Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Kallikrein-1 (EC 3.4.21.35) (Kidney/pancreas/salivary gland kallikrein) (Tissue kallikrein)

 KLK1_HUMAN              Reviewed;         262 AA.
P06870; Q66US9; Q86U61; Q8TCV8; Q9BS53; Q9NQU4; Q9UD19; Q9UMJ1;
01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
24-NOV-2009, sequence version 2.
23-MAY-2018, entry version 188.
RecName: Full=Kallikrein-1;
EC=3.4.21.35;
AltName: Full=Kidney/pancreas/salivary gland kallikrein;
AltName: Full=Tissue kallikrein;
Flags: Precursor;
Name=KLK1;
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 GLN-145 AND
GLU-186.
TISSUE=Pancreas;
PubMed=3004571; DOI=10.1021/bi00348a030;
Fukushima D., Kitamura N., Nakanishi S.;
"Nucleotide sequence of cloned cDNA for human pancreatic kallikrein.";
Biochemistry 24:8037-8043(1985).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
TISSUE=Kidney;
PubMed=2898948; DOI=10.1021/bi00409a003;
Evans B.A., Yun Z.X., Close J.A., Tregear G.W., Kitamura N.,
Nakanishi S., Callen D.F., Baker E., Hyland V.J., Sutherland G.R.,
Richards R.I.;
"Structure and chromosomal localization of the human renal kallikrein
gene.";
Biochemistry 27:3124-3129(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Salivary gland;
PubMed=2686621; DOI=10.1042/bj2620787;
Angermann A., Bergmann C., Appelhans H.;
"Cloning and expression of human salivary-gland kallikrein in
Escherichia coli.";
Biochem. J. 262:787-793(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
TISSUE SPECIFICITY.
PubMed=7749372;
Chen L.-M., Murray S.R., Chai K.X., Chao L., Chao J.;
"Molecular cloning and characterization of a novel kallikrein
transcript in colon and its distribution in human tissues.";
Braz. J. Med. Biol. Res. 27:1829-1838(1994).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11006094; DOI=10.1006/bbrc.2000.3448;
Yousef G.M., Chang A., Scorilas A., Diamandis E.P.;
"Genomic organization of the human kallikrein gene family on
chromosome 19q13.3-q13.4.";
Biochem. Biophys. Res. Commun. 276:125-133(2000).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11054574; DOI=10.1016/S0378-1119(00)00382-6;
Gan L., Lee I., Smith R., Argonza-Barrett R., Lei H., McCuaig J.,
Moss P., Paeper B., Wang K.;
"Sequencing and expression analysis of the serine protease gene
cluster located in chromosome 19q13 region.";
Gene 257:119-130(2000).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS GLN-145 AND
GLU-186.
Li T., Du G., Dai Y.;
"Kallikrein cDNA from the pancreas of a Chinese patient.";
Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-145.
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.
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT GLN-145.
SeattleSNPs variation discovery resource;
Submitted (APR-2002) to the EMBL/GenBank/DDBJ databases.
[10]
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).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
GLN-145.
TISSUE=Pancreas;
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).
[12]
NUCLEOTIDE SEQUENCE [MRNA] OF 18-262 (ISOFORM 1), AND VARIANTS GLN-145
AND GLU-186.
TISSUE=Kidney;
PubMed=3853975; DOI=10.1089/dna.1985.4.445;
Baker A.R., Shine J.;
"Human kidney kallikrein: cDNA cloning and sequence analysis.";
DNA 4:445-450(1985).
[13]
PROTEIN SEQUENCE OF 25-262 (ISOFORM 1), AND GLYCOSYLATION AT SER-93;
ASN-102; SER-104; ASN-108; ASN-165 AND SER-167.
TISSUE=Urine;
PubMed=3163150;
Kellermann J., Lottspeich F., Geiger R., Deutzmann R.;
"Human urinary kallikrein -- amino acid sequence and carbohydrate
attachment sites.";
Protein Seq. Data Anal. 1:177-182(1988).
[14]
PROTEIN SEQUENCE OF 25-262 (ISOFORM 1).
TISSUE=Urine;
PubMed=2666327;
Lu H.S., Lin F.-K., Chao L., Chao J.;
"Human urinary kallikrein. Complete amino acid sequence and sites of
glycosylation.";
Int. J. Pept. Protein Res. 33:237-249(1989).
[15]
PROTEIN SEQUENCE OF 25-55 (ISOFORM 1).
TISSUE=Urine;
PubMed=393608;
Lottspeich F., Geiger R., Henschen A., Kutzbach C.;
"N-terminal amino acid sequence of human urinary kallikrein homology
with other serine proteases.";
Hoppe-Seyler's Z. Physiol. Chem. 360:1947-1950(1979).
[16]
PROTEIN SEQUENCE OF 28-47 (ISOFORM 1).
TISSUE=Urine;
PubMed=3635530;
Takahashi S., Irie A., Katayama Y., Ito K., Miyake Y.;
"N-terminal amino acid sequence of human urinary prokallikrein.";
J. Biochem. 99:989-992(1986).
[17]
X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF 25-262, GLYCOSYLATION AT
ASN-108, AND DISULFIDE BONDS.
PubMed=15651049; DOI=10.1002/prot.20368;
Laxmikanthan G., Blaber S.I., Bernett M.J., Scarisbrick I.A.,
Juliano M.A., Blaber M.;
"1.70 A X-ray structure of human apo kallikrein 1: structural changes
upon peptide inhibitor/substrate binding.";
Proteins 58:802-814(2005).
[18]
CHARACTERIZATION OF VARIANTS HIS-77 AND GLN-145, AND POLYMORPHISM.
PubMed=11912256;
Slim R., Torremocha F., Moreau T., Pizard A., Hunt S.C., Vuagnat A.,
Williams G.H., Gauthier F., Jeunemaitre X., Alhenc-Gelas F.;
"Loss-of-function polymorphism of the human kallikrein gene with
reduced urinary kallikrein activity.";
J. Am. Soc. Nephrol. 13:968-976(2002).
[19]
POLYMORPHISM.
PubMed=15765151; DOI=10.1172/JCI200523669;
Azizi M., Boutouyrie P., Bissery A., Agharazii M., Verbeke F.,
Stern N., Bura-Riviere A., Laurent S., Alhenc-Gelas F.,
Jeunemaitre X.;
"Arterial and renal consequences of partial genetic deficiency in
tissue kallikrein activity in humans.";
J. Clin. Invest. 115:780-787(2005).
-!- FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds
in kininogen to release Lys-bradykinin.
-!- CATALYTIC ACTIVITY: Preferential cleavage of Arg-|-Xaa bonds in
small molecule substrates. Highly selective action to release
kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of
Met-|-Xaa or Leu-|-Xaa.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P06870-1; Sequence=Displayed;
Name=2;
IsoId=P06870-2; Sequence=VSP_037483;
-!- TISSUE SPECIFICITY: Isoform 2 is expressed in pancreas, salivary
glands, kidney, colon, prostate gland, testis, spleen and the
colon adenocarcinoma cell line T84. {ECO:0000269|PubMed:7749372}.
-!- PTM: The O-linked polysaccharides on Ser-93, Ser-104 and Ser-167
are probably the mucin type linked to GalNAc. In PubMed:3163150,
GalNAc was detected with the corresponding peptides but not
located. {ECO:0000269|PubMed:15651049,
ECO:0000269|PubMed:3163150}.
-!- POLYMORPHISM: Genetic variations in KLK1 are the cause of a
decreased in urinary kallikrein activity [MIM:615953]. The His-77
mutation dramatically reduces the activity of the enzyme in the
urine. There is a 50 to 60% reduction in urinary kallikrein
activity in His-77 individuals, but renal and hormonal adaptation
to dietary changes in sodium and potassium are unaffected.
However, in studies of brachial artery function, His-77
individuals consistently exhibited an increase in wall shear
stress and a paradoxical reduction in artery diameter and lumen
compared to Arg-77 individuals. This partial genetic deficiency in
kallikrein activity is associated with a form of arterial
dysfunction involving inappropriate inward remodeling of the
brachial artery despite a chronic increase in shear stress.
{ECO:0000269|PubMed:11912256, ECO:0000269|PubMed:15765151}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Kallikrein entry;
URL="https://en.wikipedia.org/wiki/Kallikrein";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/klk1/";
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; M25629; AAA36136.1; -; mRNA.
EMBL; M33109; AAA59455.1; -; Genomic_DNA.
EMBL; M33105; AAA59455.1; JOINED; Genomic_DNA.
EMBL; M33106; AAA59455.1; JOINED; Genomic_DNA.
EMBL; M33107; AAA59455.1; JOINED; Genomic_DNA.
EMBL; M33108; AAA59455.1; JOINED; Genomic_DNA.
EMBL; X13561; CAA31912.1; -; mRNA.
EMBL; AF277050; AAF86333.1; -; Genomic_DNA.
EMBL; AF243527; AAG33353.1; -; Genomic_DNA.
EMBL; AY703451; AAU12569.1; -; mRNA.
EMBL; BT007253; AAP35917.1; -; mRNA.
EMBL; AY094609; AAM11874.1; -; Genomic_DNA.
EMBL; AC010325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC005313; AAH05313.1; -; mRNA.
EMBL; M12706; AAA59201.1; -; mRNA.
CCDS; CCDS12804.1; -. [P06870-1]
PIR; A24696; KQHU.
PIR; B24696; B24696.
RefSeq; NP_002248.1; NM_002257.3. [P06870-1]
UniGene; Hs.123107; -.
PDB; 1SPJ; X-ray; 1.70 A; A=25-262.
PDBsum; 1SPJ; -.
ProteinModelPortal; P06870; -.
SMR; P06870; -.
BioGrid; 110016; 15.
STRING; 9606.ENSP00000301420; -.
BindingDB; P06870; -.
ChEMBL; CHEMBL2319; -.
DrugBank; DB06692; Aprotinin.
GuidetoPHARMACOLOGY; 2865; -.
GlyConnect; 172; -.
iPTMnet; P06870; -.
UniCarbKB; P06870; -.
BioMuta; KLK1; -.
DMDM; 269849612; -.
PaxDb; P06870; -.
PeptideAtlas; P06870; -.
PRIDE; P06870; -.
DNASU; 3816; -.
Ensembl; ENST00000301420; ENSP00000301420; ENSG00000167748. [P06870-1]
GeneID; 3816; -.
KEGG; hsa:3816; -.
UCSC; uc002ptk.3; human. [P06870-1]
CTD; 3816; -.
DisGeNET; 3816; -.
EuPathDB; HostDB:ENSG00000167748.10; -.
GeneCards; KLK1; -.
HGNC; HGNC:6357; KLK1.
MalaCards; KLK1; -.
MIM; 147910; gene.
MIM; 615953; phenotype.
neXtProt; NX_P06870; -.
OpenTargets; ENSG00000167748; -.
PharmGKB; PA224; -.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00910000144067; -.
HOVERGEN; HBG013304; -.
InParanoid; P06870; -.
KO; K01325; -.
OMA; LWLGRHN; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; P06870; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.35; 2681.
Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
ChiTaRS; KLK1; human.
EvolutionaryTrace; P06870; -.
GeneWiki; KLK1; -.
GenomeRNAi; 3816; -.
PRO; PR:P06870; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167748; -.
CleanEx; HS_KLK1; -.
ExpressionAtlas; P06870; baseline and differential.
Genevisible; P06870; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; TAS:ProtInc.
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;
3D-structure; Alternative splicing; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
Polymorphism; Protease; Reference proteome; Serine protease; Signal;
Zymogen.
SIGNAL 1 18 {ECO:0000305}.
PROPEP 19 24 Activation peptide. {ECO:0000305}.
/FTId=PRO_0000027923.
CHAIN 25 262 Kallikrein-1.
/FTId=PRO_0000027924.
DOMAIN 25 259 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 65 65 Charge relay system.
ACT_SITE 120 120 Charge relay system.
ACT_SITE 214 214 Charge relay system.
CARBOHYD 93 93 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3163150}.
CARBOHYD 102 102 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:3163150}.
CARBOHYD 104 104 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3163150}.
CARBOHYD 108 108 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:15651049,
ECO:0000269|PubMed:3163150}.
CARBOHYD 165 165 N-linked (GlcNAc...) asparagine; partial.
{ECO:0000269|PubMed:3163150}.
CARBOHYD 167 167 O-linked (GalNAc...) serine.
{ECO:0000269|PubMed:3163150}.
DISULFID 31 174 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:15651049}.
DISULFID 50 66 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:15651049}.
DISULFID 153 220 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:15651049}.
DISULFID 185 199 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:15651049}.
DISULFID 210 235 {ECO:0000255|PROSITE-ProRule:PRU00274,
ECO:0000269|PubMed:15651049}.
VAR_SEQ 1 69 MWFLVLCLALSLGGTGAAPPIQSRIVGGWECEQHSQPWQAA
LYHFSTFQCGGILVHRQWVLTAAHCISD -> MLPCPIPFS
PSRLLIPPFPSFPS (in isoform 2).
{ECO:0000303|PubMed:7749372}.
/FTId=VSP_037483.
VARIANT 77 77 R -> H (polymorphism; associated with a
significant decrease in urinary
kallikrein activity; dbSNP:rs5515).
{ECO:0000269|PubMed:11912256}.
/FTId=VAR_014567.
VARIANT 145 145 E -> Q (polymorphism; not associated with
changes in urinary kallikrein activity;
dbSNP:rs5516).
{ECO:0000269|PubMed:11912256,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2898948,
ECO:0000269|PubMed:3004571,
ECO:0000269|PubMed:3853975,
ECO:0000269|Ref.7, ECO:0000269|Ref.8,
ECO:0000269|Ref.9}.
/FTId=VAR_006625.
VARIANT 186 186 K -> E (in dbSNP:rs5517).
{ECO:0000269|PubMed:3004571,
ECO:0000269|PubMed:3853975,
ECO:0000269|Ref.7}.
/FTId=VAR_006626.
VARIANT 193 193 V -> E (in dbSNP:rs5518).
/FTId=VAR_014568.
CONFLICT 114 114 D -> N (in Ref. 7; AAU12569).
{ECO:0000305}.
CONFLICT 139 139 V -> F (in Ref. 7; AAU12569).
{ECO:0000305}.
CONFLICT 188 188 A -> V (in Ref. 8; AAP35917 and 11;
AAH05313). {ECO:0000305}.
STRAND 39 44 {ECO:0000244|PDB:1SPJ}.
STRAND 47 56 {ECO:0000244|PDB:1SPJ}.
STRAND 59 62 {ECO:0000244|PDB:1SPJ}.
HELIX 64 66 {ECO:0000244|PDB:1SPJ}.
STRAND 69 76 {ECO:0000244|PDB:1SPJ}.
STRAND 88 90 {ECO:0000244|PDB:1SPJ}.
STRAND 92 97 {ECO:0000244|PDB:1SPJ}.
HELIX 103 106 {ECO:0000244|PDB:1SPJ}.
TURN 112 114 {ECO:0000244|PDB:1SPJ}.
STRAND 122 128 {ECO:0000244|PDB:1SPJ}.
STRAND 152 159 {ECO:0000244|PDB:1SPJ}.
STRAND 161 165 {ECO:0000244|PDB:1SPJ}.
STRAND 173 180 {ECO:0000244|PDB:1SPJ}.
HELIX 182 188 {ECO:0000244|PDB:1SPJ}.
STRAND 197 201 {ECO:0000244|PDB:1SPJ}.
STRAND 206 208 {ECO:0000244|PDB:1SPJ}.
STRAND 217 220 {ECO:0000244|PDB:1SPJ}.
STRAND 223 230 {ECO:0000244|PDB:1SPJ}.
STRAND 242 246 {ECO:0000244|PDB:1SPJ}.
HELIX 247 250 {ECO:0000244|PDB:1SPJ}.
HELIX 251 260 {ECO:0000244|PDB:1SPJ}.
SEQUENCE 262 AA; 28890 MW; 7D8A715E9E104D60 CRC64;
MWFLVLCLAL SLGGTGAAPP IQSRIVGGWE CEQHSQPWQA ALYHFSTFQC GGILVHRQWV
LTAAHCISDN YQLWLGRHNL FDDENTAQFV HVSESFPHPG FNMSLLENHT RQADEDYSHD
LMLLRLTEPA DTITDAVKVV ELPTEEPEVG STCLASGWGS IEPENFSFPD DLQCVDLKIL
PNDECKKAHV QKVTDFMLCV GHLEGGKDTC VGDSGGPLMC DGVLQGVTSW GYVPCGTPNK
PSVAVRVLSY VKWIEDTIAE NS


Related products :

Catalog number Product name Quantity
E0967h ELISA Homo sapiens,Human,Kallikrein-1,Kidney_pancreas_salivary gland kallikrein,KLK1,Tissue kallikrein 96T
U0967h CLIA Homo sapiens,Human,Kallikrein-1,Kidney_pancreas_salivary gland kallikrein,KLK1,Tissue kallikrein 96T
E0967h ELISA kit Homo sapiens,Human,Kallikrein-1,Kidney_pancreas_salivary gland kallikrein,KLK1,Tissue kallikrein 96T
06-271-83288 Kallikrein Inhibitor - EC 3.4.21.35; Tissue kallikrein; Kidney_pancreas_salivary gland kallikrein 5 mg
06-271-83288 Kallikrein Inhibitor - EC 3.4.21.35; Tissue kallikrein; Kidney_pancreas_salivary gland kallikrein 1 mg
E0967m ELISA Glandular kallikrein K1,KAL-B,Kallikrein-1,Klk1,Klk6,Klk-6,mGK-6,Mouse,Mus musculus,Renal kallikrein,Tissue kallikrein-6 96T
U0967m CLIA Glandular kallikrein K1,KAL-B,Kallikrein-1,Klk1,Klk6,Klk-6,mGK-6,Mouse,Mus musculus,Renal kallikrein,Tissue kallikrein-6 96T
E0967m ELISA kit Glandular kallikrein K1,KAL-B,Kallikrein-1,Klk1,Klk6,Klk-6,mGK-6,Mouse,Mus musculus,Renal kallikrein,Tissue kallikrein-6 96T
E0691r ELISA kit Glandular kallikrein-8,Klk6,Klk8,Klk-8,P1 kallikrein,Prostatic glandular kallikrein-6,Rat,Rattus norvegicus,rGK-8,Tissue kallikrein 96T
U0691r CLIA Glandular kallikrein-8,Klk6,Klk8,Klk-8,P1 kallikrein,Prostatic glandular kallikrein-6,Rat,Rattus norvegicus,rGK-8,Tissue kallikrein 96T
E0691r ELISA Glandular kallikrein-8,Klk6,Klk8,Klk-8,P1 kallikrein,Prostatic glandular kallikrein-6,Rat,Rattus norvegicus,rGK-8,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
U0151r CLIA Glandular kallikrein-3, submandibular,Klk3,Klk-3,Rat,Rattus norvegicus,rGK-3,RSGK-50,S1 kallikrein,Tissue kallikrein 96T
E0151r ELISA Glandular kallikrein-3, submandibular,Klk3,Klk-3,Rat,Rattus norvegicus,rGK-3,RSGK-50,S1 kallikrein,Tissue kallikrein 96T
E0278h ELISA 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
E0278h ELISA kit Glandular kallikrein-1,hGK-1,Homo sapiens,Human,Kallikrein-2,KLK2,Tissue kallikrein-2 96T
Y051553 Anti-Kallikrein-1 Tissue per Pancreatic per Urinary per Renal Kallikrein; Kallikrein loop antibody 250ug
U1910r CLIA kit Esterase B,Glandular kallikrein-7, submandibular_renal,Kallikrein-related protein K1,Klk7,Klk-7,Proteinase A,Rat,Rattus norvegicus,rGK-7,RSKG-7,Tissue kallikrein 96T
E1910r ELISA kit Esterase B,Glandular kallikrein-7, submandibular_renal,Kallikrein-related protein K1,Klk7,Klk-7,Proteinase A,Rat,Rattus norvegicus,rGK-7,RSKG-7,Tissue kallikrein 96T
U1910r CLIA Esterase B,Glandular kallikrein-7, submandibular_renal,Kallikrein-related protein K1,Klk7,Klk-7,Proteinase A,Rat,Rattus norvegicus,rGK-7,RSKG-7,Tissue kallikrein 96T
E1910r ELISA Esterase B,Glandular kallikrein-7, submandibular_renal,Kallikrein-related protein K1,Klk7,Klk-7,Proteinase A,Rat,Rattus norvegicus,rGK-7,RSKG-7,Tissue kallikrein 96T
U0408r CLIA Klk9,Klk-9,Klks3,KLK-S3,Rat,Rattus norvegicus,rGK-9,S3 kallikrein,SEV,Submandibular enzymatic vasoconstrictor,Submandibular glandular kallikrein-9,Tissue kallikrein 96T
E0408r ELISA Klk9,Klk-9,Klks3,KLK-S3,Rat,Rattus norvegicus,rGK-9,S3 kallikrein,SEV,Submandibular enzymatic vasoconstrictor,Submandibular glandular kallikrein-9,Tissue kallikrein 96T
E0408r ELISA kit Klk9,Klk-9,Klks3,KLK-S3,Rat,Rattus norvegicus,rGK-9,S3 kallikrein,SEV,Submandibular enzymatic vasoconstrictor,Submandibular glandular kallikrein-9,Tissue kallikrein 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur