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Caspase-9 (CASP-9) (EC 3.4.22.62) (Apoptotic protease Mch-6) (Apoptotic protease-activating factor 3) (APAF-3) (ICE-like apoptotic protease 6) (ICE-LAP6) [Cleaved into: Caspase-9 subunit p35; Caspase-9 subunit p10]

 CASP9_HUMAN             Reviewed;         416 AA.
P55211; B4E1A3; O95348; Q53Y70; Q5JRU9; Q5UGI1; Q92852; Q9BQ62;
Q9UEQ3; Q9UIJ8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
22-FEB-2003, sequence version 3.
13-FEB-2019, entry version 212.
RecName: Full=Caspase-9;
Short=CASP-9;
EC=3.4.22.62 {ECO:0000269|PubMed:23516580};
AltName: Full=Apoptotic protease Mch-6;
AltName: Full=Apoptotic protease-activating factor 3;
Short=APAF-3;
AltName: Full=ICE-like apoptotic protease 6;
Short=ICE-LAP6;
Contains:
RecName: Full=Caspase-9 subunit p35;
Contains:
RecName: Full=Caspase-9 subunit p10;
Flags: Precursor;
Name=CASP9; Synonyms=MCH6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS VAL-28 AND
ARG-221.
PubMed=8663294; DOI=10.1074/jbc.271.28.16720;
Duan H., Orth K., Chinnaiyan A.M., Poirier G.G., Froelich C.J.,
He W.-W., Dixit V.M.;
"ICE-LAP6, a novel member of the ICE/Ced-3 gene family, is activated
by the cytotoxic T cell protease granzyme B.";
J. Biol. Chem. 271:16720-16724(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PROTEOLYTIC PROCESSING.
TISSUE=T-cell;
PubMed=8900201; DOI=10.1074/jbc.271.43.27099;
Srinivasula S.M., Fernandes-Alnemri T., Zangrilli J., Robertson N.,
Armstrong R.C., Wang L., Trapani J.A., Tomaselli K.J., Litwack G.,
Alnemri E.S.;
"The Ced-3/interleukin 1beta converting enzyme-like homolog Mch6 and
the lamin-cleaving enzyme Mch2alpha are substrates for the apoptotic
mediator CPP32.";
J. Biol. Chem. 271:27099-27106(1996).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10384055; DOI=10.1007/s003359901086;
Hadano S., Nasir J., Nichol K., Rasper D.M., Vaillancourt J.P.,
Sherer S.W., Beatty B.G., Ikeda J.E., Nicholson D.W., Hayden M.R.;
"Genomic organization of the human caspase-9 gene on chromosome
1p36.1-p36.3.";
Mamm. Genome 10:757-760(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=10070954;
Srinivasula S.M., Ahmad M., Guo Y., Zhan Y., Lazebnik Y.,
Fernandes-Alnemri T., Alnemri E.S.;
"Identification of an endogenous dominant-negative short isoform of
caspase-9 that can regulate apoptosis.";
Cancer Res. 59:999-1002(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
TISSUE=Stomach cancer;
Izawa M., Mori T., Ito H., Sairenji T.;
"Molecular cloning and sequencing of a cDNA predicting an alternative
form of pro-caspase-9 from human gastric cancer cell lines.";
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Miho Y., Momoi T., Fujita E.;
"A novel splicing product of human caspase-9 lacking protease
activity.";
Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT VAL-28.
PubMed=9890966; DOI=10.1074/jbc.274.4.2072;
Seol D.W., Billiar T.R.;
"A caspase-9 variant missing the catalytic site is an endogenous
inhibitor of apoptosis.";
J. Biol. Chem. 274:2072-2076(1999).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), AND VARIANT VAL-28.
PubMed=16780893; DOI=10.1016/j.lfs.2006.04.026;
Wang P., Shi T., Ma D.;
"Cloning of a novel human caspase-9 splice variant containing only the
CARD domain.";
Life Sci. 79:934-940(2006).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS VAL-28; LEU-99;
ILE-102; VAL-106; ASP-114; HIS-173 AND ARG-221.
NIEHS SNPs program;
Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Kidney;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[14]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Lymph;
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).
[15]
PHOSPHORYLATION AT THR-125.
PubMed=12792650; DOI=10.1038/ncb1005;
Allan L.A., Morrice N., Brady S., Magee G., Pathak S., Clarke P.R.;
"Inhibition of caspase-9 through phosphorylation at Thr 125 by ERK
MAPK.";
Nat. Cell Biol. 5:647-654(2003).
[16]
INTERACTION WITH BIRC6/BRUCE.
PubMed=15200957; DOI=10.1016/j.molcel.2004.05.018;
Bartke T., Pohl C., Pyrowolakis G., Jentsch S.;
"Dual role of BRUCE as an antiapoptotic IAP and a chimeric E2/E3
ubiquitin ligase.";
Mol. Cell 14:801-811(2004).
[17]
FUNCTION IN APOPTOSIS, INTERACTION WITH ABL1, PROTEOLYTIC PROCESSING,
PHOSPHORYLATION AT TYR-153 BY ABL1, AND MUTAGENESIS OF TYR-153.
PubMed=15657060; DOI=10.1074/jbc.M413787200;
Raina D., Pandey P., Ahmad R., Bharti A., Ren J., Kharbanda S.,
Weichselbaum R., Kufe D.;
"c-Abl tyrosine kinase regulates caspase-9 autocleavage in the
apoptotic response to DNA damage.";
J. Biol. Chem. 280:11147-11151(2005).
[18]
INTERACTION WITH HAX1, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=16857965; DOI=10.1161/01.RES.0000237387.05259.a5;
Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T.,
Kang P.M.;
"Overexpression of HAX-1 protects cardiac myocytes from apoptosis
through caspase-9 inhibition.";
Circ. Res. 99:415-423(2006).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-125; SER-302 AND
SER-307, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[20]
INTERACTION WITH EFHD2.
PubMed=19118655; DOI=10.1016/j.jprot.2008.11.016;
Checinska A., Giaccone G., Rodriguez J.A., Kruyt F.A.E., Jimenez C.R.;
"Comparative proteomics analysis of caspase-9-protein complexes in
untreated and cytochrome c/dATP stimulated lysates of NSCLC cells.";
J. Proteomics 72:575-585(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-307, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[22]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-310, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[23]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 140-416, AND SUBUNIT.
PubMed=11734640; DOI=10.1073/pnas.231465798;
Renatus M., Stennicke H.R., Scott F.L., Liddington R.C.,
Salvesen G.S.;
"Dimer formation drives the activation of the cell death protease
caspase 9.";
Proc. Natl. Acad. Sci. U.S.A. 98:14250-14255(2001).
[24]
X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 140-416 IN COMPLEX WITH
BIRC4/XIAP.
PubMed=12620238; DOI=10.1016/S1097-2765(03)00054-6;
Shiozaki E.N., Chai J., Rigotti D.J., Riedl S.J., Li P.,
Srinivasula S.M., Alnemri E.S., Fairman R., Shi Y.;
"Mechanism of XIAP-mediated inhibition of caspase-9.";
Mol. Cell 11:519-527(2003).
[25]
X-RAY CRYSTALLOGRAPHY (3.49 ANGSTROMS) OF 140-416 IN COMPLEX WITH
E.COLI NLEF, INTERACTION WITH E.COLI NLEF, SUBUNIT, CATALYTIC
ACTIVITY, FUNCTION, AND ACTIVITY REGULATION.
PubMed=23516580; DOI=10.1371/journal.pone.0058937;
Blasche S., Mortl M., Steuber H., Siszler G., Nisa S., Schwarz F.,
Lavrik I., Gronewold T.M., Maskos K., Donnenberg M.S., Ullmann D.,
Uetz P., Kogl M.;
"The E. coli effector protein NleF is a caspase inhibitor.";
PLoS ONE 8:E58937-E58937(2013).
-!- FUNCTION: Involved in the activation cascade of caspases
responsible for apoptosis execution. Binding of caspase-9 to Apaf-
1 leads to activation of the protease which then cleaves and
activates caspase-3. Promotes DNA damage-induced apoptosis in a
ABL1/c-Abl-dependent manner. Proteolytically cleaves poly(ADP-
ribose) polymerase (PARP).
-!- FUNCTION: Isoform 2 lacks activity is an dominant-negative
inhibitor of caspase-9.
-!- CATALYTIC ACTIVITY:
Reaction=Strict requirement for an Asp residue at position P1 and
with a marked preference for His at position P2. It has a
preferred cleavage sequence of Leu-Gly-His-Asp-|-Xaa.;
EC=3.4.22.62; Evidence={ECO:0000269|PubMed:23516580};
-!- ACTIVITY REGULATION: Inhibited by the effector protein NleF that
is produced by pathogenic E.coli; this inhibits apoptosis.
{ECO:0000269|PubMed:23516580}.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 35 kDa (p35) and a 10
kDa (p10) subunit. Caspase-9 and APAF1 bind to each other via
their respective NH2-terminal CED-3 homologous domains in the
presence of cytochrome C and ATP. Interacts (inactive form) with
EFHD2. Interacts with HAX1. Interacts with BIRC2/c-IAP1,
XIAP/BIRC4, BIRC5/survivin, BIRC6/bruce and BIRC7/livin. Interacts
with ABL1 (via SH3 domain); the interaction is direct and
increases in the response of cells to genotoxic stress and ABL1/c-
Abl activation. Interacts with NleF from pathogenic E.coli.
{ECO:0000269|PubMed:11734640, ECO:0000269|PubMed:12620238,
ECO:0000269|PubMed:15200957, ECO:0000269|PubMed:15657060,
ECO:0000269|PubMed:16857965, ECO:0000269|PubMed:19118655,
ECO:0000269|PubMed:23516580}.
-!- INTERACTION:
O14727:APAF1; NbExp=22; IntAct=EBI-516799, EBI-446492;
Q13490:BIRC2; NbExp=9; IntAct=EBI-516799, EBI-514538;
Q13489:BIRC3; NbExp=2; IntAct=EBI-516799, EBI-517709;
O15392:BIRC5; NbExp=2; IntAct=EBI-516799, EBI-518823;
Q96CA5:BIRC7; NbExp=10; IntAct=EBI-516799, EBI-517623;
Q6PIA0:BIRC8; NbExp=3; IntAct=EBI-516799, EBI-2129837;
P42574:CASP3; NbExp=2; IntAct=EBI-516799, EBI-524064;
P43146:DCC; NbExp=2; IntAct=EBI-516799, EBI-1222919;
Q13418:ILK; NbExp=2; IntAct=EBI-516799, EBI-747644;
P98170:XIAP; NbExp=17; IntAct=EBI-516799, EBI-517127;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=9L, Alpha;
IsoId=P55211-1; Sequence=Displayed;
Name=2; Synonyms=9S, Beta;
IsoId=P55211-2; Sequence=VSP_000818;
Name=3; Synonyms=Gamma;
IsoId=P55211-3; Sequence=VSP_043910, VSP_043911;
Note=May function as an endogenous apoptotic inhibitor, inhibits
the BAX-mediated cleavage of procaspase-3.;
Name=4;
IsoId=P55211-4; Sequence=VSP_044256;
-!- TISSUE SPECIFICITY: Ubiquitous, with highest expression in the
heart, moderate expression in liver, skeletal muscle, and
pancreas. Low levels in all other tissues. Within the heart,
specifically expressed in myocytes. {ECO:0000269|PubMed:16857965}.
-!- DEVELOPMENTAL STAGE: Expressed at low levels in fetal heart, at
moderate levels in neonate heart, and at high levels in adult
heart. {ECO:0000269|PubMed:16857965}.
-!- PTM: Cleavages at Asp-315 by granzyme B and at Asp-330 by caspase-
3 generate the two active subunits. Caspase-8 and -10 can also be
involved in these processing events.
-!- PTM: Phosphorylated at Thr-125 by MAPK1/ERK2. Phosphorylation at
Thr-125 is sufficient to block caspase-9 processing and subsequent
caspase-3 activation. Phosphorylation on Tyr-153 by ABL1/c-Abl;
occurs in the response of cells to DNA damage.
{ECO:0000269|PubMed:12792650, ECO:0000269|PubMed:15657060}.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/CASP9ID423ch1p36.html";
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp9/";
-!- WEB RESOURCE: Name=Wikipedia; Note=Caspase-9 entry;
URL="https://en.wikipedia.org/wiki/Caspase-9";
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EMBL; U56390; AAC50640.1; -; mRNA.
EMBL; U60521; AAC50776.1; -; mRNA.
EMBL; AB019205; BAA82697.1; -; Genomic_DNA.
EMBL; AF093130; AAD12248.1; -; mRNA.
EMBL; AB015653; BAA78780.1; -; mRNA.
EMBL; AB020979; BAA87905.1; -; mRNA.
EMBL; AF110376; AAD13615.1; -; mRNA.
EMBL; AY732490; AAV33129.1; -; mRNA.
EMBL; AY214168; AAO21133.1; -; Genomic_DNA.
EMBL; BT006911; AAP35557.1; -; mRNA.
EMBL; AK303743; BAG64715.1; -; mRNA.
EMBL; AL512883; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471167; EAW51730.1; -; Genomic_DNA.
EMBL; CH471167; EAW51731.1; -; Genomic_DNA.
EMBL; BC002452; AAH02452.1; -; mRNA.
EMBL; BC006463; AAH06463.1; -; mRNA.
CCDS; CCDS158.1; -. [P55211-1]
CCDS; CCDS159.2; -. [P55211-4]
CCDS; CCDS59995.1; -. [P55211-2]
PIR; G02635; G02635.
RefSeq; NP_001220.2; NM_001229.4. [P55211-1]
RefSeq; NP_001264983.1; NM_001278054.1. [P55211-2]
RefSeq; NP_127463.2; NM_032996.3. [P55211-4]
RefSeq; XP_005246071.1; XM_005246014.2. [P55211-4]
UniGene; Hs.329502; -.
PDB; 1JXQ; X-ray; 2.80 A; A/B/C/D=140-416.
PDB; 1NW9; X-ray; 2.40 A; B=140-416.
PDB; 2AR9; X-ray; 2.80 A; A/B/C/D=139-416.
PDB; 3D9T; X-ray; 1.50 A; C/D=316-321.
PDB; 3V3K; X-ray; 3.49 A; A/C/E/G/I/K/M/O=141-416.
PDB; 3YGS; X-ray; 2.50 A; P=1-95.
PDB; 4RHW; X-ray; 2.10 A; E/F=1-100.
PDB; 5JUY; EM; 4.10 A; O/P/Q/R=1-95.
PDB; 5WVC; X-ray; 2.99 A; B/D/F=1-128.
PDB; 5WVE; EM; 4.40 A; S/T/U/V/Y=1-100.
PDBsum; 1JXQ; -.
PDBsum; 1NW9; -.
PDBsum; 2AR9; -.
PDBsum; 3D9T; -.
PDBsum; 3V3K; -.
PDBsum; 3YGS; -.
PDBsum; 4RHW; -.
PDBsum; 5JUY; -.
PDBsum; 5WVC; -.
PDBsum; 5WVE; -.
ProteinModelPortal; P55211; -.
SMR; P55211; -.
BioGrid; 107292; 37.
ComplexPortal; CPX-3762; Apoptosome.
ComplexPortal; CPX-991; Caspase-9 complex.
CORUM; P55211; -.
DIP; DIP-27625N; -.
ELM; P55211; -.
IntAct; P55211; 18.
MINT; P55211; -.
STRING; 9606.ENSP00000330237; -.
BindingDB; P55211; -.
ChEMBL; CHEMBL2273; -.
GuidetoPHARMACOLOGY; 1625; -.
MEROPS; C14.010; -.
iPTMnet; P55211; -.
PhosphoSitePlus; P55211; -.
BioMuta; CASP9; -.
DMDM; 28558771; -.
EPD; P55211; -.
jPOST; P55211; -.
MaxQB; P55211; -.
PaxDb; P55211; -.
PeptideAtlas; P55211; -.
PRIDE; P55211; -.
ProteomicsDB; 56814; -.
ProteomicsDB; 56815; -. [P55211-2]
ProteomicsDB; 56816; -. [P55211-3]
DNASU; 842; -.
Ensembl; ENST00000333868; ENSP00000330237; ENSG00000132906. [P55211-1]
Ensembl; ENST00000348549; ENSP00000255256; ENSG00000132906. [P55211-2]
Ensembl; ENST00000375890; ENSP00000365051; ENSG00000132906. [P55211-4]
GeneID; 842; -.
KEGG; hsa:842; -.
UCSC; uc001awn.5; human. [P55211-1]
CTD; 842; -.
DisGeNET; 842; -.
EuPathDB; HostDB:ENSG00000132906.17; -.
GeneCards; CASP9; -.
HGNC; HGNC:1511; CASP9.
HPA; CAB004348; -.
HPA; HPA001473; -.
HPA; HPA046488; -.
MIM; 602234; gene.
neXtProt; NX_P55211; -.
OpenTargets; ENSG00000132906; -.
PharmGKB; PA26094; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00940000159698; -.
HOVERGEN; HBG059022; -.
InParanoid; P55211; -.
KO; K04399; -.
OrthoDB; 1092723at2759; -.
PhylomeDB; P55211; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.62; 2681.
Reactome; R-HSA-111458; Formation of apoptosome.
Reactome; R-HSA-111459; Activation of caspases through apoptosome-mediated cleavage.
Reactome; R-HSA-111463; SMAC (DIABLO) binds to IAPs.
Reactome; R-HSA-111464; SMAC(DIABLO)-mediated dissociation of IAP:caspase complexes.
Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
Reactome; R-HSA-198323; AKT phosphorylates targets in the cytosol.
Reactome; R-HSA-418889; Caspase activation via Dependence Receptors in the absence of ligand.
Reactome; R-HSA-5674400; Constitutive Signaling by AKT1 E17K in Cancer.
Reactome; R-HSA-9627069; Regulation of the apoptosome activity.
SABIO-RK; P55211; -.
SIGNOR; P55211; -.
EvolutionaryTrace; P55211; -.
GeneWiki; Caspase-9; -.
GenomeRNAi; 842; -.
PMAP-CutDB; P55211; -.
PRO; PR:P55211; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000132906; Expressed in 232 organ(s), highest expression level in adrenal tissue.
ExpressionAtlas; P55211; baseline and differential.
Genevisible; P55211; HS.
GO; GO:0043293; C:apoptosome; IDA:UniProtKB.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005829; C:cytosol; IDA:UniProtKB.
GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IEA:Ensembl.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IDA:UniProtKB.
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; IMP:UniProtKB.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0008233; F:peptidase activity; IDA:BHF-UCL.
GO; GO:0019901; F:protein kinase binding; IDA:UniProtKB.
GO; GO:0017124; F:SH3 domain binding; IDA:UniProtKB.
GO; GO:0008635; P:activation of cysteine-type endopeptidase activity involved in apoptotic process by cytochrome c; TAS:ProtInc.
GO; GO:0007568; P:aging; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; IMP:UniProtKB.
GO; GO:0071549; P:cellular response to dexamethasone stimulus; IEA:Ensembl.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
GO; GO:0034644; P:cellular response to UV; IDA:UniProtKB.
GO; GO:0097192; P:extrinsic apoptotic signaling pathway in absence of ligand; TAS:Reactome.
GO; GO:0034349; P:glial cell apoptotic process; IEA:Ensembl.
GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:UniProtKB.
GO; GO:0001822; P:kidney development; IEA:Ensembl.
GO; GO:0071887; P:leukocyte apoptotic process; IEA:Ensembl.
GO; GO:0030220; P:platelet formation; TAS:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0043525; P:positive regulation of neuron apoptotic process; IEA:Ensembl.
GO; GO:2001020; P:regulation of response to DNA damage stimulus; IMP:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0032025; P:response to cobalt ion; IEA:Ensembl.
GO; GO:0032355; P:response to estradiol; IEA:Ensembl.
GO; GO:0002931; P:response to ischemia; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0042770; P:signal transduction in response to DNA damage; IDA:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR033171; Caspase-9.
InterPro; IPR029030; Caspase-like_dom_sf.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom_sf.
InterPro; IPR002398; Pept_C14.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
PANTHER; PTHR10454; PTHR10454; 2.
PANTHER; PTHR10454:SF157; PTHR10454:SF157; 2.
Pfam; PF00619; CARD; 1.
PRINTS; PR00376; IL1BCENZYME.
SMART; SM00114; CARD; 1.
SMART; SM00115; CASc; 1.
SUPFAM; SSF47986; SSF47986; 1.
SUPFAM; SSF52129; SSF52129; 1.
PROSITE; PS50209; CARD; 1.
PROSITE; PS01122; CASPASE_CYS; 1.
PROSITE; PS01121; CASPASE_HIS; 1.
PROSITE; PS50207; CASPASE_P10; 1.
PROSITE; PS50208; CASPASE_P20; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Apoptosis; Complete proteome;
Hydrolase; Phosphoprotein; Polymorphism; Protease; Reference proteome;
Thiol protease; Zymogen.
PROPEP 1 ? {ECO:0000255}.
/FTId=PRO_0000004640.
CHAIN ? 315 Caspase-9 subunit p35.
/FTId=PRO_0000004641.
PROPEP 316 330
/FTId=PRO_0000004642.
CHAIN 331 416 Caspase-9 subunit p10.
/FTId=PRO_0000004643.
DOMAIN 1 92 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 237 237 {ECO:0000250}.
ACT_SITE 287 287 {ECO:0000250}.
MOD_RES 125 125 Phosphothreonine; by MAPK1.
{ECO:0000244|PubMed:18669648,
ECO:0000269|PubMed:12792650}.
MOD_RES 153 153 Phosphotyrosine; by ABL1.
{ECO:0000269|PubMed:15657060}.
MOD_RES 302 302 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 307 307 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 83 Missing (in isoform 4).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044256.
VAR_SEQ 140 289 Missing (in isoform 2).
{ECO:0000303|PubMed:10070954,
ECO:0000303|PubMed:9890966,
ECO:0000303|Ref.5, ECO:0000303|Ref.6}.
/FTId=VSP_000818.
VAR_SEQ 152 154 AYI -> TVL (in isoform 3).
{ECO:0000303|PubMed:16780893}.
/FTId=VSP_043910.
VAR_SEQ 155 416 Missing (in isoform 3).
{ECO:0000303|PubMed:16780893}.
/FTId=VSP_043911.
VARIANT 28 28 A -> V (in dbSNP:rs1052571).
{ECO:0000269|PubMed:16780893,
ECO:0000269|PubMed:8663294,
ECO:0000269|PubMed:9890966,
ECO:0000269|Ref.9}.
/FTId=VAR_015415.
VARIANT 99 99 S -> L (in dbSNP:rs4646008).
{ECO:0000269|Ref.9}.
/FTId=VAR_015416.
VARIANT 102 102 T -> I (in dbSNP:rs2308941).
{ECO:0000269|Ref.9}.
/FTId=VAR_015417.
VARIANT 106 106 L -> V (in dbSNP:rs2308938).
{ECO:0000269|Ref.9}.
/FTId=VAR_015418.
VARIANT 114 114 E -> D (in dbSNP:rs2020897).
{ECO:0000269|Ref.9}.
/FTId=VAR_015419.
VARIANT 136 136 F -> L (in dbSNP:rs1132312).
/FTId=VAR_059198.
VARIANT 173 173 R -> H (in dbSNP:rs2308950).
{ECO:0000269|Ref.9}.
/FTId=VAR_015420.
VARIANT 176 176 G -> R (in dbSNP:rs2308949).
/FTId=VAR_016131.
VARIANT 185 185 I -> M (in dbSNP:rs9282624).
/FTId=VAR_022053.
VARIANT 192 192 R -> C (in dbSNP:rs2308939).
/FTId=VAR_016132.
VARIANT 221 221 Q -> R (in dbSNP:rs1052576).
{ECO:0000269|PubMed:8663294,
ECO:0000269|Ref.9}.
/FTId=VAR_015421.
MUTAGEN 153 153 Y->F: Inhibits tyrosine phosphorylation.
Reduces caspase-9 subunit p35 formation
in response to genotoxic stress.
Attenuates ABL1/c-Abl-mediated caspase-3
activation, DNA fragmentation and UV
irradiation-induced apoptosis.
{ECO:0000269|PubMed:15657060}.
CONFLICT 32 32 R -> S (in Ref. 2; AAC50776, 3; BAA82697
and 6; BAA87905). {ECO:0000305}.
CONFLICT 96 96 A -> G (in Ref. 1; AAC50640).
{ECO:0000305}.
CONFLICT 197 197 L -> P (in Ref. 2; AAC50776 and 3;
BAA82697). {ECO:0000305}.
HELIX 3 11 {ECO:0000244|PDB:4RHW}.
HELIX 13 19 {ECO:0000244|PDB:4RHW}.
TURN 23 25 {ECO:0000244|PDB:4RHW}.
HELIX 26 31 {ECO:0000244|PDB:4RHW}.
HELIX 37 44 {ECO:0000244|PDB:4RHW}.
HELIX 51 62 {ECO:0000244|PDB:4RHW}.
HELIX 69 79 {ECO:0000244|PDB:4RHW}.
HELIX 83 93 {ECO:0000244|PDB:4RHW}.
HELIX 143 147 {ECO:0000244|PDB:1NW9}.
TURN 149 151 {ECO:0000244|PDB:1NW9}.
STRAND 157 159 {ECO:0000244|PDB:1JXQ}.
STRAND 161 167 {ECO:0000244|PDB:1NW9}.
HELIX 173 175 {ECO:0000244|PDB:1NW9}.
HELIX 183 196 {ECO:0000244|PDB:1NW9}.
STRAND 199 206 {ECO:0000244|PDB:1NW9}.
HELIX 209 221 {ECO:0000244|PDB:1NW9}.
HELIX 224 226 {ECO:0000244|PDB:2AR9}.
STRAND 228 239 {ECO:0000244|PDB:1NW9}.
STRAND 244 246 {ECO:0000244|PDB:1NW9}.
STRAND 249 251 {ECO:0000244|PDB:1NW9}.
STRAND 257 259 {ECO:0000244|PDB:1NW9}.
HELIX 260 265 {ECO:0000244|PDB:1NW9}.
TURN 269 271 {ECO:0000244|PDB:1NW9}.
HELIX 273 275 {ECO:0000244|PDB:1NW9}.
STRAND 280 287 {ECO:0000244|PDB:1NW9}.
STRAND 317 319 {ECO:0000244|PDB:3D9T}.
STRAND 340 346 {ECO:0000244|PDB:1NW9}.
STRAND 351 353 {ECO:0000244|PDB:1NW9}.
STRAND 354 356 {ECO:0000244|PDB:3V3K}.
TURN 357 359 {ECO:0000244|PDB:1JXQ}.
HELIX 362 374 {ECO:0000244|PDB:1NW9}.
TURN 375 377 {ECO:0000244|PDB:1NW9}.
HELIX 380 392 {ECO:0000244|PDB:1NW9}.
STRAND 395 398 {ECO:0000244|PDB:1JXQ}.
STRAND 402 406 {ECO:0000244|PDB:1JXQ}.
STRAND 408 410 {ECO:0000244|PDB:1NW9}.
SEQUENCE 416 AA; 46281 MW; 78E0180DF2A3BDD2 CRC64;
MDEADRRLLR RCRLRLVEEL QVDQLWDALL SRELFRPHMI EDIQRAGSGS RRDQARQLII
DLETRGSQAL PLFISCLEDT GQDMLASFLR TNRQAAKLSK PTLENLTPVV LRPEIRKPEV
LRPETPRPVD IGSGGFGDVG ALESLRGNAD LAYILSMEPC GHCLIINNVN FCRESGLRTR
TGSNIDCEKL RRRFSSLHFM VEVKGDLTAK KMVLALLELA QQDHGALDCC VVVILSHGCQ
ASHLQFPGAV YGTDGCPVSV EKIVNIFNGT SCPSLGGKPK LFFIQACGGE QKDHGFEVAS
TSPEDESPGS NPEPDATPFQ EGLRTFDQLD AISSLPTPSD IFVSYSTFPG FVSWRDPKSG
SWYVETLDDI FEQWAHSEDL QSLLLRVANA VSVKGIYKQM PGCFNFLRKK LFFKTS


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Kits Elisa; taq POLYMERASE

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Pathways :
WP1784: Apoptotic execution phase
WP1965: VEGF-receptor Signal Transduction
WP2199: Seed Development
WP2231: Degradation of apoptotic cells
WP2359: Parkin-Ubiquitin Proteasomal System pathway
WP470: Proteasome Degradation
WP712: Estrogen signaling 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
WP1046: Signaling of Hepatocyte Growth Factor Receptor

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]
[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]
[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]
[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]
[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]
[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 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]
[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]
[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]
[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]
[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)]
[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 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]
[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]
[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)]
[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]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [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) (ICE-like apoptotic protease 3) (ICE-LAP3) (SREBP cleavage activity 2) (SCA-2) [Cleaved into: Caspase-7 subunit p20; Caspase-7 subunit p11]
[CASP3] Caspase-3 (CASP-3) (EC 3.4.22.56) [Cleaved into: Caspase-3 subunit p17; Caspase-3 subunit p12]
[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]
[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]
[Nlrc4 Card12 Ipaf] NLR family CARD domain-containing protein 4 (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[gag-pol] Gag-Pol polyprotein [Cleaved into: Matrix protein p19; p2A; p2B; p10; Capsid protein p27, alternate cleaved 1; Capsid protein p27, alternate cleaved 2; Spacer peptide (SP) (p3); Nucleocapsid protein p12; Protease p15 (EC 3.4.23.-); Reverse transcriptase, beta-subunit (RT-beta); Reverse transcriptase, alpha-subunit (RT-alpha) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-) (pp32); p4]
[NLRC4 CARD12 CLAN CLAN1 IPAF UNQ6189/PRO20215] NLR family CARD domain-containing protein 4 (CARD, LRR, and NACHT-containing protein) (Clan protein) (Caspase recruitment domain-containing protein 12) (Ice protease-activating factor) (Ipaf)
[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]

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