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Caspase-8 (CASP-8) (EC 3.4.22.61) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]

 CASP8_RAT               Reviewed;         482 AA.
Q9JHX4;
01-APR-2015, integrated into UniProtKB/Swiss-Prot.
01-OCT-2000, sequence version 1.
03-JUL-2019, entry version 144.
RecName: Full=Caspase-8 {ECO:0000303|Ref.2, ECO:0000305};
Short=CASP-8;
EC=3.4.22.61;
Contains:
RecName: Full=Caspase-8 subunit p18;
Contains:
RecName: Full=Caspase-8 subunit p10;
Flags: Precursor;
Name=Casp8 {ECO:0000312|RGD:620945};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley;
Itoh T., Itoh A., Pleasure D.;
Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=Sprague-Dawley; TISSUE=Cerebellum;
Cao G., Graham S.H., Chen D., Chen J.;
"Molecular cloning and characterization of rat caspase-8: Its
implication in delayed neuronal cell death after ischemia.";
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
PubMed=15057822; DOI=10.1038/nature02426;
Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T.,
Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A.,
Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M.,
Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K.,
Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S.,
Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J.,
Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y.,
Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A.,
Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J.,
D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R.,
Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A.,
Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E.,
Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E.,
Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D.,
Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M.,
Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O.,
Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O.,
Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H.,
Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S.,
Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J.,
Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E.,
Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F.,
Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K.,
Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S.,
Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M.,
Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M.,
Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A.,
Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S.,
Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G.,
Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H.,
Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R.,
Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M.,
Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H.,
Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S.,
Collins F.S.;
"Genome sequence of the Brown Norway rat yields insights into
mammalian evolution.";
Nature 428:493-521(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Brown Norway;
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
INTERACTION WITH NOL3.
PubMed=15383280; DOI=10.1016/j.molcel.2004.08.020;
Nam Y.J., Mani K., Ashton A.W., Peng C.F., Krishnamurthy B.,
Hayakawa Y., Lee P., Korsmeyer S.J., Kitsis R.N.;
"Inhibition of both the extrinsic and intrinsic death pathways through
nonhomotypic death-fold interactions.";
Mol. Cell 15:901-912(2004).
[6]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: Most upstream protease of the activation cascade of
caspases responsible for the TNFRSF6/FAS mediated and TNFRSF1A
induced cell death. Binding to the adapter molecule FADD recruits
it to either receptor. The resulting aggregate called death-
inducing signaling complex (DISC) performs CASP8 proteolytic
activation. The active dimeric enzyme is then liberated from the
DISC and free to activate downstream apoptotic proteases.
Proteolytic fragments of the N-terminal propeptide (termed CAP3,
CAP5 and CAP6) are likely retained in the DISC. Cleaves and
activates CASP3, CASP4, CASP6, CASP7, CASP9 and CASP10. May
participate in the GZMB apoptotic pathways. Cleaves ADPRT.
Hydrolyzes the small-molecule substrate, Ac-Asp-Glu-Val-Asp-|-AMC.
Likely target for the cowpox virus CRMA death inhibitory protein.
{ECO:0000250|UniProtKB:O89110}.
-!- 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;
Evidence={ECO:0000250|UniProtKB:O89110};
-!- ACTIVITY REGULATION: Inhibited by CRMA and P35.
{ECO:0000250|UniProtKB:O89110}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 18 kDa (p18) and a 10
kDa (p10) subunit (By similarity). Interacts with FADD, CFLAR and
PEA15 (By similarity). Interacts with RFFL and RNF34; negatively
regulate CASP8 through proteasomal degradation (By similarity).
Interacts with TNFAIP8L2 (By similarity). Interacts with CASP8AP2
(By similarity). Interacts with NOL3; decreases CASP8 activity in
a mitochondria localization- and phosphorylation-dependent manner
and this interaction is dissociated by calcium (PubMed:15383280).
Interacts with UBR2 (By similarity).
{ECO:0000250|UniProtKB:O89110, ECO:0000250|UniProtKB:Q14790,
ECO:0000269|PubMed:15383280}.
-!- INTERACTION:
Q8R2E7:Fadd; NbExp=2; IntAct=EBI-4326675, EBI-4326723;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- PTM: Generation of the subunits requires association with the
death-inducing signaling complex (DISC), whereas additional
processing is likely due to the autocatalytic activity of the
activated protease. GZMB and CASP10 can be involved in these
processing events (By similarity). {ECO:0000250|UniProtKB:Q14790}.
-!- PTM: Phosphorylation on Ser-389 during mitosis by CDK1 inhibits
activation by proteolysis and prevents apoptosis. This
phosphorylation occurs in cancer cell lines, as well as in primary
breast tissues and lymphocytes (By similarity).
{ECO:0000250|UniProtKB:Q14790}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
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EMBL; AF279308; AAF87778.1; -; mRNA.
EMBL; AF288372; AAK83055.1; -; mRNA.
EMBL; AABR06060567; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AABR06060568; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH473965; EDL98978.1; -; Genomic_DNA.
EMBL; CH473965; EDL98979.1; -; Genomic_DNA.
RefSeq; NP_071613.1; NM_022277.1.
RefSeq; XP_006245077.1; XM_006245015.3.
SMR; Q9JHX4; -.
IntAct; Q9JHX4; 2.
STRING; 10116.ENSRNOP00000016613; -.
MEROPS; C14.009; -.
iPTMnet; Q9JHX4; -.
PhosphoSitePlus; Q9JHX4; -.
PaxDb; Q9JHX4; -.
PRIDE; Q9JHX4; -.
Ensembl; ENSRNOT00000016613; ENSRNOP00000016613; ENSRNOG00000012331.
Ensembl; ENSRNOT00000084498; ENSRNOP00000069982; ENSRNOG00000012331.
GeneID; 64044; -.
KEGG; rno:64044; -.
UCSC; RGD:620945; rat.
CTD; 841; -.
RGD; 620945; Casp8.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000160319; -.
HOGENOM; HOG000276884; -.
InParanoid; Q9JHX4; -.
KO; K04398; -.
OMA; CLYNIGE; -.
OrthoDB; 939331at2759; -.
PhylomeDB; Q9JHX4; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.61; 5301.
Reactome; R-RNO-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-RNO-168638; NOD1/2 Signaling Pathway.
Reactome; R-RNO-3371378; Regulation by c-FLIP.
Reactome; R-RNO-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-RNO-5218900; CASP8 activity is inhibited.
Reactome; R-RNO-5660668; CLEC7A/inflammasome pathway.
Reactome; R-RNO-69416; Dimerization of procaspase-8.
Reactome; R-RNO-75108; Activation, myristolyation of BID and translocation to mitochondria.
Reactome; R-RNO-75153; Apoptotic execution phase.
Reactome; R-RNO-75157; FasL/ CD95L signaling.
Reactome; R-RNO-75158; TRAIL signaling.
PRO; PR:Q9JHX4; -.
Proteomes; UP000002494; Chromosome 9.
Bgee; ENSRNOG00000012331; Expressed in 10 organ(s), highest expression level in colon.
Genevisible; Q9JHX4; RN.
GO; GO:0031265; C:CD95 death-inducing signaling complex; IDA:RGD.
GO; GO:0044297; C:cell body; IDA:RGD.
GO; GO:0005737; C:cytoplasm; IDA:RGD.
GO; GO:0005829; C:cytosol; IDA:RGD.
GO; GO:0031264; C:death-inducing signaling complex; IDA:RGD.
GO; GO:0045121; C:membrane raft; IDA:RGD.
GO; GO:0043005; C:neuron projection; IDA:RGD.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:RGD.
GO; GO:0032991; C:protein-containing complex; IDA:RGD.
GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:RGD.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; ISS:UniProtKB.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; IBA:GO_Central.
GO; GO:0035877; F:death effector domain binding; IBA:GO_Central.
GO; GO:0005123; F:death receptor binding; IPI:RGD.
GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005164; F:tumor necrosis factor receptor binding; IPI:RGD.
GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; IEA:Ensembl.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0006915; P:apoptotic process; IMP:RGD.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEA:Ensembl.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IBA:GO_Central.
GO; GO:0030225; P:macrophage differentiation; IBA:GO_Central.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0032731; P:positive regulation of interleukin-1 beta production; IEA:Ensembl.
GO; GO:0045651; P:positive regulation of macrophage differentiation; IEA:Ensembl.
GO; GO:1901216; P:positive regulation of neuron death; IMP:RGD.
GO; GO:0006508; P:proteolysis; IDA:RGD.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; IEA:Ensembl.
GO; GO:0046677; P:response to antibiotic; IEP:RGD.
GO; GO:0032025; P:response to cobalt ion; IEP:RGD.
GO; GO:0009409; P:response to cold; IEP:RGD.
GO; GO:0032355; P:response to estradiol; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IDA:RGD.
GO; GO:0032496; P:response to lipopolysaccharide; IEP:RGD.
GO; GO:0034612; P:response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; IEA:Ensembl.
CDD; cd00032; CASc; 1.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR001875; DED_dom.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 1.
Pfam; PF01335; DED; 2.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00115; CASc; 1.
SMART; SM00031; DED; 2.
SUPFAM; SSF47986; SSF47986; 2.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
PROSITE; PS50168; DED; 2.
1: Evidence at protein level;
Apoptosis; Complete proteome; Cytoplasm; Hydrolase; Phosphoprotein;
Protease; Reference proteome; Repeat; Thiol protease; Zymogen.
PROPEP 1 218 {ECO:0000250|UniProtKB:Q14790}.
/FTId=PRO_0000432425.
CHAIN 219 378 Caspase-8 subunit p18.
/FTId=PRO_0000432426.
PROPEP 379 388 {ECO:0000250|UniProtKB:Q14790}.
/FTId=PRO_0000432427.
CHAIN 389 482 Caspase-8 subunit p10.
/FTId=PRO_0000432428.
DOMAIN 2 80 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 100 177 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 319 319 {ECO:0000250|UniProtKB:Q14790}.
ACT_SITE 362 362 {ECO:0000250|UniProtKB:Q14790}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000250|UniProtKB:O89110}.
MOD_RES 336 336 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14790}.
MOD_RES 390 390 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q14790}.
SEQUENCE 482 AA; 55339 MW; 82B4A29330C53264 CRC64;
MDFHSCLYDI AERLGNEELA ALKFLCLDHI PQKKQESIND VLVLFQRLQE EGMLEEDNLS
FLKELLFHIS RRDLLSRVLK SSPEEMVREL QVLGKAQVSA YRVMLFKLSE DMDKEDLKSF
KFLLITEIPK CKLQDNSSLL DIFVEMEKRT ILAENNLVTL KSICFRVNRS LLGRIDDYER
SSTERRMSTE GGEELPVSVL DEVTIKMQDM WDSPGEQESE SLNSDNVYQM KSKPRGYCLI
FNNNNFSKAR EDIPKLSNMR DRKGTNYDEE ALSKTFKELH FEIVSFSDCT ASQIHEVLVS
YQSKDHKGKD CFICCILSHG DKGIVYGTDG KEASIYELTS YFTGSKCPSL AGKPKIFFIQ
ACQGNNFQKA VPVPDETGLE QEHVLEEDSS SYKNYIPDEA DFLLGMATVK NCVSYRDPTR
GTWYIQSLCQ SLRERCPRGE DILSILTGVN YDVSNKDNPR NMGKQMPQPI FTLRKKLFFP
PN


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WP88: Toll Like Receptor signaling
WP1965: VEGF-receptor Signal Transduction
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP1680: Oxidative phosphorylation
WP1711: Trinitrotoluene degradation
WP2272: Pathogenic Escherichia coli infection
WP1626: Benzoate degradation via CoA ligation
WP1655: Geraniol degradation
WP1672: Mismatch repair
WP1694: Pyrimidine metabolism
WP1614: 1- and 2-Methylnaphthalene degradation
WP1644: DNA replication
WP1671: Methane metabolism
WP1693: Purine metabolism
WP1718: Vitamin B6 metabolism
WP2292: Chemokine signaling pathway
WP1566: Citrate cycle (TCA cycle)
WP1634: Butanoate metabolism
WP1663: Homologous recombination

Related Genes :
[CASP8 MCH5] Caspase-8 (CASP-8) (EC 3.4.22.61) (Apoptotic cysteine protease) (Apoptotic protease Mch-5) (CAP4) (FADD-homologous ICE/ced-3-like protease) (FADD-like ICE) (FLICE) (ICE-like apoptotic protease 5) (MORT1-associated ced-3 homolog) (MACH) [Cleaved into: Caspase-8 subunit p18; Caspase-8 subunit p10]
[CASP14] Caspase-14 (CASP-14) (EC 3.4.22.-) [Cleaved into: Caspase-14 subunit p17, mature form; Caspase-14 subunit p10, mature form; Caspase-14 subunit p20, intermediate form; Caspase-14 subunit p8, intermediate form]
[Casp2 Ich1 Nedd-2 Nedd2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Dredd DCP2 CG7486] Caspase-8 (EC 3.4.22.61) (Death-related ced-3/NEDD2-like protein) [Cleaved into: Caspase-8 subunit p15; Caspase-8 subunit p10]
[Casp6] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP6 MCH2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[Casp4 Casp11 Caspl Ich3] Caspase-4 (CASP-4) (EC 3.4.22.64) (Caspase-11) (CASP-11) (Protease ICH-3) [Cleaved into: Caspase-4 subunit p10; Caspase-4 subunit p20]
[Casp6 Mch2] Caspase-6 (CASP-6) (EC 3.4.22.59) (Apoptotic protease Mch-2) [Cleaved into: Caspase-6 subunit p18; Caspase-6 subunit p11]
[CASP2 ICH1 NEDD2] Caspase-2 (CASP-2) (EC 3.4.22.55) (Neural precursor cell expressed developmentally down-regulated protein 2) (NEDD-2) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[Casp2 Ich1] Caspase-2 (CASP-2) (EC 3.4.22.55) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]
[CFLAR CASH CASP8AP1 CLARP MRIT] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP10 MCH4] Caspase-10 (CASP-10) (EC 3.4.22.63) (Apoptotic protease Mch-4) (FAS-associated death domain protein interleukin-1B-converting enzyme 2) (FLICE2) (ICE-like apoptotic protease 4) [Cleaved into: Caspase-10 subunit p23/17; Caspase-10 subunit p12]
[CASP3 CPP32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP7 MCH3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (CMH-1) (ICE-like apoptotic protease 3) (ICE-LAP3) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP4 ICH2] Caspase-4 (CASP-4) (EC 3.4.22.57) (ICE and Ced-3 homolog 2) (ICH-2) (ICE(rel)-II) (Mih1) (Protease TX) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[Casp7 Lice2 Mch3] Caspase-7 (CASP-7) (EC 3.4.22.60) (Apoptotic protease Mch-3) (Cysteine protease LICE2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[Casp3 Cpp32] Caspase-3 (CASP-3) (EC 3.4.22.56) (Apopain) (Cysteine protease CPP32) (CPP-32) (IRP) (LICE) (Protein Yama) (SREBP cleavage activity 1) (SCA-1) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[Cflar Cash] CASP8 and FADD-like apoptosis regulator (Caspase homolog) (CASH) (Caspase-eight-related protein) (Casper) (Caspase-like apoptosis regulatory protein) (CLARP) (Cellular FLICE-like inhibitory protein) (c-FLIP) (FADD-like antiapoptotic molecule 1) (FLAME-1) (Inhibitor of FLICE) (I-FLICE) (MACH-related inducer of toxicity) (MRIT) (Usurpin) [Cleaved into: CASP8 and FADD-like apoptosis regulator subunit p43; CASP8 and FADD-like apoptosis regulator subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[tat] Protein Tat (Transactivating regulatory protein)
[rep 1a-1b] Replicase polyprotein 1ab (pp1ab) (ORF1ab polyprotein) [Cleaved into: Non-structural protein 2 (nsp2) (p87); Non-structural protein 3 (nsp3) (EC 3.4.22.-) (Papain-like proteinase) (PL-PRO) (p195); Non-structural protein 4 (nsp4) (Peptide HD2) (p41); 3C-like proteinase (3CL-PRO) (3CLp) (EC 3.4.22.-) (M-PRO) (nsp5) (p33); Non-structural protein 6 (nsp6) (p34); Non-structural protein 7 (nsp7) (p9); Non-structural protein 8 (nsp8) (p24); Non-structural protein 9 (nsp9) (p10); Non-structural protein 10 (nsp10) (Growth factor-like peptide) (GFL) (p16); RNA-directed RNA polymerase (Pol) (RdRp) (EC 2.7.7.48) (nsp12) (p100); Helicase (Hel) (EC 3.6.4.12) (EC 3.6.4.13) (nsp13) (p68); Exoribonuclease (ExoN) (EC 3.1.13.-) (nsp14) (p58); Uridylate-specific endoribonuclease (EC 3.1.-.-) (NendoU) (nsp15) (p39); Putative 2'-O-methyl transferase (EC 2.1.1.-) (nsp16) (p35)]
[Drice ICE CG7788] Caspase (EC 3.4.22.-) (drICE) [Cleaved into: Caspase subunit p21; Caspase subunit p12]
[AMC4 AMC7 MCP2D At1g79340 YUP8H12R.4] Metacaspase-4 (AtMC4) (EC 3.4.22.-) (Metacaspase 2d) (AtMCP2d) (Metacaspase-7) [Cleaved into: Metacaspase-4 subunit p20; Metacaspase-4 subunit p10]
[env] Envelope glycoprotein gp160 (Env polyprotein) [Cleaved into: Surface protein gp120 (SU) (Glycoprotein 120) (gp120); Transmembrane protein gp41 (TM) (Glycoprotein 41) (gp41)]
[CASP4] Caspase-4 (CASP-4) (EC 3.4.22.57) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[ced-3 C48D1.2] Cell death protein 3 (EC 3.4.22.60) (Caspase ced-3) [Cleaved into: Cell death protein 3 subunit p17; Cell death protein 3 subunit p15; Cell death protein 3 subunit p13]
[CASP2 ICH1] Caspase-2 (CASP-2) (EC 3.4.22.55) (ICH-1L/1S) (Protease ICH-1) [Cleaved into: Caspase-2 subunit p18; Caspase-2 subunit p13; Caspase-2 subunit p12]

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