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PIDD Products

(P53-Induced Death Domain Protein (PIDD))

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The protein encoded by this gene contains a leucine-rich repeat and a death domain. This protein has been shown to interact with other death domain proteins, such as Fas (TNFRSF6)-associated via death domain (FADD) and MAP-kinase activating death domain-containing protein (MADD), and thus may function as an adaptor protein in cell death-related signaling processes. The expression of the mouse counterpart of this gene has been found to be positively regulated by the tumor suppressor p53 and to induce cell apoptosis in response to DNA damage, which suggests a role for this gene as an effector of p53-dependent apoptosis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2010].

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Featured PIDD Categories

PIDD Antibodies

High quality antibodies with extensive validation data.

Recommended PIDD Antibodies

Product
Reactivity
Application
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Application IHC, WB, IF
Validations
  • (6)
Cat. No. ABIN1680710
Quantity 100 μg
Datasheet Datasheet
Reactivity Human, Mouse, Rat
Application IHC, WB, IF
Validations
  • (5)
Cat. No. ABIN7261141
Quantity 200 μL
Datasheet Datasheet
Reactivity Human
Application IHC, WB, ELISA, ICC, FACS, Neut
Validations
  • (3)
Cat. No. ABIN7193396
Quantity 100 μL
Datasheet Datasheet

Recommended PIDD ELISA Kits

Product
Reactivity
Analytical Method
Validations
Cat. No.
Quantity
Datasheet
Reactivity Human
Analytical Method Quantitative Sandwich ELISA
Validations
Cat. No. ABIN6229101
Quantity 96 tests
Datasheet Datasheet

Latest Publications for our PIDD products

Liu, Shah, Li, Arora, Ung, Raman, Gorbatenko, Kozono, Zhou, Brechin, Barbaro, Thompson, White, Aguirre-Ghiso, Heymach, Lu, Silva, Panageas, Schlessinger, Maki, Skinner, de Stanchina, Sidi: "An IRAK1-PIN1 signalling axis drives intrinsic tumour resistance to radiation therapy." in: Nature cell biology, Vol. 21, Issue 2, pp. 203-213, (2019) (PubMed).

Kung, Khaku, Jennis, Zhou, Murphy: "Identification of TRIML2, a novel p53 target, that enhances p53 SUMOylation and regulates the transactivation of proapoptotic genes." in: Molecular cancer research : MCR, Vol. 13, Issue 2, pp. 250-62, (2015) (PubMed).

Tinel, Janssens, Lippens, Cuenin, Logette, Jaccard, Quadroni, Tschopp: "Autoproteolysis of PIDD marks the bifurcation between pro-death caspase-2 and pro-survival NF-kappaB pathway." in: The EMBO journal, Vol. 26, Issue 1, pp. 197-208, (2007) (PubMed).

Milleron, Bratton: "Heat shock induces apoptosis independently of any known initiator caspase-activating complex." in: The Journal of biological chemistry, Vol. 281, Issue 25, pp. 16991-7000, (2006) (PubMed).

Janssens, Tinel, Lippens, Tschopp: "PIDD mediates NF-kappaB activation in response to DNA damage." in: Cell, Vol. 123, Issue 6, pp. 1079-92, (2005) (PubMed).

Tinel, Tschopp: "The PIDDosome, a protein complex implicated in activation of caspase-2 in response to genotoxic stress." in: Science (New York, N.Y.), Vol. 304, Issue 5672, pp. 843-6, (2004) (PubMed).

Synonyms and alternative names related to PIDD

p53 induced death domain protein 1 (Pidd1), p53-induced death domain protein 1 (PIDD1), p53-induced death domain protein 1 (Pidd1), 1200011D09Rik, AU042446, LRDD, Lrdd, Pidd

Protein level used designations for PIDD

  • leucine-rich repeat and death domain-containing protein
  • p53 protein induced, with death domain
  • p53-induced protein with a death domain
  • leucine-rich repeats and death domain containing
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