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Caspase-5 (CASP-5) (EC 3.4.22.58) (ICE(rel)-III) (Protease ICH-3) (Protease TY) [Cleaved into: Caspase-5 subunit p20; Caspase-5 subunit p10]

 CASP5_HUMAN             Reviewed;         434 AA.
P51878; B4DKP5; Q0QVY7; Q0QVY8; Q0QVZ0; Q0QVZ1; Q0QVZ2; Q14DD6;
Q1HBJ3; Q6DJV7;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
20-APR-2010, sequence version 3.
05-JUL-2017, entry version 163.
RecName: Full=Caspase-5;
Short=CASP-5;
EC=3.4.22.58;
AltName: Full=ICE(rel)-III;
AltName: Full=Protease ICH-3;
AltName: Full=Protease TY;
Contains:
RecName: Full=Caspase-5 subunit p20;
Contains:
RecName: Full=Caspase-5 subunit p10;
Flags: Precursor;
Name=CASP5; Synonyms=ICH3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), ALTERNATIVE
SPLICING (ISOFORM 6), VARIANTS ALA-106 AND VAL-334, AND INDUCTION BY
LPS.
PubMed=16893518; DOI=10.1016/j.bbrc.2006.07.104;
Eckhart L., Kittel C., Gawlas S., Gruber F., Mildner M., Jilma B.,
Tschachler E.;
"Identification of a novel exon encoding the amino-terminus of the
predominant caspase-5 variants.";
Biochem. Biophys. Res. Commun. 348:682-688(2006).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
ALA-106.
TISSUE=Colon;
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-434 (ISOFORM 1), AND VARIANTS ALA-106
AND VAL-334.
PubMed=7797592; DOI=10.1074/jbc.270.26.15870;
Munday N.A., Vaillancourt J.P., Ali A., Casano F.J., Miller D.K.,
Molineaux S.M., Yamin T.-T., Yu V.L., Nicholson D.W.;
"Molecular cloning and pro-apoptotic activity of ICErelII and
ICErelIII, members of the ICE/CED-3 family of cysteine proteases.";
J. Biol. Chem. 270:15870-15876(1995).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-434 (ISOFORM 1), AND
VARIANTS LEU-29; ALA-106; HIS-168; LEU-217 AND VAL-334.
TISSUE=Colon;
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).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 37-434, AND VARIANT ALA-106.
TISSUE=Placenta, and Spleen;
PubMed=8617266; DOI=10.1111/j.1432-1033.1996.t01-1-00207.x;
Faucheu C., Blanchet A.-M., Collard-Dutilleul V., Lalanne J.-L.,
Diu-Hercend A.;
"Identification of a cysteine protease closely related to interleukin-
1 beta-converting enzyme.";
Eur. J. Biochem. 236:207-213(1996).
[7]
PARTIAL NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-19;
LEU-29; ARG-75; ALA-106; HIS-168; LEU-217; HIS-298; VAL-334; LYS-353
AND GLN-382.
NIEHS SNPs program;
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
[8]
PARTIAL NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT
ALA-106.
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.
[9]
INTERACTION WITH MEFV.
PubMed=17431422; DOI=10.1038/sj.cdd.4402142;
Papin S., Cuenin S., Agostini L., Martinon F., Werner S., Beer H.D.,
Grutter C., Grutter M., Tschopp J.;
"The SPRY domain of Pyrin, mutated in familial Mediterranean fever
patients, interacts with inflammasome components and inhibits proIL-
1beta processing.";
Cell Death Differ. 14:1457-1466(2007).
[10]
FUNCTION, AND MUTAGENESIS OF CYS-315.
PubMed=28314590; DOI=10.1016/j.immuni.2017.02.011;
Wang Y., Ning X., Gao P., Wu S., Sha M., Lv M., Zhou X., Gao J.,
Fang R., Meng G., Su X., Jiang Z.;
"Inflammasome Activation Triggers Caspase-1-Mediated Cleavage of cGAS
to Regulate Responses to DNA Virus Infection.";
Immunity 46:393-404(2017).
-!- FUNCTION: Mediator of programmed cell death (apoptosis). During
non-canonical inflammasome activation, cuts MB21D1 and may play a
role in the regulation of antiviral innate immune activation
(PubMed:28314590). {ECO:0000269|PubMed:28314590}.
-!- CATALYTIC ACTIVITY: Strict requirement for Asp at the P1 position.
It has a preferred cleavage sequence of Tyr-Val-Ala-Asp-|- but
also cleaves at Asp-Glu-Val-Asp-|-.
-!- SUBUNIT: Heterotetramer that consists of two anti-parallel
arranged heterodimers, each one formed by a 20 kDa (p20) and a 10
kDa (p10) subunits. Interacts with MEFV.
{ECO:0000269|PubMed:17431422}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=6;
Name=1; Synonyms=caspase-5/a;
IsoId=P51878-1; Sequence=Displayed;
Note=Most abundant isoform.;
Name=2; Synonyms=Caspase-5/b;
IsoId=P51878-2; Sequence=VSP_038993;
Note=Most abundant isoform.;
Name=3; Synonyms=Caspase-5/c;
IsoId=P51878-3; Sequence=VSP_038990;
Name=4; Synonyms=Caspase-5/e;
IsoId=P51878-4; Sequence=VSP_038993, VSP_038994, VSP_038995;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
Name=5; Synonyms=Caspase-5/f;
IsoId=P51878-5; Sequence=VSP_038992;
Name=6; Synonyms=Caspase-5-S;
IsoId=P51878-6; Sequence=VSP_038991;
Note=Produced by alternative initiation at Met-71 of isoform 1.;
-!- TISSUE SPECIFICITY: Expressed in barely detectable amounts in most
tissues except brain, highest levels being found in lung, liver
and skeletal muscle.
-!- INDUCTION: Up-regulated by bacterial lipopolysaccharides (LPS).
{ECO:0000269|PubMed:16893518}.
-!- PTM: The two subunits are derived from the precursor sequence by
an autocatalytic mechanism.
-!- SIMILARITY: Belongs to the peptidase C14A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA75172.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH74994.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAI13407.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=ABF47103.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAG59257.1; Type=Frameshift; Positions=10; Evidence={ECO:0000305};
Sequence=CAA64450.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/casp5/";
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EMBL; DQ228672; ABB58698.1; -; mRNA.
EMBL; DQ228673; ABB58699.1; -; mRNA.
EMBL; DQ228674; ABB58700.1; -; mRNA.
EMBL; DQ228676; ABB58702.1; -; mRNA.
EMBL; DQ228677; ABB58703.1; -; mRNA.
EMBL; AK296660; BAG59257.1; ALT_FRAME; mRNA.
EMBL; AP001153; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; U28015; AAA75172.1; ALT_INIT; mRNA.
EMBL; BC074994; AAH74994.1; ALT_INIT; mRNA.
EMBL; BC113406; AAI13407.1; ALT_INIT; mRNA.
EMBL; X94993; CAA64450.1; ALT_INIT; mRNA.
EMBL; DQ508420; ABF47103.1; ALT_INIT; Genomic_DNA.
EMBL; CH471065; EAW67054.1; -; Genomic_DNA.
CCDS; CCDS44718.1; -. [P51878-3]
CCDS; CCDS44719.1; -. [P51878-2]
CCDS; CCDS44720.1; -. [P51878-5]
CCDS; CCDS8328.2; -. [P51878-1]
PIR; B57511; B57511.
RefSeq; NP_001129581.1; NM_001136109.1. [P51878-2]
RefSeq; NP_001129582.1; NM_001136110.1. [P51878-3]
RefSeq; NP_001129584.1; NM_001136112.1. [P51878-5]
RefSeq; NP_004338.3; NM_004347.3. [P51878-1]
UniGene; Hs.213327; -.
ProteinModelPortal; P51878; -.
SMR; P51878; -.
BioGrid; 107288; 4.
DIP; DIP-40038N; -.
IntAct; P51878; 1.
MINT; MINT-245149; -.
STRING; 9606.ENSP00000376849; -.
BindingDB; P51878; -.
ChEMBL; CHEMBL3131; -.
GuidetoPHARMACOLOGY; 1621; -.
MEROPS; C14.008; -.
iPTMnet; P51878; -.
PhosphoSitePlus; P51878; -.
BioMuta; CASP5; -.
DMDM; 294862523; -.
MaxQB; P51878; -.
PaxDb; P51878; -.
PeptideAtlas; P51878; -.
PRIDE; P51878; -.
Ensembl; ENST00000260315; ENSP00000260315; ENSG00000137757. [P51878-1]
Ensembl; ENST00000393141; ENSP00000376849; ENSG00000137757. [P51878-5]
Ensembl; ENST00000418434; ENSP00000398130; ENSG00000137757. [P51878-3]
Ensembl; ENST00000444749; ENSP00000388365; ENSG00000137757. [P51878-2]
Ensembl; ENST00000456200; ENSP00000408455; ENSG00000137757. [P51878-4]
Ensembl; ENST00000526056; ENSP00000436877; ENSG00000137757. [P51878-5]
Ensembl; ENST00000531367; ENSP00000434471; ENSG00000137757. [P51878-3]
GeneID; 838; -.
KEGG; hsa:838; -.
UCSC; uc010ruz.1; human. [P51878-1]
CTD; 838; -.
DisGeNET; 838; -.
GeneCards; CASP5; -.
HGNC; HGNC:1506; CASP5.
HPA; HPA040937; -.
MIM; 602665; gene.
neXtProt; NX_P51878; -.
OpenTargets; ENSG00000137757; -.
PharmGKB; PA26089; -.
eggNOG; KOG3573; Eukaryota.
eggNOG; ENOG410ZQIE; LUCA.
GeneTree; ENSGT00760000118912; -.
HOVERGEN; HBG076981; -.
InParanoid; P51878; -.
KO; K04395; -.
OMA; HDEIYPI; -.
OrthoDB; EOG091G07NO; -.
PhylomeDB; P51878; -.
TreeFam; TF102023; -.
BRENDA; 3.4.22.58; 2681.
SABIO-RK; P51878; -.
GenomeRNAi; 838; -.
PRO; PR:P51878; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000137757; -.
CleanEx; HS_CASP5; -.
ExpressionAtlas; P51878; baseline and differential.
Genevisible; P51878; HS.
GO; GO:0043005; C:neuron projection; IEA:Ensembl.
GO; GO:0043025; C:neuronal cell body; IEA:Ensembl.
GO; GO:0072558; C:NLRP1 inflammasome complex; IDA:UniProtKB.
GO; GO:0097153; F:cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
GO; GO:0008234; F:cysteine-type peptidase activity; TAS:ProtInc.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0006915; P:apoptotic process; TAS:ProtInc.
GO; GO:0071260; P:cellular response to mechanical stimulus; IEP:UniProtKB.
GO; GO:0035234; P:ectopic germ cell programmed cell death; IEA:Ensembl.
GO; GO:0050718; P:positive regulation of interleukin-1 beta secretion; IEA:Ensembl.
GO; GO:0006508; P:proteolysis; TAS:ProtInc.
GO; GO:0070269; P:pyroptosis; IEA:Ensembl.
GO; GO:0042981; P:regulation of apoptotic process; IEA:InterPro.
GO; GO:0050727; P:regulation of inflammatory response; IBA:GO_Central.
GO; GO:0021762; P:substantia nigra development; IEP:UniProtKB.
CDD; cd00032; CASc; 1.
InterPro; IPR001315; CARD.
InterPro; IPR029030; Caspase-like_dom.
InterPro; IPR033139; Caspase_cys_AS.
InterPro; IPR016129; Caspase_his_AS.
InterPro; IPR011029; DEATH-like_dom.
InterPro; IPR002138; Pept_C14_p10.
InterPro; IPR001309; Pept_C14_p20.
InterPro; IPR015917; Pept_C14A.
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;
Alternative initiation; Alternative splicing; Apoptosis;
Complete proteome; Hydrolase; Polymorphism; Protease;
Reference proteome; Thiol protease; Zymogen.
PROPEP 1 136 {ECO:0000255}.
/FTId=PRO_0000004604.
CHAIN 137 327 Caspase-5 subunit p20.
/FTId=PRO_0000004605.
PROPEP 328 346 {ECO:0000255}.
/FTId=PRO_0000004606.
CHAIN 347 434 Caspase-5 subunit p10.
/FTId=PRO_0000004607.
DOMAIN 56 148 CARD. {ECO:0000255|PROSITE-
ProRule:PRU00046}.
ACT_SITE 267 267 {ECO:0000250}.
ACT_SITE 315 315
VAR_SEQ 1 145 MAEDSGKKKRRKNFEAMFKGILQSGLDNFVINHMLKNNVAG
QTSIQTLVPNTDQKSTSVKKDNHKKKTVKMLEYLGKDVLHG
VFNYLAKHDVLTLKEEEKKKYYDTKIEDKALILVDSLRKNR
VAHQMFTQTLLNMDQKITSVKP -> MAA (in isoform
3). {ECO:0000303|PubMed:16893518}.
/FTId=VSP_038990.
VAR_SEQ 1 70 Missing (in isoform 6). {ECO:0000305}.
/FTId=VSP_038991.
VAR_SEQ 1 2 MA -> MAAVPRVEGVFIFLI (in isoform 5).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038992.
VAR_SEQ 5 62 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:16893518}.
/FTId=VSP_038993.
VAR_SEQ 145 166 PLLQIEAGPPESAESTNILKLC -> HLSNKKERGPQTPGS
HHMQYKV (in isoform 4).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038994.
VAR_SEQ 167 434 Missing (in isoform 4).
{ECO:0000303|PubMed:16893518}.
/FTId=VSP_038995.
VARIANT 19 19 K -> N (in dbSNP:rs45483102).
{ECO:0000269|Ref.7}.
/FTId=VAR_047216.
VARIANT 26 26 L -> W (in dbSNP:rs1792778).
/FTId=VAR_047217.
VARIANT 29 29 F -> L (in dbSNP:rs3181320).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024403.
VARIANT 75 75 L -> R (in dbSNP:rs45585331).
{ECO:0000269|Ref.7}.
/FTId=VAR_054480.
VARIANT 106 106 T -> A (in dbSNP:rs507879).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16893518,
ECO:0000269|PubMed:7797592,
ECO:0000269|PubMed:8617266,
ECO:0000269|Ref.7, ECO:0000269|Ref.8}.
/FTId=VAR_047218.
VARIANT 168 168 R -> H (in dbSNP:rs3181179).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024404.
VARIANT 217 217 V -> L (in dbSNP:rs3181326).
{ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.7}.
/FTId=VAR_024405.
VARIANT 298 298 R -> H (in dbSNP:rs45464699).
{ECO:0000269|Ref.7}.
/FTId=VAR_054481.
VARIANT 334 334 L -> V (in dbSNP:rs523104).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16893518,
ECO:0000269|PubMed:7797592,
ECO:0000269|Ref.7}.
/FTId=VAR_047219.
VARIANT 353 353 E -> K (in dbSNP:rs45619739).
{ECO:0000269|Ref.7}.
/FTId=VAR_047220.
VARIANT 382 382 E -> Q (in dbSNP:rs45458695).
{ECO:0000269|Ref.7}.
/FTId=VAR_054482.
MUTAGEN 315 315 C->A: Abolishes protease activity.
{ECO:0000269|PubMed:28314590}.
SEQUENCE 434 AA; 49736 MW; C5257C2BF15EB6D5 CRC64;
MAEDSGKKKR RKNFEAMFKG ILQSGLDNFV INHMLKNNVA GQTSIQTLVP NTDQKSTSVK
KDNHKKKTVK MLEYLGKDVL HGVFNYLAKH DVLTLKEEEK KKYYDTKIED KALILVDSLR
KNRVAHQMFT QTLLNMDQKI TSVKPLLQIE AGPPESAEST NILKLCPREE FLRLCKKNHD
EIYPIKKRED RRRLALIICN TKFDHLPARN GAHYDIVGMK RLLQGLGYTV VDEKNLTARD
MESVLRAFAA RPEHKSSDST FLVLMSHGIL EGICGTAHKK KKPDVLLYDT IFQIFNNRNC
LSLKDKPKVI IVQACRGEKH GELWVRDSPA SLALISSQSS ENLEADSVCK IHEEKDFIAF
CSSTPHNVSW RDRTRGSIFI TELITCFQKY SCCCHLMEIF RKVQKSFEVP QAKAQMPTIE
RATLTRDFYL FPGN


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18-272-195091 Caspase 8 - Rabbit polyclonal to Caspase 8; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FADD-like ICE; FLICE; Ap 0.1 ml
18-272-196464 Caspase 8 prediluted - Rabbit polyclonal to Caspase 8 prediluted; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FA 7 ml
20-272-192408 Caspase 8 - Mouse monoclonal [C502S] to Caspase 8; EC 3.4.22.61; CASP-8; ICE-like apoptotic protease 5; MORT1-associated CED-3 homolog; MACH; FADD-homologous ICE_CED-3-like protease; FADD-like ICE; FL 0.05 mg
18-272-197069 active Caspase 9 - Rabbit polyclonal to active Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polycl 0.05 mg
18-272-197070 active Caspase 9 - Rabbit polyclonal to active Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polycl 0.05 mg
18-272-196465 Caspase 9 prediluted - Rabbit polyclonal to Caspase 9 prediluted; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF- 7 ml
20-272-191348 Caspase 9 - Mouse monoclonal [1-2] to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Monoclonal 0.05 mg
18-272-197018 Caspase 9 - Rabbit polyclonal to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polyclonal 0.1 mg
18-272-197017 Caspase 9 - Rabbit polyclonal to Caspase 9; EC 3.4.22.62; CASP-9; ICE-like apoptotic protease 6; ICE-LAP6; Apoptotic protease Mch-6; Apoptotic protease-activating factor 3; APAF-3 Polyclonal 0.1 mg
20-002-35037 Caspase-2 (anti-human Caspase-2. clone 1C10) - EC 3.4.22.-; CASP-2; ICH-1 protease; ICH-1L_1S Monoclonal 0.05 ml
20-002-35037 Caspase-2 (anti-human Caspase-2. clone 1C10) - EC 3.4.22.-; CASP-2; ICH-1 protease; ICH-1L_1S Monoclonal 0.1 ml
20-272-190220 Caspase 4 - Mouse monoclonal [CAS4] to Caspase 4; EC 3.4.22.57; CASP-4; ICH-2 protease; TX protease; ICE(rel)-II Monoclonal 0.05 ml
20-272-190221 Caspase 5 - Mouse monoclonal [CAS5] to Caspase 5; EC 3.4.22.58; CASP-5; ICH-3 protease; TY protease; ICE(rel)-III Monoclonal 0.05 ml
18-272-196627 Caspase 5 - Rabbit polyclonal to Caspase 5; EC 3.4.22.58; CASP-5; ICH-3 protease; TY protease; ICE(rel)-III Polyclonal 0.25 ml
18-272-195088 Caspase 4 - Rabbit polyclonal to Caspase 4; EC 3.4.22.57; CASP-4; ICH-2 protease; TX protease; ICE(rel)-II Polyclonal 0.1 ml
20-272-191808 Caspase 7 - Mouse monoclonal [4G2] to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Monoclonal 0.05 mg
20-272-192362 Caspase 7 - Mouse monoclonal [B4 - G2] to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Monoclonal 0.05 mg
18-272-195089 Caspase 7 - Rabbit polyclonal to Caspase 7; EC 3.4.22.60; CASP-7; ICE-like apoptotic protease 3; ICE-LAP3; Apoptotic protease Mch-3; CMH-1 Polyclonal 0.1 ml


 

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