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Kallikrein-8 (mK8) (EC 3.4.21.118) (Neuropsin) (NP) (Serine protease 19)

 KLK8_MOUSE              Reviewed;         260 AA.
Q61955; Q8K5D7;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-JUN-2017, entry version 144.
RecName: Full=Kallikrein-8;
Short=mK8;
EC=3.4.21.118;
AltName: Full=Neuropsin;
Short=NP;
AltName: Full=Serine protease 19;
Flags: Precursor;
Name=Klk8; Synonyms=Nrpn, Prss19;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
STRAIN=BALB/cJ; TISSUE=Hippocampus;
PubMed=7623137;
Chen Z.-L., Yoshida S., Kato K., Momota Y., Suzuki J., Tanaka T.,
Ito J., Nishino H., Aimoto S., Kiyama H., Shiosaka S.;
"Expression and activity-dependent changes of a novel limbic-serine
protease gene in the hippocampus.";
J. Neurosci. 15:5088-5097(1995).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10773678;
Yoshida S., Hirata A., Inoue N., Shiosaka S.;
"Assignment of the neuropsin gene (Prss19) to mouse chromosome band
7B4 by in situ hybridization.";
Cytogenet. Cell Genet. 88:97-98(2000).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=Czech II; TISSUE=Mammary gland;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, ENZYME REGULATION,
BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND MASS
SPECTROMETRY.
STRAIN=BALB/cJ; TISSUE=Brain;
PubMed=9556608; DOI=10.1074/jbc.273.18.11189;
Shimizu C., Yoshida S., Shibata M., Kato K., Momota Y., Matsumoto K.,
Shiosaka T., Midorikawa R., Kamachi T., Kawabe A., Shiosaka S.;
"Characterization of recombinant and brain neuropsin, a plasticity-
related serine protease.";
J. Biol. Chem. 273:11189-11196(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 85-260, AND TISSUE SPECIFICITY.
STRAIN=C57BL/6J;
PubMed=12354676; DOI=10.1016/S0303-7207(02)00184-3;
Katsu Y., Takasu E., Iguchi T.;
"Estrogen-independent expression of neuropsin, a serine protease in
the vagina of mice exposed neonatally to diethylstilbestrol.";
Mol. Cell. Endocrinol. 195:99-107(2002).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8602273; DOI=10.1016/0168-0102(95)00960-2;
Suzuki J., Yoshida S., Chen Z.-L., Momota Y., Kato K., Hirata A.,
Shiosaka S.;
"Ontogeny of neuropsin mRNA expression in the mouse brain.";
Neurosci. Res. 23:345-351(1995).
[7]
INDUCTION.
PubMed=8864305; DOI=10.1016/S0006-8993(96)00473-8;
Okabe A., Momota Y., Yoshida S., Hirata A., Ito J., Nishino H.,
Shiosaka S.;
"Kindling induces neuropsin mRNA in the mouse brain.";
Brain Res. 728:116-120(1996).
[8]
INDUCTION.
PubMed=9374276; DOI=10.1016/S0006-8993(97)00674-4;
Akita H., Matsuyama T., Iso H., Sugita M., Yoshida S.;
"Effects of oxidative stress on the expression of limbic-specific
protease neuropsin and avoidance learning in mice.";
Brain Res. 769:86-96(1997).
[9]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=9749739; DOI=10.1046/j.1460-9568.1998.00068.x;
Momota Y., Yoshida S., Ito J., Shibata M., Kato K., Sakurai K.,
Matsumoto K., Shiosaka S.;
"Blockade of neuropsin, a serine protease, ameliorates kindling
epilepsy.";
Eur. J. Neurosci. 10:760-764(1998).
[10]
TISSUE SPECIFICITY.
PubMed=9620300; DOI=10.1046/j.1523-1747.1998.00212.x;
Inoue N., Kuwae K., Ishida-Yamamoto A., Iizuka H., Shibata M.,
Yoshida S., Kato K., Shiosaka S.;
"Expression of neuropsin in the keratinizing epithelial tissue
- immunohistochemical analysis of wild-type and nude mice.";
J. Invest. Dermatol. 110:923-931(1998).
[11]
INDUCTION.
PubMed=10421059; DOI=10.1007/s004030050418;
Kitayoshi H., Inoue N., Kuwae K., Chen Z.-L., Sato H., Ohta T.,
Hosokawa K., Itami S., Yoshikawa K., Yoshida S., Shiosaka S.;
"Effect of 12-O-tetradecanoyl-phorbol ester and incisional wounding on
neuropsin mRNA and its protein expression in murine skin.";
Arch. Dermatol. Res. 291:333-338(1999).
[12]
INDUCTION.
PubMed=10196465; DOI=10.1016/S0006-8993(99)01238-X;
Tomizawa K., He X.-P., Yamanaka H., Shiosaka S., Yoshida S.;
"Injury induces neuropsin mRNA in the central nervous system.";
Brain Res. 824:308-311(1999).
[13]
FUNCTION.
PubMed=10762375; DOI=10.1046/j.1460-9568.2000.00035.x;
Komai S., Matsuyama T., Matsumoto K., Kato K., Kobayashi M.,
Imamura K., Yoshida S., Ugawa S., Shiosaka S.;
"Neuropsin regulates an early phase of Schaffer-collateral long-term
potentiation in the murine hippocampus.";
Eur. J. Neurosci. 12:1479-1486(2000).
[14]
DISRUPTION PHENOTYPE.
PubMed=11549709;
Davies B., Kearns I.R., Ure J., Davies C.H., Lathe R.;
"Loss of hippocampal serine protease BSP1/neuropsin predisposes to
global seizure activity.";
J. Neurosci. 21:6993-7000(2001).
[15]
DISRUPTION PHENOTYPE.
PubMed=11273653; DOI=10.1006/mcne.2000.0945;
Hirata A., Yoshida S., Inoue N., Matsumoto-Miyai K., Ninomiya A.,
Taniguchi M., Matsuyama T., Kato K., Iizasa H., Kataoka Y.,
Yoshida N., Shiosaka S.;
"Abnormalities of synapses and neurons in the hippocampus of
neuropsin-deficient mice.";
Mol. Cell. Neurosci. 17:600-610(2001).
[16]
INDUCTION.
PubMed=11274744; DOI=10.1016/S0168-0102(01)00200-0;
He X.-P., Shiosaka S., Yoshida S.;
"Expression of neuropsin in oligodendrocytes after injury to the
CNS.";
Neurosci. Res. 39:455-462(2001).
[17]
FUNCTION.
PubMed=11880192; DOI=10.1016/S0304-3940(01)02470-3;
Oka T., Akisada M., Okabe A., Sakurai K., Shiosaka S., Kato K.;
"Extracellular serine protease neuropsin (KLK8) modulates neurite
outgrowth and fasciculation of mouse hippocampal neurons in culture.";
Neurosci. Lett. 321:141-144(2002).
[18]
INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=14616360; DOI=10.1046/j.1365-2133.2003.05484.x;
Kirihara T., Matsumoto-Miyai K., Nakamura Y., Sadayama T., Yoshida S.,
Shiosaka S.;
"Prolonged recovery of ultraviolet B-irradiated skin in neuropsin
(KLK8)-deficient mice.";
Br. J. Dermatol. 149:700-706(2003).
[19]
FUNCTION.
PubMed=12944500;
Matsumoto-Miyai K., Ninomiya A., Yamasaki H., Tamura H., Nakamura Y.,
Shiosaka S.;
"NMDA-dependent proteolysis of presynaptic adhesion molecule L1 in the
hippocampus by neuropsin.";
J. Neurosci. 23:7727-7736(2003).
[20]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16537644; DOI=10.1242/jcs.02862;
Nakamura Y., Tamura H., Horinouchi K., Shiosaka S.;
"Role of neuropsin in formation and maturation of Schaffer-collateral
L1cam-immunoreactive synaptic boutons.";
J. Cell Sci. 119:1341-1349(2006).
[21]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=16308352; DOI=10.1113/jphysiol.2005.098715;
Tamura H., Ishikawa Y., Hino N., Maeda M., Yoshida S., Kaku S.,
Shiosaka S.;
"Neuropsin is essential for early processes of memory acquisition and
Schaffer collateral long-term potentiation in adult mouse hippocampus
in vivo.";
J. Physiol. (Lond.) 570:541-551(2006).
[22]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=17761692; DOI=10.1093/jb/mvm156;
Scott F.L., Sun J., Whisstock J.C., Kato K., Bird P.I.;
"SerpinB6 is an inhibitor of kallikrein-8 in keratinocytes.";
J. Biochem. 142:435-442(2007).
[23]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=17182622; DOI=10.1074/jbc.M607998200;
Kishibe M., Bando Y., Terayama R., Namikawa K., Takahashi H.,
Hashimoto Y., Ishida-Yamamoto A., Jiang Y.-P., Mitrovic B., Perez D.,
Iizuka H., Yoshida S.;
"Kallikrein 8 is involved in skin desquamation in cooperation with
other kallikreins.";
J. Biol. Chem. 282:5834-5841(2007).
[24]
FUNCTION, TISSUE SPECIFICITY, INDUCTION, AND DISRUPTION PHENOTYPE.
PubMed=17629414; DOI=10.1016/j.neuroscience.2007.05.037;
Terayama R., Bando Y., Murakami K., Kato K., Kishibe M., Yoshida S.;
"Neuropsin promotes oligodendrocyte death, demyelination and axonal
degeneration after spinal cord injury.";
Neuroscience 148:175-187(2007).
[25]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 33-257.
TISSUE=Hippocampus;
PubMed=9933620; DOI=10.1074/jbc.274.7.4220;
Kishi T., Kato M., Shimizu T., Kato K., Matsumoto K., Yoshida S.,
Shiosaka S., Hakoshima T.;
"Crystal structure of neuropsin, a hippocampal protease involved in
kindling epileptogenesis.";
J. Biol. Chem. 274:4220-4224(1999).
-!- FUNCTION: Serine protease which is capable of degrading a number
of proteins such as casein, fibrinogen, kininogen, fibronectin and
collagen type IV. Also cleaves L1CAM in response to increased
neural activity. Induces neurite outgrowth and fasciculation of
cultured hippocampal neurons. Plays a role in the formation and
maturation of orphan and small synaptic boutons in the Schaffer-
collateral pathway, regulates Schaffer-collateral long-term
potentiation in the hippocampus and is required for memory
acquisition and synaptic plasticity. Involved in skin desquamation
and keratinocyte proliferation. Plays a role in the secondary
phase of pathogenesis following spinal cord injury.
{ECO:0000269|PubMed:10762375, ECO:0000269|PubMed:11880192,
ECO:0000269|PubMed:12944500, ECO:0000269|PubMed:16308352,
ECO:0000269|PubMed:16537644, ECO:0000269|PubMed:17182622,
ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:9556608}.
-!- CATALYTIC ACTIVITY: Cleavage of amide substrates following the
basic amino acids Arg or Lys at the P1 position, with a preference
for Arg over Lys.
-!- ENZYME REGULATION: Strongly inhibited by diisopropyl
fluorophosphate, leupeptin and (4-amidinophenyl)methanesulfonyl 1-
fluoride. {ECO:0000269|PubMed:9556608}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=300 uM for Boc-Val-Pro-Arg-MCA {ECO:0000269|PubMed:9556608};
KM=540 uM for Boc-Phe-Ser-Arg-MCA {ECO:0000269|PubMed:9556608};
KM=280 uM for D-Val-Leu-Arg-MCA {ECO:0000269|PubMed:9556608};
-!- SUBUNIT: Interacts with SPINK9. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted. Cytoplasm. Note=Shows a
cytoplasmic distribution in the keratinocytes.
-!- TISSUE SPECIFICITY: Expressed in the limbic system of mouse brain
and is localized at highest concentration in pyramidal neurons of
the hippocampal CA1-3 subfields. Also detected in spinal cord gray
matter and in keratinized stratified epithelia of epidermis, hair,
tongue, palate, nasal cavity, pharynges, esophagus and
forestomach. In skin and mucus membranes, expressed in stratum
spinosum and stratum granulosum. Expressed during estrus in
vaginal epithelial cells but not stromal cells. Within the vaginal
epithelium, expressed in prickle cells, granular cells and
parakeratotic cells but not in basal cells. Not expressed in
uterus. Expressed in the keratinocytes.
{ECO:0000269|PubMed:12354676, ECO:0000269|PubMed:17629414,
ECO:0000269|PubMed:17761692, ECO:0000269|PubMed:7623137,
ECO:0000269|PubMed:8602273, ECO:0000269|PubMed:9620300,
ECO:0000269|PubMed:9749739}.
-!- DEVELOPMENTAL STAGE: Expression is detected in the brain from
embryonic day 12 and continues into adulthood.
{ECO:0000269|PubMed:8602273}.
-!- INDUCTION: By chemical/incision-induced brain injury which leads
to increased expression in axon fiber bundles of the peri-lesioned
region, by electrically-induced seizure (kindling) in brain, by UV
irradiation in skin and by incisional and chemically-induced skin
wounding which causes epidermal proliferation and hyperkeratosis.
Induced by chemically-induced oxidative stress which leads to
increased expression in the hippocampal pyramidal neurons 2 hours
after treatment. Levels then decrease, drop to 60% of pretreated
control levels at day 7 when avoidance learning is impaired and
return to control levels at day 30. Also induced by spinal crush
injury which leads to increased expression in spinal cord white
matter adjacent to the lesion. Expression increases between days
1-14 post-injury with a peak at day 4.
{ECO:0000269|PubMed:10196465, ECO:0000269|PubMed:10421059,
ECO:0000269|PubMed:11274744, ECO:0000269|PubMed:14616360,
ECO:0000269|PubMed:17629414, ECO:0000269|PubMed:8864305,
ECO:0000269|PubMed:9374276, ECO:0000269|PubMed:9749739}.
-!- MASS SPECTROMETRY: Mass=26613; Method=MALDI; Range=29-260;
Evidence={ECO:0000269|PubMed:9556608};
-!- MASS SPECTROMETRY: Mass=26229; Method=MALDI; Range=33-260;
Evidence={ECO:0000269|PubMed:9556608};
-!- DISRUPTION PHENOTYPE: Mice display marked abnormalities of
synapses and neurons in the CA1 subfield of the hippocampus with
enlarged and elongated pyramidal cell soma and reduced
asymmetrical synapse numbers. Mutants also display impaired
spatial memory acquisition, increased hippocampal susceptibility
to hyperexcitability in response to repetitive afferent
stimulation and prolonged recovery of UV-irradiated skin.
Following spinal cord injury, mutants display reduced
demyelination, oligodendrocyte death and axonal degeneration, and
inproved hind limb recovery, suggesting that attenuation of
neuropsin activity may be beneficial in the treatment of spinal
cord injury. Blocking of Klk8 activity by intraventricular
injection with monoclonal antibodies reduces or eliminates
epileptic seizures in kindled mice. {ECO:0000269|PubMed:11273653,
ECO:0000269|PubMed:11549709, ECO:0000269|PubMed:14616360,
ECO:0000269|PubMed:16308352, ECO:0000269|PubMed:16537644,
ECO:0000269|PubMed:17182622, ECO:0000269|PubMed:17629414}.
-!- SIMILARITY: Belongs to the peptidase S1 family. Kallikrein
subfamily. {ECO:0000255|PROSITE-ProRule:PRU00274}.
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EMBL; D30785; BAA06451.1; -; mRNA.
EMBL; AB032202; BAA92435.1; -; Genomic_DNA.
EMBL; BC055895; AAH55895.1; -; mRNA.
EMBL; AB074296; BAB92021.1; -; mRNA.
CCDS; CCDS21182.1; -.
PIR; I56559; I56559.
RefSeq; NP_001311327.1; NM_001324398.1.
RefSeq; NP_032966.1; NM_008940.3.
UniGene; Mm.458023; -.
PDB; 1NPM; X-ray; 2.10 A; A/B=33-257.
PDBsum; 1NPM; -.
ProteinModelPortal; Q61955; -.
SMR; Q61955; -.
STRING; 10090.ENSMUSP00000082588; -.
MEROPS; S01.244; -.
iPTMnet; Q61955; -.
PhosphoSitePlus; Q61955; -.
EPD; Q61955; -.
PaxDb; Q61955; -.
PRIDE; Q61955; -.
Ensembl; ENSMUST00000085461; ENSMUSP00000082588; ENSMUSG00000064023.
GeneID; 259277; -.
KEGG; mmu:259277; -.
UCSC; uc009gns.1; mouse.
CTD; 11202; -.
MGI; MGI:1343327; Klk8.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000118862; -.
HOGENOM; HOG000251820; -.
HOVERGEN; HBG013304; -.
InParanoid; Q61955; -.
KO; K08650; -.
OMA; FPQKKCE; -.
OrthoDB; EOG091G0DF7; -.
PhylomeDB; Q61955; -.
TreeFam; TF331065; -.
BRENDA; 3.4.21.118; 3474.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
EvolutionaryTrace; Q61955; -.
PRO; PR:Q61955; -.
Proteomes; UP000000589; Chromosome 7.
Bgee; ENSMUSG00000064023; -.
CleanEx; MM_KLK8; -.
ExpressionAtlas; Q61955; baseline and differential.
Genevisible; Q61955; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IMP:UniProtKB.
GO; GO:0043616; P:keratinocyte proliferation; IMP:UniProtKB.
GO; GO:0007613; P:memory; IMP:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; IMP:UniProtKB.
GO; GO:0031642; P:negative regulation of myelination; IMP:UniProtKB.
GO; GO:0048812; P:neuron projection morphogenesis; IDA:UniProtKB.
GO; GO:0050807; P:regulation of synapse organization; IMP:UniProtKB.
GO; GO:0009611; P:response to wounding; IDA:UniProtKB.
GO; GO:0050808; P:synapse organization; IMP:MGI.
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; Complete proteome; Cytoplasm; Direct protein sequencing;
Disulfide bond; Glycoprotein; Hydrolase; Protease; Reference proteome;
Secreted; Serine protease; Signal; Zymogen.
SIGNAL 1 28 {ECO:0000255}.
PROPEP 29 32 {ECO:0000269|PubMed:9556608}.
/FTId=PRO_0000027948.
CHAIN 33 260 Kallikrein-8.
/FTId=PRO_0000027949.
DOMAIN 33 257 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 73 73 Charge relay system. {ECO:0000250}.
ACT_SITE 120 120 Charge relay system. {ECO:0000250}.
ACT_SITE 212 212 Charge relay system. {ECO:0000250}.
CARBOHYD 110 110 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 39 173
DISULFID 58 74
DISULFID 145 246
DISULFID 152 218
DISULFID 184 198
DISULFID 208 233
STRAND 47 52 {ECO:0000244|PDB:1NPM}.
STRAND 55 64 {ECO:0000244|PDB:1NPM}.
STRAND 67 70 {ECO:0000244|PDB:1NPM}.
HELIX 72 74 {ECO:0000244|PDB:1NPM}.
STRAND 80 84 {ECO:0000244|PDB:1NPM}.
STRAND 96 98 {ECO:0000244|PDB:1NPM}.
STRAND 100 105 {ECO:0000244|PDB:1NPM}.
STRAND 122 128 {ECO:0000244|PDB:1NPM}.
STRAND 133 136 {ECO:0000244|PDB:1NPM}.
STRAND 151 158 {ECO:0000244|PDB:1NPM}.
STRAND 160 164 {ECO:0000244|PDB:1NPM}.
STRAND 172 178 {ECO:0000244|PDB:1NPM}.
HELIX 181 187 {ECO:0000244|PDB:1NPM}.
TURN 189 191 {ECO:0000244|PDB:1NPM}.
STRAND 196 200 {ECO:0000244|PDB:1NPM}.
STRAND 215 218 {ECO:0000244|PDB:1NPM}.
STRAND 221 228 {ECO:0000244|PDB:1NPM}.
STRAND 231 233 {ECO:0000244|PDB:1NPM}.
STRAND 240 244 {ECO:0000244|PDB:1NPM}.
HELIX 245 256 {ECO:0000244|PDB:1NPM}.
SEQUENCE 260 AA; 28524 MW; BE5F6F6BE37CD60E CRC64;
MGRPPPCAIQ PWILLLLFMG AWAGLTRAQG SKILEGRECI PHSQPWQAAL FQGERLICGG
VLVGDRWVLT AAHCKKQKYS VRLGDHSLQS RDQPEQEIQV AQSIQHPCYN NSNPEDHSHD
IMLIRLQNSA NLGDKVKPVQ LANLCPKVGQ KCIISGWGTV TSPQENFPNT LNCAEVKIYS
QNKCERAYPG KITEGMVCAG SSNGADTCQG DSGGPLVCDG MLQGITSWGS DPCGKPEKPG
VYTKICRYTT WIKKTMDNRD


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Y051559 Anti-Kallikrein-4 PRSS17 KLK-L1 enamel matrix serine protease EMPS1 Prostase; Kallikrein loop antibody 250ug
Y051559 Anti-Kallikrein-4 (PRSS17, KLK-L1, enamel matrix serine protease (EMPS1), Prostase); Kallikrein loop Antibody 100μg
30-381 PEBP1 binds ATP, opioids and phosphatidylethanolamine. It has lower affinity for phosphatidylinositol and phosphatidylcholine. It is also a serine protease inhibitor which inhibits thrombin, neuropsin 0.1 mg
EIAAB32605 Disp,Distal intestinal serine protease,Prss30,Rat,Rattus norvegicus,Serine protease 30,Tmprss8,Tmsp1,TMSP-1,Tmsp-1,Transmembrane serine protease 1,Transmembrane serine protease 8
EIAAB32606 Disp,Distal intestinal serine protease,Mouse,Mus musculus,Prss30,Serine protease 30,Tmprss8,Transmembrane serine protease 8
E0669h ELISA kit Hippostasin,hK11,Homo sapiens,Human,Kallikrein-11,KLK11,PRSS20,Serine protease 20,TLSP,Trypsin-like protease,UNQ649_PRO1279 96T
E0669h ELISA Hippostasin,hK11,Homo sapiens,Human,Kallikrein-11,KLK11,PRSS20,Serine protease 20,TLSP,Trypsin-like protease,UNQ649_PRO1279 96T
U0669h CLIA Hippostasin,hK11,Homo sapiens,Human,Kallikrein-11,KLK11,PRSS20,Serine protease 20,TLSP,Trypsin-like protease,UNQ649_PRO1279 96T
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
U2234h CLIA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA kit Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T
E2234h ELISA Homo sapiens,Human,Mannan-binding lectin serine protease 2,Mannose-binding protein-associated serine protease 2,MASP2,MASP-2,MBL-associated serine protease 2 96T


 

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