or Mort 1) functions as an important adaptor in coupling death signaling from membrane receptors, such as the Fas ligand and TNF family (DR3, DR4 and DR5), to caspase-8 (1,2). FADD has a carboxy-terminal death domain, which interacts with the cytoplasmic tail of the membrane receptor, and an amino-terminal death effector domain, which interacts with caspase-8. Clustering of the receptors upon stimulation brings about FADD and caspase-8 oligomerization, activating the caspase signaling pathway. Human FADD is phosphorylated mainly at Ser194, while mouse FADD is phosphorylated at Ser191. In both cases, the phosphorylation is cell cycle-dependent (3) and may be related to its regulatory role in embryonic development and cell cycle progression (4,5).
    For Research Use Only. Not For Use In Diagnostic Procedures.
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