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

 CASP8_MOUSE             Reviewed;         480 AA.
O89110; O35669;
15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1998, sequence version 1.
13-FEB-2019, entry version 175.
RecName: Full=Caspase-8;
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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND CHARACTERIZATION.
STRAIN=129/SvJ;
PubMed=9654089; DOI=10.1046/j.1432-1327.1998.2530399.x;
Sakamaki K., Tsukumo S., Yonehara S.;
"Molecular cloning and characterization of mouse caspase-8.";
Eur. J. Biochem. 253:399-405(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA], CHARACTERIZATION, AND ACTIVITY REGULATION.
PubMed=9837723; DOI=10.1006/jmbi.1998.2226;
Van de Craen M., Van Loo G., Declercq W., Schotte P.,
van den Brande I., Mandruzzato S., van der Bruggen P., Fiers W.,
Vandenabeele P.;
"Molecular cloning and identification of murine caspase-8.";
J. Mol. Biol. 284:1017-1026(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N; TISSUE=Colon, and Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 57-476.
Kioschis P., Kischkel F., Poustka A., Krammer P.;
Submitted (JUL-1997) 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]
INTERACTION WITH CASP8AP2.
PubMed=17245429; DOI=10.1038/sj.emboj.7601504;
Milovic-Holm K., Krieghoff E., Jensen K., Will H., Hofmann T.G.;
"FLASH links the CD95 signaling pathway to the cell nucleus and
nuclear bodies.";
EMBO J. 26:391-401(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[8]
INTERACTION WITH TNFAIP8L2.
PubMed=18455983; DOI=10.1016/j.cell.2008.03.026;
Sun H., Gong S., Carmody R.J., Hilliard A., Li L., Sun J., Kong L.,
Xu L., Hilliard B., Hu S., Shen H., Yang X., Chen Y.H.;
"TIPE2, a negative regulator of innate and adaptive immunity that
maintains immune homeostasis.";
Cell 133:415-426(2008).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=19131326; DOI=10.1074/mcp.M800451-MCP200;
Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
"Large scale localization of protein phosphorylation by use of
electron capture dissociation mass spectrometry.";
Mol. Cell. Proteomics 8:904-912(2009).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-188 AND SER-213, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brown adipose tissue, Kidney, Liver, Lung, Pancreas, and
Spleen;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-226, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic fibroblast;
PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z.,
Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
"SIRT5-mediated lysine desuccinylation impacts diverse metabolic
pathways.";
Mol. Cell 50:919-930(2013).
-!- 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.
-!- 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;
-!- ACTIVITY REGULATION: Inhibited by CRMA and P35.
{ECO:0000269|PubMed:9837723}.
-!- 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 (PubMed:18455983). Interacts with
CASP8AP2 (PubMed:17245429). 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:Q14790, ECO:0000250|UniProtKB:Q9JHX4,
ECO:0000269|PubMed:15383280, ECO:0000269|PubMed:17245429,
ECO:0000269|PubMed:18455983}.
-!- INTERACTION:
P19091:Ar; NbExp=2; IntAct=EBI-851690, EBI-1776062;
Q61160:Fadd; NbExp=6; IntAct=EBI-851690, EBI-524415;
P25446:Fas; NbExp=3; IntAct=EBI-851690, EBI-296206;
P01375:TNF (xeno); NbExp=2; IntAct=EBI-851690, EBI-359977;
Q9D8Y7:Tnfaip8l2; NbExp=2; IntAct=EBI-851690, EBI-1781612;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- TISSUE SPECIFICITY: Expressed in a wide variety of tissues.
Highest expression in spleen, thymus, lung, liver and kidney.
Lower expression in heart, brain, testis and skeletal muscle.
-!- DEVELOPMENTAL STAGE: In the embryo, highest expression occurs at
day 7.
-!- 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}.
-!- 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}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF067841; AAC40132.1; -; Genomic_DNA.
EMBL; AF067835; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067836; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067837; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067838; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067839; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067840; AAC40132.1; JOINED; Genomic_DNA.
EMBL; AF067834; AAC40131.1; -; mRNA.
EMBL; AJ007749; CAA07677.1; -; mRNA.
EMBL; BC006737; AAH06737.1; -; mRNA.
EMBL; BC049955; AAH49955.1; -; mRNA.
EMBL; AJ000641; CAA04196.1; -; mRNA.
CCDS; CCDS14979.1; -.
RefSeq; NP_001073595.1; NM_001080126.1.
RefSeq; NP_033942.1; NM_009812.2.
UniGene; Mm.336851; -.
ProteinModelPortal; O89110; -.
SMR; O89110; -.
BioGrid; 198500; 6.
ComplexPortal; CPX-1914; Ripoptosome.
ComplexPortal; CPX-3663; Caspase-8 complex.
DIP; DIP-37435N; -.
IntAct; O89110; 8.
MINT; O89110; -.
STRING; 10090.ENSMUSP00000027189; -.
MEROPS; C14.009; -.
iPTMnet; O89110; -.
PhosphoSitePlus; O89110; -.
EPD; O89110; -.
jPOST; O89110; -.
PaxDb; O89110; -.
PeptideAtlas; O89110; -.
PRIDE; O89110; -.
Ensembl; ENSMUST00000027189; ENSMUSP00000027189; ENSMUSG00000026029.
Ensembl; ENSMUST00000165549; ENSMUSP00000127375; ENSMUSG00000026029.
GeneID; 12370; -.
KEGG; mmu:12370; -.
UCSC; uc007bcs.1; mouse.
CTD; 841; -.
MGI; MGI:1261423; Casp8.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000160319; -.
HOGENOM; HOG000276884; -.
HOVERGEN; HBG050803; -.
InParanoid; O89110; -.
KO; K04398; -.
OMA; RVMLFQI; -.
OrthoDB; 939331at2759; -.
PhylomeDB; O89110; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.61; 3474.
Reactome; R-MMU-111465; Apoptotic cleavage of cellular proteins.
Reactome; R-MMU-140534; Caspase activation via Death Receptors in the presence of ligand.
Reactome; R-MMU-168638; NOD1/2 Signaling Pathway.
Reactome; R-MMU-2562578; TRIF-mediated programmed cell death.
Reactome; R-MMU-3371378; Regulation by c-FLIP.
Reactome; R-MMU-5213460; RIPK1-mediated regulated necrosis.
Reactome; R-MMU-5218900; CASP8 activity is inhibited.
Reactome; R-MMU-5660668; CLEC7A/inflammasome pathway.
Reactome; R-MMU-69416; Dimerization of procaspase-8.
Reactome; R-MMU-75108; Activation, myristolyation of BID and translocation to mitochondria.
Reactome; R-MMU-75153; Apoptotic execution phase.
Reactome; R-MMU-75157; FasL/ CD95L signaling.
Reactome; R-MMU-75158; TRAIL signaling.
PRO; PR:O89110; -.
Proteomes; UP000000589; Chromosome 1.
Bgee; ENSMUSG00000026029; Expressed in 249 organ(s), highest expression level in jejunum.
ExpressionAtlas; O89110; baseline and differential.
Genevisible; O89110; MM.
GO; GO:0031265; C:CD95 death-inducing signaling complex; ISO:MGI.
GO; GO:0044297; C:cell body; ISO:MGI.
GO; GO:0005737; C:cytoplasm; IDA:ParkinsonsUK-UCL.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031264; C:death-inducing signaling complex; ISO:MGI.
GO; GO:0045121; C:membrane raft; ISO:MGI.
GO; GO:0005739; C:mitochondrion; HDA:MGI.
GO; GO:0043005; C:neuron projection; ISO:MGI.
GO; GO:0030690; C:Noc1p-Noc2p complex; IMP:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0005886; C:plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0032991; C:protein-containing complex; ISO:MGI.
GO; GO:0097342; C:ripoptosome; ISS:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:MGI.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0097199; F:cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
GO; GO:0035877; F:death effector domain binding; ISO:MGI.
GO; GO:0005123; F:death receptor binding; ISO:MGI.
GO; GO:0004175; F:endopeptidase activity; IDA:MGI.
GO; GO:0042802; F:identical protein binding; ISO:MGI.
GO; GO:0008233; F:peptidase activity; IDA:MGI.
GO; GO:0046982; F:protein heterodimerization activity; IPI:MGI.
GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0005164; F:tumor necrosis factor receptor binding; ISO:MGI.
GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
GO; GO:0097202; P:activation of cysteine-type endopeptidase activity; ISO:MGI.
GO; GO:0006919; P:activation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
GO; GO:0001525; P:angiogenesis; IMP:MGI.
GO; GO:0006915; P:apoptotic process; IDA:MGI.
GO; GO:0097190; P:apoptotic signaling pathway; IDA:MGI.
GO; GO:0048738; P:cardiac muscle tissue development; TAS:UniProtKB.
GO; GO:0097194; P:execution phase of apoptosis; ISS:UniProtKB.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IDA:MGI.
GO; GO:0008625; P:extrinsic apoptotic signaling pathway via death domain receptors; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0030225; P:macrophage differentiation; IMP:MGI.
GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0060546; P:negative regulation of necroptotic process; IGI:MGI.
GO; GO:0001841; P:neural tube formation; IMP:MGI.
GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
GO; GO:2001238; P:positive regulation of extrinsic apoptotic signaling pathway; IGI:MGI.
GO; GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB signaling; ISO:MGI.
GO; GO:0045651; P:positive regulation of macrophage differentiation; ISO:MGI.
GO; GO:1901216; P:positive regulation of neuron death; ISO:MGI.
GO; GO:0045862; P:positive regulation of proteolysis; ISO:MGI.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0051603; P:proteolysis involved in cellular protein catabolic process; ISO:MGI.
GO; GO:2001233; P:regulation of apoptotic signaling pathway; IGI:MGI.
GO; GO:0070243; P:regulation of thymocyte apoptotic process; IGI:MGI.
GO; GO:0045471; P:response to ethanol; ISO:MGI.
GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
GO; GO:0036462; P:TRAIL-activated apoptotic signaling pathway; ISO:MGI.
CDD; cd00032; CASc; 1.
InterPro; IPR033170; Caspase-8.
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.
PANTHER; PTHR10454:SF162; PTHR10454:SF162; 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;
Acetylation; Apoptosis; Complete proteome; Cytoplasm; Hydrolase;
Phosphoprotein; Protease; Reference proteome; Repeat; Thiol protease;
Zymogen.
PROPEP 1 218 {ECO:0000250}.
/FTId=PRO_0000004632.
CHAIN 219 376 Caspase-8 subunit p18.
/FTId=PRO_0000004633.
PROPEP 377 387 {ECO:0000250}.
/FTId=PRO_0000004634.
CHAIN 388 480 Caspase-8 subunit p10.
/FTId=PRO_0000004635.
DOMAIN 3 80 DED 1. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
DOMAIN 101 177 DED 2. {ECO:0000255|PROSITE-
ProRule:PRU00065}.
ACT_SITE 319 319 {ECO:0000250}.
ACT_SITE 362 362 {ECO:0000250}.
MOD_RES 188 188 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19131326,
ECO:0000244|PubMed:21183079}.
MOD_RES 213 213 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 226 226 N6-acetyllysine.
{ECO:0000244|PubMed:23806337}.
MOD_RES 336 336 Phosphotyrosine.
{ECO:0000250|UniProtKB:Q14790}.
MOD_RES 389 389 Phosphoserine; by CDK1.
{ECO:0000250|UniProtKB:Q14790}.
CONFLICT 68 71 HISR -> PHPVG (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 94 99 DNAQIS -> RQCPRFL (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 96 96 A -> V (in Ref. 2; CAA07677).
{ECO:0000305}.
CONFLICT 103 107 VMLFK -> SCSFR (in Ref. 4; CAA04196).
{ECO:0000305}.
CONFLICT 475 475 K -> N (in Ref. 4; CAA04196).
{ECO:0000305}.
SEQUENCE 480 AA; 55357 MW; 045268AE3DE5ED4F CRC64;
MDFQSCLYAI AEELGSEDLA ALKFLCLDYI PHKKQETIED AQKLFLRLRE KGMLEEGNLS
FLKELLFHIS RWDLLVNFLD CNREEMVREL RDPDNAQISP YRVMLFKLSE EVSELELRSF
KFLLNNEIPK CKLEDDLSLL EIFVEMEKRT MLAENNLETL KSICDQVNKS LLGKIEDYER
SSTERRMSLE GREELPPSVL DEMSLKMAEL CDSPREQDSE SRTSDKVYQM KNKPRGYCLI
INNHDFSKAR EDITQLRKMK DRKGTDCDKE ALSKTFKELH FEIVSYDDCT ANEIHEILEG
YQSADHKNKD CFICCILSHG DKGVVYGTDG KEASIYDLTS YFTGSKCPSL SGKPKIFFIQ
ACQGSNFQKG VPDEAGFEQQ NHTLEVDSSS HKNYIPDEAD FLLGMATVKN CVSYRDPVNG
TWYIQSLCQS LRERCPQGDD ILSILTGVNY DVSNKDDRRN KGKQMPQPTF TLRKKLFFPP


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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
E1058m ELISA 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
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
20-272-191563 Caspase 3 - Mouse monoclonal [4i29] to Caspase 3; EC 3.4.22.56; CASP-3; Apopain; Cysteine protease CPP32; Yama protein; CPP-32; SREBP cleavage activity 1; SCA-1 Monoclonal 0.05 mg
20-272-192342 Caspase 3 - Mouse monoclonal [3CSP03] to Caspase 3; EC 3.4.22.56; CASP-3; Apopain; Cysteine protease CPP32; Yama protein; CPP-32; SREBP cleavage activity 1; SCA-1 Monoclonal 0.5 ml

Kits Elisa; taq POLYMERASE

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

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]
[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]
[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]
[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] 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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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]
[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)]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[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]
[CASP4] Caspase-4 (CASP-4) (EC 3.4.22.57) [Cleaved into: Caspase-4 subunit 1; Caspase-4 subunit 2]
[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]
[csp-1 Y48E1B.13] Caspase A (EC 3.4.22.36) [Cleaved into: Caspase A subunit p16; Caspase A subunit p14]
[csp-2 Y73B6BL.7] Putative inactive caspase B [Cleaved into: Putative inactive caspase B subunit p31; Putative inactive caspase B subunit p17; Putative inactive caspase subunit p14]
[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]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]

Bibliography :
[19521670] Alternative Fas-mediated cell death pathway is dependent on the different cleavage patterns of procaspase-8.
[15450950] Cadmium induces apoptotic cell death in WI 38 cells via caspase-dependent Bid cleavage and calpain-mediated mitochondrial Bax cleavage by Bcl-2-independent pathway.
[11520907] Temporal and spatial profile of caspase 8 expression and proteolysis after experimental traumatic brain injury.
[11437602] [W206R]-procaspase 3: an inactivatable substrate for caspase 8.
[10203698] Identification of a new caspase homologue: caspase-14.
[9880531] The role of c-FLIP in modulation of CD95-induced apoptosis.