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Death-associated inhibitor of apoptosis 2 (EC 6.3.2.-) (Apoptosis 2 inhibitor) (IAP homolog A) (IAP-like protein) (ILP) (dILP) (Inhibitor of apoptosis 2)

 DIAP2_DROME             Reviewed;         498 AA.
Q24307; A4UZI4; Q24115; Q24149; Q24177; Q960U3; Q9V7G1;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
02-SEP-2008, sequence version 3.
27-SEP-2017, entry version 158.
RecName: Full=Death-associated inhibitor of apoptosis 2;
EC=6.3.2.-;
AltName: Full=Apoptosis 2 inhibitor;
AltName: Full=IAP homolog A;
AltName: Full=IAP-like protein;
Short=ILP;
Short=dILP;
AltName: Full=Inhibitor of apoptosis 2;
Name=Diap2; Synonyms=DIHA, Iap2, Ilp; ORFNames=CG8293;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
TISSUE=Eye imaginal disk;
PubMed=8548811; DOI=10.1016/0092-8674(95)90150-7;
Hay B.A., Wassarman D.A., Rubin G.M.;
"Drosophila homologs of baculovirus inhibitor of apoptosis proteins
function to block cell death.";
Cell 83:1253-1262(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Embryo;
PubMed=8552191; DOI=10.1038/379349a0;
Liston P., Roy N., Tamai K., Lefebvre C., Baird S., Cherton-Horvat G.,
Farahani R., McLean M., Ikeda J., Mackenzie A., Korneluk R.G.;
"Suppression of apoptosis in mammalian cells by NAIP and a related
family of IAP genes.";
Nature 379:349-353(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
STRAIN=Canton-S;
PubMed=8654366;
Duckett C.S., Nava V.E., Gedrich R.W., Clem R.J., van Dongen J.L.,
Gilfillan M.C., Shiels H., Hardwick J.M., Thompson C.B.;
"A conserved family of cellular genes related to the baculovirus iap
gene and encoding apoptosis inhibitors.";
EMBO J. 15:2685-2694(1996).
[4]
NUCLEOTIDE SEQUENCE.
STRAIN=Canton-S;
Ross J.L.;
Thesis (1991), Vanderbilt University / Nashville, United States.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley;
PubMed=10731132; DOI=10.1126/science.287.5461.2185;
Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X.,
Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D.,
Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G.,
Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D.,
Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M.,
Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S.,
Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P.,
Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I.,
Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P.,
de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M.,
Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P.,
Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W.,
Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K.,
Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J.,
Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C.,
Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A.,
Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z.,
Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X.,
Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D.,
Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A.,
Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L.,
Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M.,
Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G.,
Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H.,
Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
Spier E., Spradling A.C., Stapleton M., Strong R., Sun E.,
Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X.,
Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J.,
Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A.,
Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L.,
Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X.,
Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.;
"The genome sequence of Drosophila melanogaster.";
Science 287:2185-2195(2000).
[6]
GENOME REANNOTATION.
STRAIN=Berkeley;
PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q.,
Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M.,
Lewis S.E.;
"Annotation of the Drosophila melanogaster euchromatic genome: a
systematic review.";
Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Berkeley; TISSUE=Embryo;
PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M.,
George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H.,
Rubin G.M., Celniker S.E.;
"A Drosophila full-length cDNA resource.";
Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
[8]
NUCLEOTIDE SEQUENCE [MRNA] OF 17-498.
TISSUE=Larva;
PubMed=8643514; DOI=10.1073/pnas.93.10.4974;
Uren A.G., Pakusch M., Hawkins C.J., Puls K.L., Vaux D.L.;
"Cloning and expression of apoptosis inhibitory protein homologs that
function to inhibit apoptosis and/or bind tumor necrosis factor
receptor-associated factors.";
Proc. Natl. Acad. Sci. U.S.A. 93:4974-4978(1996).
[9]
INTERACTION WITH STRICA.
PubMed=11550090; DOI=10.1038/sj.cdd.4400864;
Doumanis J., Quinn L., Richardson H., Kumar S.;
"STRICA, a novel Drosophila melanogaster caspase with an unusual
serine/threonine-rich prodomain, interacts with DIAP1 and DIAP2.";
Cell Death Differ. 8:387-394(2001).
[10]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16894030; DOI=10.1128/MCB.00548-06;
Leulier F., Lhocine N., Lemaitre B., Meier P.;
"The Drosophila inhibitor of apoptosis protein DIAP2 functions in
innate immunity and is essential to resist gram-negative bacterial
infection.";
Mol. Cell. Biol. 26:7821-7831(2006).
[11]
FUNCTION, DOMAIN, INTERACTION WITH DRICE; GRIM; HID AND RPR,
DISRUPTION PHENOTYPE, CLEAVAGE, AND MUTAGENESIS OF ASP-92; ASP-100;
CYS-149; ASP-163; CYS-249 AND ASP-263.
PubMed=18166655; DOI=10.1083/jcb.200706027;
Ribeiro P.S., Kuranaga E., Tenev T., Leulier F., Miura M., Meier P.;
"DIAP2 functions as a mechanism-based regulator of drICE that
contributes to the caspase activity threshold in living cells.";
J. Cell Biol. 179:1467-1480(2007).
[12]
FUNCTION, DISRUPTION PHENOTYPE, AND INDUCTION BY GRAM-NEGATIVE
BACTERIA.
PubMed=17068333; DOI=10.1074/jbc.M608051200;
Huh J.R., Foe I., Muro I., Chen C.H., Seol J.H., Yoo S.J., Guo M.,
Park J.M., Hay B.A.;
"The Drosophila inhibitor of apoptosis (IAP) DIAP2 is dispensable for
cell survival, required for the innate immune response to gram-
negative bacterial infection, and can be negatively regulated by the
reaper/hid/grim family of IAP-binding apoptosis inducers.";
J. Biol. Chem. 282:2056-2068(2007).
[13]
REVIEW ON FUNCTION.
PubMed=19217783; DOI=10.1016/j.tcb.2009.01.004;
Broemer M., Meier P.;
"Ubiquitin-mediated regulation of apoptosis.";
Trends Cell Biol. 19:130-140(2009).
[14]
REVIEW ON FUNCTION.
PubMed=20888210; DOI=10.1016/j.ceb.2010.08.025;
Lopez J., Meier P.;
"To fight or die - inhibitor of apoptosis proteins at the crossroad of
innate immunity and death.";
Curr. Opin. Cell Biol. 22:872-881(2010).
[15]
FUNCTION, INTERACTION WITH DREDD, DOMAIN, AND MUTAGENESIS OF CYS-149;
ASP-163; CYS-249; ASP-263 AND CYS-466.
PubMed=22549468; DOI=10.1038/emboj.2012.121;
Meinander A., Runchel C., Tenev T., Chen L., Kim C.H., Ribeiro P.S.,
Broemer M., Leulier F., Zvelebil M., Silverman N., Meier P.;
"Ubiquitylation of the initiator caspase DREDD is required for innate
immune signalling.";
EMBO J. 31:2770-2783(2012).
[16]
FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL
STAGE, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=24374974; DOI=10.1002/jcp.24541;
Verma P., Tapadia M.G.;
"Epithelial immune response in Drosophila malpighian tubules:
interplay between Diap2 and ion channels.";
J. Cell. Physiol. 229:1078-1095(2014).
-!- FUNCTION: Required for activation of NF-kappaB transcription
factors in the immune deficiency (Imd) signaling cascade which is
essential for innate immune responses upon infection by Gram-
negative bacteria (PubMed:16894030, PubMed:17068333). Promotes
cytoplasmic cleavage of Rel and its translocation to the nucleus
where it drives expression of antimicrobial peptides
(PubMed:17068333, PubMed:24374974). Binds, polyubiquitinates and
activates Dredd which is required for Rel-mediated induction of
antimicrobial peptides (PubMed:22549468). Anti-apoptotic protein
which binds, ubiquitinates and inactivates the effector caspase
Drice (PubMed:18166655). Suppresses rpr and hid-dependent cell
death in the eye (PubMed:8548811). However, has also been shown to
have little, if any, role in the regulation of the canonical
caspase-dependent apoptosis pathway (PubMed:17068333). Plays a
role in regulating the expression of ion channels
(PubMed:24374974). {ECO:0000269|PubMed:16894030,
ECO:0000269|PubMed:17068333, ECO:0000269|PubMed:18166655,
ECO:0000269|PubMed:22549468, ECO:0000269|PubMed:24374974,
ECO:0000269|PubMed:8548811}.
-!- SUBUNIT: Interacts with the caspase Strica (PubMed:11550090).
Interacts (via BIR2 domain) with rpr and grim (PubMed:18166655).
Interacts (via the BIR2 and BIR3 domains) with hid
(PubMed:18166655). Interacts (via BIR3 domain) with Drice
(PubMed:18166655). Interacts with Dredd; likely to bind Dredd
simultaneously with Fadd to form a trimeric complex
(PubMed:22549468). {ECO:0000269|PubMed:11550090,
ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:22549468}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24374974}.
Cytoplasm {ECO:0000269|PubMed:24374974}.
-!- TISSUE SPECIFICITY: Expressed in both principal and stellar cells
of the Malphigian tubules. {ECO:0000269|PubMed:24374974}.
-!- DEVELOPMENTAL STAGE: Expressed in Malpighian tubules from the 3rd
instar larval stage and expression continues in pupae and adults
with highest levels in adults (at protein level).
{ECO:0000269|PubMed:24374974}.
-!- INDUCTION: Constitutively expressed (PubMed:17068333). Up-
regulated by bacterial lipopolysaccharides (LPS) in Malpighian
tubules but not in salivary glands (PubMed:24374974).
{ECO:0000269|PubMed:17068333, ECO:0000269|PubMed:24374974}.
-!- PTM: Caspase-dependent cleavage is required for suppression of
Drice-mediated cell death. {ECO:0000269|PubMed:18166655}.
-!- DISRUPTION PHENOTYPE: Normal development and viability
(PubMed:16894030, PubMed:17068333). Acute sensitivity to infection
by Gram-negative bacteria with failure to induce expression of
antibacterial peptide genes and inability to mount a proper innate
immune response (PubMed:16894030, PubMed:17068333,
PubMed:24374974). Loss of cleavage and nuclear translocation of
Rel (PubMed:17068333, PubMed:24374974). Increased activity of the
effector caspase Drice and increased apoptosis following x-ray
irradiation (PubMed:18166655). Reduced ion channel expression in
Malpighian tubules (PubMed:24374974).
{ECO:0000269|PubMed:16894030, ECO:0000269|PubMed:17068333,
ECO:0000269|PubMed:18166655, ECO:0000269|PubMed:24374974}.
-!- SIMILARITY: Belongs to the IAP family. {ECO:0000305}.
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EMBL; L49441; AAC41610.1; -; mRNA.
EMBL; U45881; AAC46988.1; -; mRNA.
EMBL; U32373; AAC47155.1; -; mRNA.
EMBL; M96581; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AE013599; AAF58095.1; -; Genomic_DNA.
EMBL; AE013599; AAO41389.1; -; Genomic_DNA.
EMBL; AY051844; AAK93268.1; -; mRNA.
EMBL; U38809; AAB08398.1; -; mRNA.
PIR; S68452; S68452.
PIR; S69545; S69545.
RefSeq; NP_477127.1; NM_057779.5.
RefSeq; NP_788362.1; NM_176182.2.
UniGene; Dm.7173; -.
ProteinModelPortal; Q24307; -.
SMR; Q24307; -.
BioGrid; 62475; 180.
IntAct; Q24307; 7.
STRING; 7227.FBpp0086432; -.
MEROPS; I32.011; -.
PaxDb; Q24307; -.
PRIDE; Q24307; -.
EnsemblMetazoa; FBtr0087296; FBpp0086431; FBgn0015247.
EnsemblMetazoa; FBtr0087297; FBpp0086432; FBgn0015247.
GeneID; 36748; -.
KEGG; dme:Dmel_CG8293; -.
UCSC; CG8293-RB; d. melanogaster.
CTD; 36748; -.
FlyBase; FBgn0015247; Diap2.
eggNOG; KOG1101; Eukaryota.
eggNOG; ENOG410YPNM; LUCA.
GeneTree; ENSGT00500000044782; -.
InParanoid; Q24307; -.
KO; K16060; -.
OMA; CSMVLAP; -.
OrthoDB; EOG091G0CXH; -.
PhylomeDB; Q24307; -.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-3769402; Deactivation of the beta-catenin transactivating complex.
Reactome; R-DME-5675482; Regulation of necroptotic cell death.
Reactome; R-DME-8948747; Regulation of PTEN localization.
Reactome; R-DME-8948751; Regulation of PTEN stability and activity.
SignaLink; Q24307; -.
GenomeRNAi; 36748; -.
PRO; PR:Q24307; -.
Proteomes; UP000000803; Chromosome 2R.
Bgee; FBgn0015247; -.
Genevisible; Q24307; DM.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:FlyBase.
GO; GO:0089720; F:caspase binding; IPI:FlyBase.
GO; GO:0043027; F:cysteine-type endopeptidase inhibitor activity involved in apoptotic process; IDA:FlyBase.
GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:FlyBase.
GO; GO:0031625; F:ubiquitin protein ligase binding; IPI:FlyBase.
GO; GO:0008270; F:zinc ion binding; ISM:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:FlyBase.
GO; GO:1990001; P:inhibition of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; IDA:FlyBase.
GO; GO:0043154; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:FlyBase.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:FlyBase.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:FlyBase.
GO; GO:0033160; P:positive regulation of protein import into nucleus, translocation; IMP:FlyBase.
GO; GO:0070936; P:protein K48-linked ubiquitination; IDA:FlyBase.
GO; GO:0070534; P:protein K63-linked ubiquitination; IDA:FlyBase.
GO; GO:0016567; P:protein ubiquitination; IDA:FlyBase.
GO; GO:0042787; P:protein ubiquitination involved in ubiquitin-dependent protein catabolic process; IMP:FlyBase.
GO; GO:0043281; P:regulation of cysteine-type endopeptidase activity involved in apoptotic process; IMP:FlyBase.
GO; GO:0009966; P:regulation of signal transduction; IBA:GO_Central.
GO; GO:0007423; P:sensory organ development; IMP:FlyBase.
CDD; cd00022; BIR; 3.
InterPro; IPR001370; BIR_rpt.
InterPro; IPR001841; Znf_RING.
Pfam; PF00653; BIR; 3.
SMART; SM00238; BIR; 3.
SMART; SM00184; RING; 1.
PROSITE; PS01282; BIR_REPEAT_1; 3.
PROSITE; PS50143; BIR_REPEAT_2; 3.
PROSITE; PS50089; ZF_RING_2; 1.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Immunity; Innate immunity;
Ligase; Metal-binding; Nucleus; Reference proteome; Repeat; Zinc;
Zinc-finger.
CHAIN 1 498 Death-associated inhibitor of apoptosis
2.
/FTId=PRO_0000122368.
REPEAT 12 77 BIR 1. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
REPEAT 116 180 BIR 2. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
REPEAT 215 280 BIR 3. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
ZN_FING 451 486 RING-type. {ECO:0000255|PROSITE-
ProRule:PRU00175}.
METAL 249 249 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 252 252 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 269 269 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
METAL 276 276 Zinc. {ECO:0000255|PROSITE-
ProRule:PRU00029}.
SITE 100 101 Cleavage; by caspases.
{ECO:0000269|PubMed:18166655}.
MUTAGEN 92 92 D->E: No effect on caspase-mediated
cleavage. {ECO:0000269|PubMed:18166655}.
MUTAGEN 100 100 D->E: Loss of caspase-mediated cleavage,
failure to protect against Drice-mediated
cell death and loss of binding to Drice.
{ECO:0000269|PubMed:18166655}.
MUTAGEN 149 149 C->G: No effect on binding to Drice or
Dredd. {ECO:0000269|PubMed:18166655,
ECO:0000269|PubMed:22549468}.
MUTAGEN 163 163 D->A: No effect on binding to Drice. Loss
of immunity to Gram-negative bacteria;
when associated with A-263.
{ECO:0000269|PubMed:18166655,
ECO:0000269|PubMed:22549468}.
MUTAGEN 249 249 C->G: Abolishes binding to Drice and
fails to inhibit cell death. No effect on
binding to Dredd.
{ECO:0000269|PubMed:18166655,
ECO:0000269|PubMed:22549468}.
MUTAGEN 263 263 D->A: Abolishes binding to Drice. Loss of
immunity to Gram-negative bacteria; when
associated with A-163.
{ECO:0000269|PubMed:18166655,
ECO:0000269|PubMed:22549468}.
MUTAGEN 466 466 C->Y: Fails to bind to Dredd and promote
its polyubiquitylation.
{ECO:0000269|PubMed:22549468}.
CONFLICT 5 5 G -> V (in Ref. 2; AAC46988).
{ECO:0000305}.
CONFLICT 40 40 N -> K (in Ref. 2; AAC46988).
{ECO:0000305}.
CONFLICT 64 65 ER -> AG (in Ref. 3; AAC47155).
{ECO:0000305}.
CONFLICT 94 94 E -> K (in Ref. 1; AAC41610).
{ECO:0000305}.
CONFLICT 282 282 A -> D (in Ref. 8; AAB08398).
{ECO:0000305}.
CONFLICT 286 286 A -> S (in Ref. 3; AAC47155).
{ECO:0000305}.
CONFLICT 302 302 Q -> P (in Ref. 1; AAC41610, 3; AAC47155
and 8; AAB08398). {ECO:0000305}.
CONFLICT 303 303 P -> T (in Ref. 8; AAB08398).
{ECO:0000305}.
CONFLICT 327 327 A -> T (in Ref. 2; AAC46988).
{ECO:0000305}.
CONFLICT 369 376 ALEVREPP -> DWRCASR (in Ref. 3;
AAC47155). {ECO:0000305}.
SEQUENCE 498 AA; 54538 MW; 0D0303DB2B26FA22 CRC64;
MTELGMELES VRLATFGEWP LNAPVSAEDL VANGFFATGN WLEAECHFCH VRIDRWEYGD
QVAERHRRSS PICSMVLAPN HCGNVPRSQE SDNEGNSVVD SPESCSCPDL LLEANRLVTF
KDWPNPNITP QALAKAGFYY LNRLDHVKCV WCNGVIAKWE KNDNAFEEHK RFFPQCPRVQ
MGPLIEFATG KNLDELGIQP TTLPLRPKYA CVDARLRTFT DWPISNIQPA SALAQAGLYY
QKIGDQVRCF HCNIGLRSWQ KEDEPWFEHA KWSPKCQFVL LAKGPAYVSE VLATTAANAS
SQPATAPAPT LQADVLMDEA PAKEALALGI DGGVVRNAIQ RKLLSSGCAF STLDELLHDI
FDDAGAGAAL EVREPPEPSA PFIEPCQATT SKAASVPIPV ADSIPAKPQA AEAVANISKI
TDEIQKMSVA TPNGNLSLEE ENRQLKDARL CKVCLDEEVG VVFLPCGHLA TCNQCAPSVA
NCPMCRADIK GFVRTFLS


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E2045h ELISA kit API4,Apoptosis inhibitor 4,Apoptosis inhibitor survivin,Baculoviral IAP repeat-containing protein 5,BIRC5,Homo sapiens,Human,IAP4 96T
E2045m ELISA kit Api4,Apoptosis inhibitor 4,Apoptosis inhibitor survivin,Baculoviral IAP repeat-containing protein 5,Birc5,Iap4,Mouse,Mus musculus,TIAP 96T
E2045m ELISA Api4,Apoptosis inhibitor 4,Apoptosis inhibitor survivin,Baculoviral IAP repeat-containing protein 5,Birc5,Iap4,Mouse,Mus musculus,TIAP 96T
E2045h ELISA API4,Apoptosis inhibitor 4,Apoptosis inhibitor survivin,Baculoviral IAP repeat-containing protein 5,BIRC5,Homo sapiens,Human,IAP4 96T
U2045h CLIA kit API4,Apoptosis inhibitor 4,Apoptosis inhibitor survivin,Baculoviral IAP repeat-containing protein 5,BIRC5,Homo sapiens,Human,IAP4 96T
18-661-15083 Baculoviral IAP repeat-containing protein 5 - Apoptosis inhibitor survivin; Apoptosis inhibitor 4 Polyclonal 0.1 mg
18-661-15082 Baculoviral IAP repeat-containing protein 5 - Apoptosis inhibitor survivin; Apoptosis inhibitor 4 Polyclonal 0.1 mg
18-661-15084 Baculoviral IAP repeat-containing protein 5 - Apoptosis inhibitor survivin; Apoptosis inhibitor 4 Polyclonal 0.1 mg
18-661-15126 Baculoviral IAP repeat-containing protein 7 - Kidney inhibitor of apoptosis protein; KIAP; Melanoma inhibitor of apoptosis protein; ML-IAP; Livin Polyclonal 0.1 mg
18-661-15131 Baculoviral IAP repeat-containing protein 8 - Inhibitor of apoptosis-like protein 2; IAP-like protein 2; ILP-2; Testis-specific inhibitor of apoptosis Polyclonal 0.1 mg
U1152c CLIA Chicken,Gallus gallus,IAP,IAP1,Inhibitor of apoptosis protein,Inhibitor of T-cell apoptosis protein,ITA 96T
E1152c ELISA Chicken,Gallus gallus,IAP,IAP1,Inhibitor of apoptosis protein,Inhibitor of T-cell apoptosis protein,ITA 96T
E1152c ELISA kit Chicken,Gallus gallus,IAP,IAP1,Inhibitor of apoptosis protein,Inhibitor of T-cell apoptosis protein,ITA 96T
18-661-15191 Baculoviral IAP repeat-containing protein 4 - Inhibitor of apoptosis protein 3; X-linked inhibitor of apoptosis protein; X-linked IAP; IAP-like protein; HILP Polyclonal 0.1 mg
20-272-190690 Livin - Mouse monoclonal [88C570] to Livin; Kidney inhibitor of apoptosis protein; KIAP; Melanoma inhibitor of apoptosis protein; ML-IAP; Livin; RING finger protein 50 Monoclonal 0.05 mg
31-015 DIABLO is an inhibitor of apoptosis protein (IAP)-binding protein. The encoded mitochondrial protein enters the cytosol when cells undergo apoptosis, and it moderates the caspase inhibition of IAPs. M 0.1 mg
EIAAB06361 Aim,Api6,Apoptosis inhibitor expressed by macrophages,Apoptosis inhibitory 6,CD5 antigen-like,Cd5l,CT-2,Mouse,Mus musculus,SP-alpha
25-190 ZMYM4 regulates apoptosis by altering mRNA turnover and CDIR inhibits apoptosis by acting as a competitive inhibitor of AUF1, preventing AUF1 from binding to its targets. 0.05 mg
EIAAB09052 Anamorsin,Ciapin1,Cytokine-induced apoptosis inhibitor 1,Fe-S cluster assembly protein DRE2 homolog,Rat,Rattus norvegicus
EIAAB09054 Anamorsin,Bos taurus,Bovine,CIAPIN1,Cytokine-induced apoptosis inhibitor 1,Fe-S cluster assembly protein DRE2 homolog
EIAAB09053 Anamorsin,Ciapin1,Cytokine-induced apoptosis inhibitor 1,Fe-S cluster assembly protein DRE2 homolog,Mouse,Mus musculus


 

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