Description

Background:

Apoptotic adaptor molecule that recruits caspase-8 or caspase-10 to the activated Fas (CD95) or TNFR-1 receptors. The resulting aggregate called the death-inducing signaling complex (DISC) performs caspase-8 proteolytic activation. Active caspase-8 initiates the subsequent cascade of caspases mediating apoptosis (By similarity). Involved in interferon-mediated antiviral immune response, playing a role in the positive regulation of interferon signaling (By similarity).

Product datasheet:

Overview

Product Description   Phospho-FADD (S191) Polyclonal Antibody, 100µg, (ATB-P0838)
Image
Species ReactivitiesMouse
ImmunogenSynthesized peptide derived from human FADD around the phosphorylation site of S191.

Properties

FormLiquid in PBS containing 50% glycerol, 0.5% BSA and 0.02% sodium azide.
Storage Instructions-20°C/1 year
ClonalityPolyclonal

References:

  1. FADD is essential for glucose uptake and survival of thymocytes. Zhang XY, et al. Biochem Biophys Res Commun, 2014 Aug 22. PMID 25078620
  2. Self-renewal and differentiation of muscle satellite cells are regulated by the Fas-associated death domain. Cheng W, et al. J Biol Chem, 2014 Feb 21. PMID 24375410 Free PMC Article
  3. Inhibition of Fas-associated death domain-containing protein (FADD) protects against myocardial ischemia/reperfusion injury in a heart failure mouse model. Fan Q, et al. PLoS One, 2013. PMID 24058479 Free PMC Article
  4. Role of Fas-associated death domain-containing protein (FADD) phosphorylation in regulating glucose homeostasis: from proteomic discovery to physiological validation. Yao C, et al. Mol Cell Proteomics, 2013 Oct. PMID 23828893 Free PMC Article
  5. Comparative proteomics analysis reveals roles for FADD in the regulation of energy metabolism and proteolysis pathway in mouse embryonic fibroblast. Zhuang H, et al. Proteomics, 2013 Aug. PMID 23744592
  6. A mouse Fas-associated protein with homology to the human Mort1/FADD protein is essential for Fas-induced apoptosis.
    Zhang J., Winoto A.
    Mol. Cell. Biol. 16:2756-2763(1996) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  7. TRADD-TRAF2 and TRADD-FADD interactions define two distinct TNF receptor 1 signal transduction pathways.
    Hsu H., Shu H.-B., Pan M.G., Goeddel D.V.
    Cell 84:299-308(1996) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  8. The transcriptional landscape of the mammalian genome.
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC]

    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: C57BL/6J and NOD.
    Tissue: Heart and Thymus.

  9. The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Czech II.
    Tissue: Mammary gland and Salivary gland.
  10. The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
    Jeong E.-J., Bang S., Lee T.H., Park Y.-I., Sim W.-S., Kim K.-S.
    J. Biol. Chem. 274:16337-16342(1999) [PubMed] [Europe PMC] Cited for: STRUCTURE BY NMR OF 89-183.
external
sizechest(in.)waist(in.)hips(in.)
XS34-3627-2934.5-36.5
S36-3829-3136.5-38.5
M38-4031-3338.5-40.5
L40-4233-3640.5-43.5
XL42-4536-4043.5-47.5
XXL45-4840-4447.5-51.5

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