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Kallikrein-14 (hK14) (EC 3.4.21.-) (Kallikrein-like protein 6) (KLK-L6)

 KLK14_HUMAN             Reviewed;         267 AA.
Q9P0G3; A7UNK5; Q1RMZ2; Q6B089;
11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 2.
30-AUG-2017, entry version 142.
RecName: Full=Kallikrein-14;
Short=hK14;
EC=3.4.21.-;
AltName: Full=Kallikrein-like protein 6;
Short=KLK-L6;
Flags: Precursor;
Name=KLK14; Synonyms=KLKL6;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TISSUE SPECIFICITY.
PubMed=11309303;
Yousef G.M., Magklara A., Chang A., Jung K., Katsaros D.,
Diamandis E.P.;
"Cloning of a new member of the human kallikrein gene family, KLK14,
which is down-regulated in different malignancies.";
Cancer Res. 61:3425-3431(2001).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND TISSUE SPECIFICITY.
PubMed=11352573; DOI=10.1006/geno.2000.6490;
Hooper J.D., Bui L.T., Rae F.K., Harvey T.J., Myers S.A.,
Ashworth L.K., Clements J.A.;
"Identification and characterization of KLK14, a novel kallikrein
serine protease gene located on human chromosome 19q13.4 and expressed
in prostate and skeletal muscle.";
Genomics 73:117-122(2001).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=17922479; DOI=10.1002/gepi.20185;
Andres A.M., Clark A.G., Shimmin L., Boerwinkle E., Sing C.F.,
Hixson J.E.;
"Understanding the accuracy of statistical haplotype inference with
sequence data of known phase.";
Genet. Epidemiol. 31:659-671(2007).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ARG-33 AND
TYR-45.
TISSUE=Lung;
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).
[7]
TISSUE SPECIFICITY.
PubMed=10969073; DOI=10.1074/jbc.M004525200;
Harvey T.J., Hooper J.D., Myers S.A., Stephenson S.A., Ashworth L.K.,
Clements J.A.;
"Tissue-specific expression patterns and fine mapping of the human
kallikrein (KLK) locus on proximal 19q13.4.";
J. Biol. Chem. 275:37397-37406(2000).
[8]
INDUCTION BY STEROID HORMONE.
PubMed=12645335; DOI=10.1309/0UA57MNAYV0MCE9U;
Yousef G.M., Fracchioli S., Scorilas A., Borgono C.A., Iskander L.,
Puopolo M., Massobrio M., Diamandis E.P., Katsaros D.;
"Steroid hormone regulation and prognostic value of the human
kallikrein gene 14 in ovarian cancer.";
Am. J. Clin. Pathol. 119:346-355(2003).
[9]
CHARACTERIZATION.
PubMed=15843175; DOI=10.1515/BC.2005.035;
Felber L.M., Borgono C.A., Cloutier S.M., Kuendig C., Kishi T.,
Ribeiro Chagas J., Jichlinski P., Gygi C.M., Leisinger H.-J.,
Diamandis E.P., Deperthes D.;
"Enzymatic profiling of human kallikrein 14 using phage-display
substrate technology.";
Biol. Chem. 386:291-298(2005).
[10]
FUNCTION, SUBCELLULAR LOCATION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
PROPERTIES, AND ENZYME REGULATION.
PubMed=15654974; DOI=10.1111/j.0022-202X.2004.23547.x;
Brattsand M., Stefansson K., Lundh C., Haasum Y., Egelrud T.;
"A proteolytic cascade of kallikreins in the stratum corneum.";
J. Invest. Dermatol. 124:198-203(2005).
[11]
PROTEIN SEQUENCE OF 41-55, AND TISSUE SPECIFICITY.
PubMed=16800737; DOI=10.1515/BC.2006.095;
Stefansson K., Brattsand M., Ny A., Glas B., Egelrud T.;
"Kallikrein-related peptidase 14 may be a major contributor to
trypsin-like proteolytic activity in human stratum corneum.";
Biol. Chem. 387:761-768(2006).
[12]
FUNCTION IN G PROTEIN-COUPLED RECEPTOR SIGNALING.
PubMed=16885167; DOI=10.1074/jbc.M513138200;
Oikonomopoulou K., Hansen K.K., Saifeddine M., Tea I., Blaber M.,
Blaber S.I., Scarisbrick I., Andrade-Gordon P., Cottrell G.S.,
Bunnett N.W., Diamandis E.P., Hollenberg M.D.;
"Proteinase-activated receptors, targets for kallikrein signaling.";
J. Biol. Chem. 281:32095-32112(2006).
[13]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=16456535; DOI=10.1038/sj.jid.5700146;
Komatsu N., Tsai B., Sidiropoulos M., Saijoh K., Levesque M.A.,
Takehara K., Diamandis E.P.;
"Quantification of eight tissue kallikreins in the stratum corneum and
sweat.";
J. Invest. Dermatol. 126:925-929(2006).
[14]
SUBCELLULAR LOCATION, TISSUE SPECIFICITY, PROTEOLYTIC PROCESSING,
BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME REGULATION.
PubMed=17110383; DOI=10.1074/jbc.M608348200;
Borgono C.A., Michael I.P., Shaw J.L.V., Luo L.-Y., Ghosh M.C.,
Soosaipillai A., Grass L., Katsaros D., Diamandis E.P.;
"Expression and functional characterization of the cancer-related
serine protease, human tissue kallikrein 14.";
J. Biol. Chem. 282:2405-2422(2007).
[15]
FUNCTION, AND ENZYME REGULATION.
PubMed=17158887; DOI=10.1074/jbc.M607567200;
Borgono C.A., Michael I.P., Komatsu N., Jayakumar A., Kapadia R.,
Clayman G.L., Sotiropoulou G., Diamandis E.P.;
"A potential role for multiple tissue kallikrein serine proteases in
epidermal desquamation.";
J. Biol. Chem. 282:3640-3652(2007).
[16]
FUNCTION.
PubMed=18056261; DOI=10.1074/jbc.M707253200;
Emami N., Diamandis E.P.;
"Human kallikrein-related peptidase 14 (KLK14) is a new activator
component of the KLK proteolytic cascade. Possible function in seminal
plasma and skin.";
J. Biol. Chem. 283:3031-3041(2008).
[17]
FUNCTION.
PubMed=18482984; DOI=10.1074/jbc.M801194200;
Emami N., Deperthes D., Malm J., Diamandis E.P.;
"Major role of human KLK14 in seminal clot liquefaction.";
J. Biol. Chem. 283:19561-19569(2008).
[18]
FUNCTION.
PubMed=17625593; DOI=10.1038/sj.jid.5700965;
Stefansson K., Brattsand M., Roosterman D., Kempkes C., Bocheva G.,
Steinhoff M., Egelrud T.;
"Activation of proteinase-activated receptor-2 by human kallikrein-
related peptidases.";
J. Invest. Dermatol. 128:18-25(2008).
-!- FUNCTION: Serine-type endopeptidase with a dual trypsin-like and
chymotrypsin-like substrate specificity. May activate/inactivate
the proteinase-activated receptors F2R, F2RL1 and F2RL3 and other
kallikreins including KLK1, KLK3, KLK5 and KLK11. May function in
seminal clot liquefaction through direct cleavage of the
semenogelin SEMG1 and SEMG2 and activation of KLK3. May function
through desmoglein DSG1 cleavage in epidermal desquamation a
process by which the most superficial corneocytes are shed from
the skin surface. May be involved in several aspects of tumor
progression including growth, invasion and angiogenesis.
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16885167,
ECO:0000269|PubMed:17158887, ECO:0000269|PubMed:17625593,
ECO:0000269|PubMed:18056261, ECO:0000269|PubMed:18482984}.
-!- ENZYME REGULATION: Inhibited by SERPINA1, SERPINC1, SERPINE1,
SERPINF2, aprotinin, soybean, trypsin inhibitor and leupeptin.
Inhibited by serine protease inhibitor SPINK5. Has an
autoproteolytic activity which may have a regulatory effect.
Activated by citrate and inhibited by zinc and to a lower extent
by manganese. {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383, ECO:0000269|PubMed:17158887}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.3 mM for S-2288 {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383};
KM=0.2 mM for S-2222 {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383};
KM=0.2 mM for S-2302 {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383};
KM=0.7 mM for S-2586 {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383};
KM=0.045 mM for Gln-Ala-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.043 mM for Val-Pro-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.09 mM for Pro-Phe-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.278 mM for Phe-Ser-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.0577 mM for Leu-Gly-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.139 mM for Gln-Gly-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.173 mM for Gly-Pro-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.0268 mM for Gln-Arg-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.130 mM for Gly-Gly-Arg synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
KM=0.578 mM for Val-Leu-Lys synthetic peptide
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:17110383};
Note=Has a higher catalytic efficiency for the trypsin-like
enzyme substrates S-2288, S-2222 and S-2302 compared to S-2586 a
chymotrypsin-like enzyme substrate. Has a lower catalytic
activity compared to trypsin towards S-2288, S-2222 and S-2302.
Cleaves preferentially after Arg residues.;
pH dependence:
Optimum pH is 8.0. {ECO:0000269|PubMed:15654974,
ECO:0000269|PubMed:17110383};
-!- SUBCELLULAR LOCATION: Secreted, extracellular space
{ECO:0000269|PubMed:15654974, ECO:0000269|PubMed:16456535,
ECO:0000269|PubMed:17110383}.
-!- TISSUE SPECIFICITY: Highly expressed in CNS, bone marrow and fetal
liver. Also expressed in breast, thyroid, kidney, colon, pancreas,
spleen, prostate, uterus, small intestine, placenta and skeletal
muscle. Among 40 tissues tested, the highest expression is
detected in skin followed by breast and prostate (at protein
level). Expressed in stratum corneum by sweat ducts and sweat
glands and detected in sweat (at protein level).
{ECO:0000269|PubMed:10969073, ECO:0000269|PubMed:11309303,
ECO:0000269|PubMed:11352573, ECO:0000269|PubMed:16456535,
ECO:0000269|PubMed:16800737, ECO:0000269|PubMed:17110383}.
-!- INDUCTION: Up-regulated by steroid hormone.
{ECO:0000269|PubMed:12645335}.
-!- PTM: Proteolytic cleavage of the activation peptide produces the
active enzyme. {ECO:0000269|PubMed:17110383}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- CAUTION: It is uncertain whether Met-1 or Met-17 is the initiator.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAD50773.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAG23260.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAK48523.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
Sequence=AAK48524.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=ABU63131.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; AF161221; AAD50773.2; ALT_SEQ; Genomic_DNA.
EMBL; AF283669; AAK48523.1; ALT_SEQ; Genomic_DNA.
EMBL; AF283670; AAK48524.1; ALT_INIT; mRNA.
EMBL; EU091477; ABU63131.1; ALT_SEQ; Genomic_DNA.
EMBL; AC011473; AAG23260.1; ALT_SEQ; Genomic_DNA.
EMBL; CH471135; EAW71982.1; -; Genomic_DNA.
EMBL; BC074904; AAH74904.2; -; mRNA.
EMBL; BC074905; AAH74905.2; -; mRNA.
EMBL; BC114614; AAI14615.2; -; mRNA.
CCDS; CCDS12823.2; -.
RefSeq; NP_001298111.1; NM_001311182.1.
RefSeq; NP_071329.2; NM_022046.5.
UniGene; Hs.283925; -.
ProteinModelPortal; Q9P0G3; -.
SMR; Q9P0G3; -.
BioGrid; 119063; 2.
STRING; 9606.ENSP00000156499; -.
BindingDB; Q9P0G3; -.
ChEMBL; CHEMBL2641; -.
GuidetoPHARMACOLOGY; 2866; -.
MEROPS; S01.029; -.
iPTMnet; Q9P0G3; -.
PhosphoSitePlus; Q9P0G3; -.
BioMuta; KLK14; -.
DMDM; 251757292; -.
PaxDb; Q9P0G3; -.
PeptideAtlas; Q9P0G3; -.
PRIDE; Q9P0G3; -.
Ensembl; ENST00000156499; ENSP00000156499; ENSG00000129437.
Ensembl; ENST00000391802; ENSP00000375678; ENSG00000129437.
GeneID; 43847; -.
KEGG; hsa:43847; -.
UCSC; uc002pvs.1; human.
CTD; 43847; -.
DisGeNET; 43847; -.
GeneCards; KLK14; -.
HGNC; HGNC:6362; KLK14.
HPA; CAB026228; -.
MIM; 606135; gene.
neXtProt; NX_Q9P0G3; -.
OpenTargets; ENSG00000129437; -.
PharmGKB; PA30151; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q9P0G3; -.
KO; K09622; -.
OMA; SAPKMFL; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; Q9P0G3; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.B45; 2681.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
GeneWiki; KLK14; -.
GenomeRNAi; 43847; -.
PMAP-CutDB; Q9P0G3; -.
PRO; PR:Q9P0G3; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000129437; -.
CleanEx; HS_KLK14; -.
ExpressionAtlas; Q9P0G3; baseline and differential.
Genevisible; Q9P0G3; HS.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0048730; P:epidermis morphogenesis; IDA:UniProtKB.
GO; GO:0009566; P:fertilization; IDA:UniProtKB.
GO; GO:0045744; P:negative regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0045745; P:positive regulation of G-protein coupled receptor protein signaling pathway; IDA:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0070684; P:seminal clot liquefaction; IDA:UniProtKB.
CDD; cd00190; Tryp_SPc; 1.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Autocatalytic cleavage; Complete proteome; Direct protein sequencing;
Disulfide bond; Hydrolase; Polymorphism; Protease; Reference proteome;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 34
PROPEP 35 40 Activation peptide.
{ECO:0000269|PubMed:16800737}.
/FTId=PRO_0000027958.
CHAIN 41 267 Kallikrein-14.
/FTId=PRO_0000027959.
DOMAIN 41 265 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 83 83 Charge relay system. {ECO:0000250}.
ACT_SITE 127 127 Charge relay system. {ECO:0000250}.
ACT_SITE 220 220 Charge relay system. {ECO:0000250}.
DISULFID 47 180 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 68 84 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 159 226 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 191 205 {ECO:0000255|PROSITE-ProRule:PRU00274}.
DISULFID 216 241 {ECO:0000255|PROSITE-ProRule:PRU00274}.
VARIANT 33 33 Q -> R (in dbSNP:rs35287116).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058018.
VARIANT 45 45 H -> Y (in dbSNP:rs2569491).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_058019.
VARIANT 64 64 R -> H (in dbSNP:rs2569490).
/FTId=VAR_058020.
SEQUENCE 267 AA; 29122 MW; 0CE085DA7BD1D92B CRC64;
MSLRVLGSGT WPSAPKMFLL LTALQVLAIA MTQSQEDENK IIGGHTCTRS SQPWQAALLA
GPRRRFLCGG ALLSGQWVIT AAHCGRPILQ VALGKHNLRR WEATQQVLRV VRQVTHPNYN
SRTHDNDLML LQLQQPARIG RAVRPIEVTQ ACASPGTSCR VSGWGTISSP IARYPASLQC
VNINISPDEV CQKAYPRTIT PGMVCAGVPQ GGKDSCQGDS GGPLVCRGQL QGLVSWGMER
CALPGYPGVY TNLCKYRSWI EETMRDK


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E0151r ELISA Glandular kallikrein-3, submandibular,Klk3,Klk-3,Rat,Rattus norvegicus,rGK-3,RSGK-50,S1 kallikrein,Tissue kallikrein 96T
E0151r ELISA kit Glandular kallikrein-3, submandibular,Klk3,Klk-3,Rat,Rattus norvegicus,rGK-3,RSGK-50,S1 kallikrein,Tissue kallikrein 96T
E0967h ELISA kit Homo sapiens,Human,Kallikrein-1,Kidney_pancreas_salivary gland kallikrein,KLK1,Tissue kallikrein 96T
U0151r CLIA Glandular kallikrein-3, submandibular,Klk3,Klk-3,Rat,Rattus norvegicus,rGK-3,RSGK-50,S1 kallikrein,Tissue kallikrein 96T
U0967h CLIA Homo sapiens,Human,Kallikrein-1,Kidney_pancreas_salivary gland kallikrein,KLK1,Tissue kallikrein 96T
Y051553 Anti-Kallikrein-1 Tissue per Pancreatic per Urinary per Renal Kallikrein; Kallikrein loop antibody 250ug
E0278h ELISA Glandular kallikrein-1,hGK-1,Homo sapiens,Human,Kallikrein-2,KLK2,Tissue kallikrein-2 96T
E0278h ELISA kit Glandular kallikrein-1,hGK-1,Homo sapiens,Human,Kallikrein-2,KLK2,Tissue kallikrein-2 96T
U0278h CLIA Glandular kallikrein-1,hGK-1,Homo sapiens,Human,Kallikrein-2,KLK2,Tissue kallikrein-2 96T
06-271-83288 Kallikrein Inhibitor - EC 3.4.21.35; Tissue kallikrein; Kidney_pancreas_salivary gland kallikrein 1 mg
06-271-83288 Kallikrein Inhibitor - EC 3.4.21.35; Tissue kallikrein; Kidney_pancreas_salivary gland kallikrein 5 mg
Y051555 Anti-Kallikrein-2 Glandular Kallikrein; Kallikrein loop antibody 250ug
Y051553 Anti-Kallikrein-1 (Tissue_Pancreatic_Urinary_Renal Kallikrein); Kallikrein loop Antibody 100μg
Y051555 Anti-Kallikrein-2 (Glandular Kallikrein); Kallikrein loop Antibody 100μg


 

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