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Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]

 CASP8_DROME             Reviewed;         494 AA.
Q8IRY7; O02433; O76797; O76798; Q95T94; Q9UB42; Q9W5E3;
07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 3.
18-SEP-2019, entry version 150.
RecName: Full=Caspase-8;
EC=3.4.22.61;
AltName: Full=Death-related ced-3/NEDD2-like protein;
Contains:
RecName: Full=Caspase-8 subunit p15;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=Dredd; Synonyms=DCP2; ORFNames=CG7486;
Drosophila melanogaster (Fruit fly).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta;
Pterygota; Neoptera; Holometabola; Diptera; Brachycera; Muscomorpha;
Ephydroidea; Drosophilidae; Drosophila; Sophophora.
NCBI_TaxID=7227;
[1] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS D; E AND ALPHA), FUNCTION,
SUBUNIT, PROTEOLYTIC CLEAVAGE, SUBCELLULAR LOCATION, AND DEVELOPMENTAL
STAGE.
TISSUE=Embryo {ECO:0000269|PubMed:9740659};
PubMed=9740659; DOI=10.1006/dbio.1998.9000;
Chen P., Rodriguez A., Erskine R., Thach T., Abrams J.M.;
"Dredd, a novel effector of the apoptosis activators reaper, grim, and
hid in Drosophila.";
Dev. Biol. 201:202-216(1998).
[2] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Berkeley {ECO:0000269|PubMed:10731132};
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).
[3] {ECO:0000305}
GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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).
[4] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Oregon-R {ECO:0000269|PubMed:10731137};
PubMed=10731137; DOI=10.1126/science.287.5461.2220;
Benos P.V., Gatt M.K., Ashburner M., Murphy L., Harris D.,
Barrell B.G., Ferraz C., Vidal S., Brun C., Demailles J., Cadieu E.,
Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Borkova D.,
Minana B., Kafatos F.C., Louis C., Siden-Kiamos I., Bolshakov S.,
Papagiannakis G., Spanos L., Cox S., Madueno E., de Pablos B.,
Modolell J., Peter A., Schoettler P., Werner M., Mourkioti F.,
Beinert N., Dowe G., Schaefer U., Jaeckle H., Bucheton A.,
Callister D.M., Campbell L.A., Darlamitsou A., Henderson N.S.,
McMillan P.J., Salles C., Tait E.A., Valenti P., Saunders R.D.C.,
Glover D.M.;
"From sequence to chromosome: the tip of the X chromosome of D.
melanogaster.";
Science 287:2220-2222(2000).
[5] {ECO:0000305}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM F).
STRAIN=Berkeley {ECO:0000269|PubMed:12537569};
TISSUE=Head {ECO:0000269|PubMed:12537569};
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).
[6] {ECO:0000305}
NUCLEOTIDE SEQUENCE [MRNA] OF 25-494 (ISOFORM E).
PubMed=9380701; DOI=10.1073/pnas.94.20.10717;
Inohara N., Koseki T., Hu Y., Chen S., Nunez G.;
"CLARP, a death effector domain-containing protein interacts with
caspase-8 and regulates apoptosis.";
Proc. Natl. Acad. Sci. U.S.A. 94:10717-10722(1997).
[7] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND MUTAGENESIS OF GLY-98 AND TRP-436.
PubMed=11269502; DOI=10.1093/embo-reports/kvd073;
Leulier F., Rodriguez A., Khush R.S., Abrams J.M., Lemaitre B.;
"The Drosophila caspase Dredd is required to resist Gram-negative
bacterial infection.";
EMBO Rep. 1:353-358(2000).
[8]
FUNCTION, INTERACTION WITH FADD, AND SUBCELLULAR LOCATION.
PubMed=10934188; DOI=10.1074/jbc.c000341200;
Hu S., Yang X.;
"dFADD, a novel death domain-containing adapter protein for the
Drosophila caspase DREDD.";
J. Biol. Chem. 275:30761-30764(2000).
[9]
FUNCTION, UBIQUITINATION, MUTAGENESIS OF GLY-98, AND INTERACTION WITH
FADD AND DIAP2.
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).
-!- FUNCTION: Effector of the programmed cell death (PCD) activators
rpr, grim and hid (PubMed:9740659). May play an apoptotic role in
the germline as well as soma. Fadd interacts with Dredd to promote
cleavage of Dredd and is necessary and sufficient for enhancing
Dredd-induced apoptosis (PubMed:10934188). Plays a role in the
innate immune response. Required for resistance to Gram-negative
bacterial infection (PubMed:11269502). Diap2-mediated
ubiquitination of Dredd is critical for processing of imd and rel
and the subsequent expression of antimicrobial genes such as DptA
(PubMed:22549468). {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:11269502, ECO:0000269|PubMed:22549468,
ECO:0000269|PubMed:9740659}.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for Asp at position P1 and has a
preferred cleavage sequence of (Leu/Asp/Val)-Glu-Thr-Asp-|-
(Gly/Ser/Ala).; EC=3.4.22.61;
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 15 kDa (caspase-8
subunit p15) and a 10 kDa (caspase-8 subunit p10) subunit
(PubMed:9740659). Interacts (via N-terminus) with Diap2; likely to
bind Diap2 simultaneously with Fadd to form a trimeric complex
(PubMed:10934188, PubMed:22549468). {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:22549468, ECO:0000269|PubMed:9740659}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10934188,
ECO:0000269|PubMed:9740659}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=E; Synonyms=Caspase-8 delta;
IsoId=Q8IRY7-1; Sequence=Displayed;
Name=D; Synonyms=Caspase-8 gamma;
IsoId=Q8IRY7-2; Sequence=VSP_050749;
Name=F;
IsoId=Q8IRY7-3; Sequence=VSP_050750, VSP_050751;
Name=alpha {ECO:0000269|PubMed:9740659};
IsoId=Q8IRY7-4; Sequence=VSP_050748;
-!- TISSUE SPECIFICITY: Constitutively expressed in fat bodies of
larvae and adults. {ECO:0000269|PubMed:11269502}.
-!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
Embryos exhibit ubiquitous low level of expression until stage 11
and then expression becomes spatially and temporally restricted to
areas of PCD. {ECO:0000269|PubMed:9740659}.
-!- PTM: Polyubiquitinated by Diap2 following activation of the immune
deficiency (Imd) pathway. {ECO:0000269|PubMed:22549468}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAL25314.1; Type=Erroneous initiation; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AF007016; AAC31214.1; -; mRNA.
EMBL; AF083894; AAC33117.1; -; mRNA.
EMBL; AF083895; AAC33118.1; -; mRNA.
EMBL; AE014298; AAF45533.3; -; Genomic_DNA.
EMBL; AE014298; AAN09022.2; -; Genomic_DNA.
EMBL; AE014298; AAN09023.2; -; Genomic_DNA.
EMBL; AL031581; CAA20893.1; -; Genomic_DNA.
EMBL; AY060275; AAL25314.1; ALT_INIT; mRNA.
EMBL; AF031652; AAC15843.1; -; mRNA.
PIR; T13385; T13385.
RefSeq; NP_477249.3; NM_057901.4. [Q8IRY7-1]
RefSeq; NP_477250.3; NM_057902.4. [Q8IRY7-3]
RefSeq; NP_477251.3; NM_057903.4. [Q8IRY7-2]
BioGrid; 57579; 73.
IntAct; Q8IRY7; 5.
MINT; Q8IRY7; -.
STRING; 7227.FBpp0113052; -.
MEROPS; C14.040; -.
PaxDb; Q8IRY7; -.
PRIDE; Q8IRY7; -.
EnsemblMetazoa; FBtr0114559; FBpp0113051; FBgn0020381. [Q8IRY7-2]
EnsemblMetazoa; FBtr0114560; FBpp0113052; FBgn0020381. [Q8IRY7-1]
EnsemblMetazoa; FBtr0114561; FBpp0113053; FBgn0020381. [Q8IRY7-3]
GeneID; 31011; -.
KEGG; dme:Dmel_CG7486; -.
CTD; 31011; -.
FlyBase; FBgn0020381; Dredd.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000160994; -.
InParanoid; Q8IRY7; -.
KO; K04398; -.
PhylomeDB; Q8IRY7; -.
Reactome; R-DME-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-DME-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-DME-214397; Assembly of the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214399; Activated IkappaB kinase (IKK) complex, Phospho IRD5:KEY dimer, phosphorylates REL in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214411; REL binds to DREDD in the PGN:PGRP-LC/LE receptor 'signalling complex'.
Reactome; R-DME-214416; Phosphorylated REL is cleaved by and dissociates from DREDD.
Reactome; R-DME-264870; Caspase-mediated cleavage of cytoskeletal proteins.
Reactome; R-DME-448706; Interleukin-1 processing.
Reactome; R-DME-75153; Apoptotic execution phase.
GenomeRNAi; 31011; -.
PRO; PR:Q8IRY7; -.
Proteomes; UP000000803; Chromosome X.
Bgee; FBgn0020381; Expressed in 39 organ(s), highest expression level in eye disc (Drosophila).
ExpressionAtlas; Q8IRY7; baseline and differential.
Genevisible; Q8IRY7; DM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0008656; F:cysteine-type endopeptidase activator activity involved in apoptotic process; IMP:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:FlyBase.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0004175; F:endopeptidase activity; IDA:FlyBase.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0006952; P:defense response; IMP:FlyBase.
GO; GO:0050829; P:defense response to Gram-negative bacterium; IMP:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; IBA:GO_Central.
GO; GO:0006955; P:immune response; IMP:FlyBase.
GO; GO:0045087; P:innate immune response; TAS:FlyBase.
GO; GO:0043069; P:negative regulation of programmed cell death; IMP:FlyBase.
GO; GO:0061057; P:peptidoglycan recognition protein signaling pathway; IMP:UniProtKB.
GO; GO:0048935; P:peripheral nervous system neuron development; IMP:FlyBase.
GO; GO:0006963; P:positive regulation of antibacterial peptide biosynthetic process; TAS:FlyBase.
GO; GO:0006964; P:positive regulation of biosynthetic process of antibacterial peptides active against Gram-negative bacteria; IMP:UniProtKB.
GO; GO:0002230; P:positive regulation of defense response to virus by host; IMP:FlyBase.
GO; GO:0045089; P:positive regulation of innate immune response; HMP:FlyBase.
GO; GO:0016485; P:protein processing; IDA:FlyBase.
GO; GO:0007291; P:sperm individualization; IMP:FlyBase.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Complete proteome; Cytoplasm;
Hydrolase; Immunity; Innate immunity; Protease; Reference proteome;
Thiol protease; Ubl conjugation; Zymogen.
PROPEP 1 242 {ECO:0000250}.
/FTId=PRO_0000004636.
CHAIN 243 400 Caspase-8 subunit p15.
/FTId=PRO_0000004637.
PROPEP 401 410 {ECO:0000250}.
/FTId=PRO_0000004638.
CHAIN 411 494 Caspase-8 subunit p10.
/FTId=PRO_0000004639.
ACT_SITE 345 345 {ECO:0000250}.
ACT_SITE 386 386 {ECO:0000250}.
VAR_SEQ 1 128 Missing (in isoform alpha).
{ECO:0000303|PubMed:9740659}.
/FTId=VSP_050748.
VAR_SEQ 273 278 Missing (in isoform D).
{ECO:0000303|PubMed:9740659}.
/FTId=VSP_050749.
VAR_SEQ 279 284 KFLSPD -> VSSLQY (in isoform F).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_050750.
VAR_SEQ 285 494 Missing (in isoform F).
{ECO:0000303|PubMed:12537569}.
/FTId=VSP_050751.
MUTAGEN 98 98 G->R: In D44; reduces polyubiquitination
by Diap2, abolishes rel cleavage and
blocks expression of DptA following
bacterial infection. No effect on binding
to Diap2 or Fadd, processing,
dimerization, catalytic activity or
stability. {ECO:0000269|PubMed:11269502,
ECO:0000269|PubMed:22549468}.
MUTAGEN 436 436 W->R: In L23; blocks expression of DptA
following bacterial infection.
{ECO:0000269|PubMed:11269502}.
CONFLICT 481 481 K -> N (in Ref. 1; AAC33117/AAC33118).
{ECO:0000305}.
SEQUENCE 494 AA; 56153 MW; B9730DB3FDC58D4C CRC64;
MAGSNLLIHL DTIDQNDLIY VERDMNFAQK VGLCFLLYGD DHSDATYILQ KLLAMTRSDF
PQSDLLIKFA KSRPETWRRH LVEALCIIGA RKVLRRLGFC WQELRMHYLP HIAGITLHVH
PLLKSLYRMC EELSLVQSGR LLLDVREKVE SQQAGDPLRF YDPAYLEIFL LDWLTRRSIK
LGDINAAGSD VQLLVGHLKS NGLQAQANLL KDTIISNAPE PDAAGTAAMA VKQEIESDNQ
QSYCSTQIDA LKLTRENAGI ALIINQQKFH RNVSRDNMKF LSPDPLRRRD GTDVDKERLI
EVFSSMGYNV EAYDNVDHMG IIERIRSACD RSLVRDSLVV FILSHGFEEA VYASNSIAMK
ITDIEDLLCS YDTLYYKPKL LIIQACQEKL VHKKKPNELF RIDVTTVSPD QHIDMLRAMS
TVNGYAALRH TQTGSWFIGS LCDAIDRRSA SEHIADILTI VTNEVSKKRG SNDESMVPNV
KSTFRQHVYF PPRL


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E1058m ELISA kit CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Mouse,Mus musculus 96T
E1058r ELISA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Rat,Rattus norvegicus 96T
U1058r CLIA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Rat,Rattus norvegicus 96T
U1058m CLIA CAD,Cad,Caspase-activated deoxyribonuclease,Caspase-activated DNase,DFF-40,Dffb,DNA fragmentation factor 40 kDa subunit,DNA fragmentation factor subunit beta,Mouse,Mus musculus 96T
18-783-76408 RABBIT ANTI MOUSE CAD (aa314-329) - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD Polyclonal 0.1 mg
18-783-76333 RABBIT ANTI MOUSE CAD (aa205-222) - EC 3.-.-.-; DNA fragmentation factor 40 kDa subunit; DFF-40; Caspase-activated deoxyribonuclease; Caspase-activated DNase; CAD Polyclonal 0.1 mg
18-661-15024 CASP8 and FADD-like apoptosis regulator - Cellular FLICE-like inhibitory protein; c-FLIP; Caspase-eight-related protein; Casper; Caspase-like apoptosis regulatory protein; CLARP; MACH-related inducer 0.1 mg
18-003-42865 CASP8 and FADD-like apoptosis regulator - Cellular FLICE-like inhibitory protein; c-FLIP; Caspase-eight-related protein; Casper; Caspase-like apoptosis regulatory protein; CLARP; MACH-related inducer 0.1 mg Protein A
Pathways :
WP2272: Pathogenic Escherichia coli infection
WP1694: Pyrimidine metabolism
WP1566: Citrate cycle (TCA cycle)
WP2292: Chemokine signaling pathway
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1965: VEGF-receptor Signal Transduction
WP1693: Purine metabolism
WP1663: Homologous recombination
WP88: Toll Like Receptor signaling
WP1672: Mismatch repair
WP1644: DNA replication
WP1680: Oxidative phosphorylation
WP1634: Butanoate metabolism
WP731: Sterol regulatory element binding protein related
WP1626: Benzoate degradation via CoA ligation
WP2199: Seed Development
WP1711: Trinitrotoluene degradation
WP1614: 1- and 2-Methylnaphthalene degradation
WP1718: Vitamin B6 metabolism
WP1655: Geraniol degradation
WP1671: Methane metabolism
WP1937: Transport of vitamins, nucleosides, and related molecules
WP1049: G Protein Signaling Pathways
WP2371: Parkinsons Disease Pathway
WP367: Programmed Cell Death

Related Genes :
[psbX] Photosystem II reaction center X protein
[ndhA] NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1)
[KK1_045969] 40S ribosomal protein SA
[KK1_006657] Uncharacterized protein
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[KK1_031928] Tyrosine N-monooxygenase
[] UDP-glycosyltransferase homolog (Fragment)
[ndhA] NAD(P)H-quinone oxidoreductase subunit 1, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 1) (NDH subunit 1) (NADH-plastoquinone oxidoreductase subunit 1)
[KK1_005898] Secologanin synthase
[ndhD] NAD(P)H-quinone oxidoreductase chain 4, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase, chain 4) (NADH-plastoquinone oxidoreductase chain 4)
[psbH] Photosystem II reaction center protein H (PSII-H)
[KK1_044146] Uncharacterized protein
[petB] Cytochrome b6
[ARD1] 1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase (EC 1.13.11.54) (Acireductone dioxygenase (Fe(2+)-requiring)) (ARD) (Fe-ARD)
[COB] Cytochrome b (Fragment)
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5)
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[atpF] ATP synthase subunit b, chloroplastic (ATP synthase F(0) sector subunit b) (ATPase subunit I)
[malate dehydrogenase] Malate dehydrogenase
[ndhE] NAD(P)H-quinone oxidoreductase subunit 4L, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit 4L) (NADH-plastoquinone oxidoreductase subunit 4L)
[g.33360] 4-alpha-glucanotransferase (EC 2.4.1.25) (Amylomaltase) (Disproportionating enzyme) (Fragment)
[ndhI] NAD(P)H-quinone oxidoreductase subunit I, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit I) (NDH subunit I) (NADH-plastoquinone oxidoreductase subunit I)
[ndhK] NAD(P)H-quinone oxidoreductase subunit K, chloroplastic (EC 7.1.1.-) (NAD(P)H dehydrogenase subunit K) (NADH-plastoquinone oxidoreductase subunit K)
[psbA] Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein)
[LOC101502735] Lipoxygenase (EC 1.13.11.-)
[AM588_10001736] Uncharacterized protein
[ndhF] NAD(P)H-quinone oxidoreductase subunit 5, chloroplastic (EC 7.1.1.-) (NADH-plastoquinone oxidoreductase subunit 5) (Fragment)
[LOC101491357] cytochrome P450 734A1-like isoform X1
[psbI] Photosystem II reaction center protein I (PSII-I) (PSII 4.8 kDa protein)
[petB] Cytochrome b6

Bibliography :