LRDD Purified Maxpab Mouse Polyclonal Antibody (B01P)

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LRDD Purified Maxpab Mouse Polyclonal Antibody (B01P)

LRDD purified MaxPab mouse page for detailed protocols polyclonal antibody (B01P) Storage Buffer: In 1x PBS, pH 7.4 Catalog Number: H00055367-B01P Storage Instruction: Store at -20°C or lower. Aliquot to avoid repeated freezing and thawing. Regulatory Status: For research use only (RUO) Entrez GeneID: 55367 Product Description: Mouse polyclonal antibody raised against a full-length human LRDD protein. Gene Symbol: LRDD Immunogen: LRDD (ABW03662.1, 1 a.a. ~ 893 a.a) Gene Alias: DKFZp434D229, MGC16925, PIDD full-length human protein. Gene Summary: The protein encoded by this gene Sequence: contains a leucine-rich repeat and a death domain. This MAATVEGPELEAAAAAGDASEDSDAGSRALPFLGGN protein has been shown to interact with other death RLSLDLYPGGCQQLLHLCVQQPLQLLQVEFLRLSTHE domain proteins, such as Fas (TNFRSF6)-associated via DPQLLEATLAQLPQSLSCLRSLVLKGGQRRDTLGACL death domain (FADD) and MAP-kinase activating death RGALTNLPAGLSGLAHLAHLDLSFNSLETLPACVLQMR domain-containing protein (MADD), and thus may GLGALLLSHNCLSELPEALGALPALTFLTVTHNRLQTLP function as an adaptor protein in cell death-related PALGALSTLQRLDLSQNLLDTLPPEIGGLGSLLELNLAS signaling processes. The expression of the mouse NRLQSLPASLAGLRSLRLLVLHSNLLASVPADLARLPLL counterpart of this gene has been found to be positively TRLDLRDNQLRDLPPELLDAPFVRLQGNPLGEASPDA regulated by the tumor suppressor p53 and to induce PSSPVAALIPEMPRLFLTSDLDSFPVTPRGCSVTLACG cell apoptosis in response to DNA damage, which VRLQFPAGATATPITIRYRLLLPEPGLVPLGPHDALLSH suggests a role for this gene as an effector of VLELQPHGVAFQQDVGLWLLFTPPQARRCREVVVRT p53-dependent apoptosis. Three alternatively spliced RNDNSWGDLETYLEEEAPQRLWAHCQVPHFSWFLVV transcript variants encoding distinct isoforms have been SRPVSNACLVPPEGTLLCSSGHPGVKVIFPPGATEEP reported. [provided by RefSeq] RRVSMQVVRMAGRELQALLGEPEAAVSPLLCLSQSG PPSFLQPVTVQLPLPSGITGLSLDRSRLHLLYWAPPAA TWDDITAQVVLELTHLYARFQVTHFSWYWLWYTTKNC VGGLARKAWERLRLHRVNLIALQRRRDPEQVLLQCLP RNKVDATLRRLLERYRGPEPSDTVEMFEGEEFFAAFE RGIDVDADRPDCVEGRICFVFYSHLKNVKEVSFYRGA VPVRVPEEAEAARQRKGADALWMATLPIKLPRLRGSE GPRRGAGLSLAPLNLGDAETGFLTQSNLLSVAGRLGL DWPAVALHLGVSYREVQRIRHEFRDDLDEQIRHMLFS WAERQAGQPGAVGLLVQALEQSDRQDVAEEVRAVLE LGRRKYQDSIRRMGLAPKDPALPGSSAPQPPEPAQA Host: Mouse Reactivity: Human Applications: WB-Tr (See our web site product page for detailed applications information) Protocols: See our web site at http://www.abnova.com/support/protocols.asp or product Page 1/1 Powered by TCPDF (www.tcpdf.org).

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The Piddosome, DNA-Damage-Induced Apoptosis and Beyond
Cell Death and Differentiation (2012) 19, 13–20 & 2012 Macmillan Publishers Limited All rights reserved 1350-9047/12 www.nature.com/cdd Review The PIDDosome, DNA-damage-induced apoptosis and beyond S Janssens*,1 and A Tinel*,2 P53-induced protein with a death domain (PIDD) was cloned as a death domain (DD)-containing protein whose expression is induced by p53. It was later described as the core of a molecular platform-activating caspase-2, named the PIDDosome. These first results pointed towards a role for PIDD in apoptosis, in response to DNA damage. Identification of new PIDDosome complexes involved in DNA repair and nuclear factor-jB signaling challenged this early concept. PIDD functions are growing as new complexes and new interaction partners are being discovered, and as additional functions are being revealed. A fascinating feature of PIDD lies within its complex and tight regulation mechanisms, which allow the molecule to fine-tune its different functions: from transcriptional regulation to the expression of different isoforms, and from the interaction with regulatory proteins to an ingenious post-translational cleavage mechanism generating various active fragments with specific functions. Further studies still need to be carried out to provide answers to many unresolved issues and to reconcile conflicting results. This review aims at providing an overview of the current PIDD knowledge status. Cell Death and Differentiation (2012) 19, 13–20; doi:10.1038/cdd.2011.162; published online 18 November 2011 Facts Is PIDD involved at all in caspase-2 activation (which is distinct from processing) in vivo? Are both proteins P53-induced protein with a death domain (PIDD) has operating in the same pathway or acting independently of been identified as a p53-inducible molecule implicated in each other? p53-dependent apoptosis.
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The Genetics of Bipolar Disorder
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