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Klotho (EC 3.2.1.31) [Cleaved into: Klotho peptide]

 KLOT_MOUSE              Reviewed;        1014 AA.
O35082; B2RR78; O70175; O70621;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
12-SEP-2018, entry version 145.
RecName: Full=Klotho;
EC=3.2.1.31;
Contains:
RecName: Full=Klotho peptide;
Flags: Precursor;
Name=Kl;
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] (ISOFORMS 1 AND 2), FUNCTION, TISSUE
SPECIFICITY, DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
TISSUE=Kidney;
PubMed=9363890; DOI=10.1038/36285;
Kuro-o M., Matsumura Y., Aizawa H., Kawaguchi H., Suga T., Utsugi T.,
Ohyama Y., Kurabayashi M., Kaname T., Kume E., Iwasaki H., Iida A.,
Shiraki-Iida T., Nishikawa S., Nagai R., Nabeshima Y.;
"Mutation of the mouse klotho gene leads to a syndrome resembling
ageing.";
Nature 390:45-51(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1
AND 2), AND TISSUE SPECIFICITY.
PubMed=9537505; DOI=10.1016/S0014-5793(98)00127-6;
Shiraki-Iida T., Aizawa H., Matsumura Y., Sekine S., Iida A.,
Anazawa H., Nagai R., Kuro-o M., Nabeshima Y.;
"Structure of the mouse klotho gene and its two transcripts encoding
membrane and secreted protein.";
FEBS Lett. 424:6-10(1998).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain;
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]
TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=10631108; DOI=10.1006/bbrc.1999.2009;
Kato Y., Arakawa E., Kinoshita S., Shirai A., Furuya A., Yamano K.,
Nakamura K., Iida A., Anazawa H., Koh N., Iwano A., Imura A.,
Fujimori T., Kuro-o M., Hanai N., Takeshige K., Nabeshima Y.;
"Establishment of the anti-Klotho monoclonal antibodies and detection
of Klotho protein in kidneys.";
Biochem. Biophys. Res. Commun. 267:597-602(2000).
[5]
FUNCTION, AND DISRUPTION PHENOTYPE.
PubMed=11095966; DOI=10.1006/bbrc.2000.3864;
Mori K., Yahata K., Mukoyama M., Suganami T., Makino H., Nagae T.,
Masuzaki H., Ogawa Y., Sugawara A., Nabeshima Y., Nakao K.;
"Disruption of klotho gene causes an abnormal energy homeostasis in
mice.";
Biochem. Biophys. Res. Commun. 278:665-670(2000).
[6]
FUNCTION.
PubMed=11016890; DOI=10.1053/meta.2000.8606;
Utsugi T., Ohno T., Ohyama Y., Uchiyama T., Saito Y., Matsumura Y.,
Aizawa H., Itoh H., Kurabayashi M., Kawazu S., Tomono S., Oka Y.,
Suga T., Kuro-o M., Nabeshima Y., Nagai R.;
"Decreased insulin production and increased insulin sensitivity in the
klotho mutant mouse, a novel animal model for human aging.";
Metabolism 49:1118-1123(2000).
[7]
INDUCTION, AND TISSUE SPECIFICITY.
PubMed=11411791; DOI=10.1016/S0024-3205(01)01092-X;
Mizuno I., Takahashi Y., Okimura Y., Kaji H., Chihara K.;
"Upregulation of the klotho gene expression by thyroid hormone and
during adipose differentiation in 3T3-L1 adipocytes.";
Life Sci. 68:2917-2923(2001).
[8]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=12204354; DOI=10.1016/S0378-5955(02)00483-5;
Kamemori M., Ohyama Y., Kurabayashi M., Takahashi K., Nagai R.,
Furuya N.;
"Expression of Klotho protein in the inner ear.";
Hear. Res. 171:103-110(2002).
[9]
FUNCTION, AND INDUCTION.
PubMed=14528024; DOI=10.1210/me.2003-0048;
Tsujikawa H., Kurotaki Y., Fujimori T., Fukuda K., Nabeshima Y.;
"Klotho, a gene related to a syndrome resembling human premature
aging, functions in a negative regulatory circuit of vitamin D
endocrine system.";
Mol. Endocrinol. 17:2393-2403(2003).
[10]
INDUCTION.
PubMed=15485693; DOI=10.1016/j.cardiores.2004.07.011;
Narumiya H., Sasaki S., Kuwahara N., Irie H., Kusaba T., Kameyama H.,
Tamagaki K., Hatta T., Takeda K., Matsubara H.;
"HMG-CoA reductase inhibitors up-regulate anti-aging klotho mRNA via
RhoA inactivation in IMCD3 cells.";
Cardiovasc. Res. 64:331-336(2004).
[11]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=15665504; DOI=10.1247/csf.29.91;
Li S.-A., Watanabe M., Yamada H., Nagai A., Kinuta M., Takei K.;
"Immunohistochemical localization of Klotho protein in brain, kidney,
and reproductive organs of mice.";
Cell Struct. Funct. 29:91-99(2004).
[12]
CLEAVAGE, TISSUE SPECIFICITY, SUBUNIT, GLYCOSYLATION, AND SUBCELLULAR
LOCATION.
PubMed=15135068; DOI=10.1016/j.febslet.2004.03.090;
Imura A., Iwano A., Tohyama O., Tsuji Y., Nozaki K., Hashimoto N.,
Fujimori T., Nabeshima Y.;
"Secreted Klotho protein in sera and CSF: implication for post-
translational cleavage in release of Klotho protein from cell
membrane.";
FEBS Lett. 565:143-147(2004).
[13]
ENZYME ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL
PROPERTIES.
PubMed=14701853; DOI=10.1074/jbc.M312392200;
Tohyama O., Imura A., Iwano A., Freund J.-N., Henrissat B.,
Fujimori T., Nabeshima Y.;
"Klotho is a novel beta-glucuronidase capable of hydrolyzing steroid
beta-glucuronides.";
J. Biol. Chem. 279:9777-9784(2004).
[14]
FUNCTION, LACK OF ENZYMATIC ACTIVITY, TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
PubMed=16123266; DOI=10.1126/science.1112766;
Kurosu H., Yamamoto M., Clark J.D., Pastor J.V., Nandi A., Gurnani P.,
McGuinness O.P., Chikuda H., Yamaguchi M., Kawaguchi H., Shimomura I.,
Takayama Y., Herz J., Kahn C.R., Rosenblatt K.P., Kuro-o M.;
"Suppression of aging in mice by the hormone Klotho.";
Science 309:1829-1833(2005).
[15]
FUNCTION, AND INTERACTION WITH FGF23 AND FGFR1.
PubMed=17086194; DOI=10.1038/nature05315;
Urakawa I., Yamazaki Y., Shimada T., Iijima K., Hasegawa H., Okawa K.,
Fujita T., Fukumoto S., Yamashita T.;
"Klotho converts canonical FGF receptor into a specific receptor for
FGF23.";
Nature 444:770-774(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
-!- FUNCTION: May have weak glycosidase activity towards
glucuronylated steroids. However, it lacks essential active site
Glu residues at positions 241 and 874, suggesting it may be
inactive as a glycosidase in vivo. May be involved in the
regulation of calcium and phosphorus homeostasis by inhibiting the
synthesis of active vitamin D. Essential factor for the specific
interaction between FGF23 and FGFR1.
-!- FUNCTION: The Klotho peptide generated by cleavage of the
membrane-bound isoform may be an anti-aging circulating hormone
which would extend life span by inhibiting insulin/IGF1 signaling.
-!- CATALYTIC ACTIVITY: A beta-D-glucuronoside + H(2)O = D-glucuronate
+ an alcohol. {ECO:0000269|PubMed:14701853}.
-!- ACTIVITY REGULATION: Inhibited by D-saccharic acid 1,4-lactone and
taurocholic acid. {ECO:0000269|PubMed:14701853}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.249 mM for 4-methylumbelliferylglucuronide
{ECO:0000269|PubMed:14701853};
KM=0.251 mM for estrone 3-beta-D-glucuronide
{ECO:0000269|PubMed:14701853};
KM=0.174 mM for beta-estradiol 3-beta-D-glucuronide
{ECO:0000269|PubMed:14701853};
KM=0.251 mM for estriol 3-beta-D-glucuronide
{ECO:0000269|PubMed:14701853};
Vmax=0.62 uM/h/ug enzyme {ECO:0000269|PubMed:14701853};
pH dependence:
Optimum pH is 5.5. {ECO:0000269|PubMed:14701853};
-!- SUBUNIT: Homodimer. Interacts with FGF23 and FGFR1.
{ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:17086194}.
-!- INTERACTION:
Q9GZV9:FGF23 (xeno); NbExp=5; IntAct=EBI-1570828, EBI-6594125;
P11362:FGFR1 (xeno); NbExp=2; IntAct=EBI-1570828, EBI-1028277;
P11362-7:FGFR1 (xeno); NbExp=3; IntAct=EBI-1570828, EBI-15609945;
P16092:Fgfr1; NbExp=2; IntAct=EBI-1570828, EBI-7953898;
Q61851-1:Fgfr3; NbExp=2; IntAct=EBI-1570828, EBI-15820536;
Q03142:Fgfr4; NbExp=2; IntAct=EBI-1570828, EBI-15633599;
P04426:Wnt1; NbExp=2; IntAct=EBI-1570828, EBI-1570911;
P17553:Wnt3; NbExp=4; IntAct=EBI-1570828, EBI-1570853;
P22724:Wnt4; NbExp=2; IntAct=EBI-1570828, EBI-1570945;
P22725:Wnt5a; NbExp=2; IntAct=EBI-1570828, EBI-1570983;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:12204354,
ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:9363890}; Single-
pass type I membrane protein {ECO:0000305|PubMed:9363890}. Apical
cell membrane {ECO:0000269|PubMed:15665504}; Single-pass type I
membrane protein {ECO:0000305|PubMed:15665504}. Note=Isoform 1
shedding leads to a soluble peptide.
{ECO:0000269|PubMed:16123266}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:10631108, ECO:0000269|PubMed:15135068}.
-!- SUBCELLULAR LOCATION: Klotho peptide: Secreted
{ECO:0000269|PubMed:16123266}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Membrane-bound;
IsoId=O35082-1; Sequence=Displayed;
Note=Predominates over the secreted form by more than 10 times
in all tissues examined.;
Name=2; Synonyms=Secreted;
IsoId=O35082-2; Sequence=VSP_015828, VSP_015829;
-!- TISSUE SPECIFICITY: Membrane-bound protein is present in distal
renal tubules, inner ear, ependymal cells of brain choroid plexus,
elongating spermatids and mature oocytes (at protein level).
Soluble peptide is present in serum (100 pM) and cerebrospinal
fluid. Expressed strongly in kidney, moderately in brain choroid
plexus, and at low levels in pituitary, placenta, skeletal muscle,
urinary bladder, aorta, pancreas, testis, ovary, colon, thyroid
gland and adipocytes. {ECO:0000269|PubMed:10631108,
ECO:0000269|PubMed:11411791, ECO:0000269|PubMed:12204354,
ECO:0000269|PubMed:15135068, ECO:0000269|PubMed:15665504,
ECO:0000269|PubMed:16123266, ECO:0000269|PubMed:9363890,
ECO:0000269|PubMed:9537505}.
-!- DEVELOPMENTAL STAGE: Not expressed in the embryo. Expressed in the
kidney of newborns. {ECO:0000269|PubMed:9363890}.
-!- INDUCTION: Induced by 1,25-dihydroxyvitamin D(3) in kidney. Down-
regulated by angiotensin II and up-regulated by statins through
modulation of the RhoA pathway in epithelial cells (in vitro).
Isoform 1 (but not isoform 2) is up-regulated by thyroid hormone
in adipocytes. {ECO:0000269|PubMed:11411791,
ECO:0000269|PubMed:14528024, ECO:0000269|PubMed:15485693}.
-!- DOMAIN: Contains 2 glycosyl hydrolase 1 regions. However, the
first region lacks the essential Glu active site residue at
position 241, and the second one lacks the essential Glu active
site residue at position 874.
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:15135068}.
-!- DISRUPTION PHENOTYPE: Mice display a syndrome resembling to human
aging, with short lifespan, infertility, atherosclerosis, skin
atrophy, osteoporosis and emphysema. They have various metabolic
abnormalities, including increased insulin sensitivity and
decreased insulin production. Mice overexpressing Kl have
increased resistance to insulin and IGF1, a lifespan extended of
more than 20%, and generate fewer offspring.
{ECO:0000269|PubMed:11095966}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 1 family. Klotho
subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=Protein Spotlight; Note=The thread of life
- Issue 65 of December 2005;
URL="https://web.expasy.org/spotlight/back_issues/065";
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EMBL; AB005141; BAA23381.1; -; mRNA.
EMBL; AB010088; BAA25307.1; -; mRNA.
EMBL; AB010091; BAA25308.1; -; Genomic_DNA.
EMBL; AB010091; BAA25309.1; -; Genomic_DNA.
EMBL; BC138258; AAI38259.1; -; mRNA.
EMBL; BC138259; AAI38260.1; -; mRNA.
CCDS; CCDS19889.1; -. [O35082-1]
RefSeq; NP_038851.2; NM_013823.2. [O35082-1]
UniGene; Mm.6500; -.
ProteinModelPortal; O35082; -.
SMR; O35082; -.
BioGrid; 200958; 5.
CORUM; O35082; -.
DIP; DIP-39894N; -.
IntAct; O35082; 10.
MINT; O35082; -.
STRING; 10090.ENSMUSP00000077899; -.
CAZy; GH1; Glycoside Hydrolase Family 1.
iPTMnet; O35082; -.
PhosphoSitePlus; O35082; -.
PaxDb; O35082; -.
PeptideAtlas; O35082; -.
PRIDE; O35082; -.
Ensembl; ENSMUST00000078856; ENSMUSP00000077899; ENSMUSG00000058488. [O35082-1]
GeneID; 16591; -.
KEGG; mmu:16591; -.
UCSC; uc009auk.2; mouse. [O35082-2]
UCSC; uc009aul.2; mouse. [O35082-1]
CTD; 9365; -.
MGI; MGI:1101771; Kl.
eggNOG; KOG0626; Eukaryota.
eggNOG; COG2723; LUCA.
GeneTree; ENSGT00550000074452; -.
HOGENOM; HOG000060126; -.
HOVERGEN; HBG081856; -.
InParanoid; O35082; -.
KO; K14756; -.
OMA; YYLKKFI; -.
OrthoDB; EOG091G0035; -.
TreeFam; TF314803; -.
Reactome; R-MMU-109704; PI3K Cascade.
Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
Reactome; R-MMU-190374; FGFR1c and Klotho ligand binding and activation.
Reactome; R-MMU-5654219; Phospholipase C-mediated cascade: FGFR1.
Reactome; R-MMU-5654687; Downstream signaling of activated FGFR1.
Reactome; R-MMU-5654688; SHC-mediated cascade:FGFR1.
Reactome; R-MMU-5654689; PI-3K cascade:FGFR1.
Reactome; R-MMU-5654693; FRS-mediated FGFR1 signaling.
Reactome; R-MMU-5654700; FRS-mediated FGFR2 signaling.
Reactome; R-MMU-5654706; FRS-mediated FGFR3 signaling.
Reactome; R-MMU-5654712; FRS-mediated FGFR4 signaling.
Reactome; R-MMU-5654726; Negative regulation of FGFR1 signaling.
Reactome; R-MMU-5673001; RAF/MAP kinase cascade.
Reactome; R-MMU-6811558; PI5P, PP2A and IER3 Regulate PI3K/AKT Signaling.
PRO; PR:O35082; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000058488; Expressed in 72 organ(s), highest expression level in kidney.
CleanEx; MM_KL; -.
Genevisible; O35082; MM.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; ISS:MGI.
GO; GO:0005615; C:extracellular space; IEA:InterPro.
GO; GO:0016021; C:integral component of membrane; ISS:MGI.
GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
GO; GO:0008422; F:beta-glucosidase activity; IBA:GO_Central.
GO; GO:0004566; F:beta-glucuronidase activity; IEA:UniProtKB-EC.
GO; GO:0017134; F:fibroblast growth factor binding; IPI:UniProtKB.
GO; GO:0005104; F:fibroblast growth factor receptor binding; IPI:UniProtKB.
GO; GO:0002526; P:acute inflammatory response; ISO:MGI.
GO; GO:0007568; P:aging; IMP:MGI.
GO; GO:0055074; P:calcium ion homeostasis; IGI:MGI.
GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
GO; GO:0006112; P:energy reserve metabolic process; IMP:MGI.
GO; GO:1901657; P:glycosyl compound metabolic process; IBA:GO_Central.
GO; GO:0008286; P:insulin receptor signaling pathway; IEA:InterPro.
GO; GO:0003085; P:negative regulation of systemic arterial blood pressure; ISO:MGI.
GO; GO:0042421; P:norepinephrine biosynthetic process; ISO:MGI.
GO; GO:0030501; P:positive regulation of bone mineralization; ISO:MGI.
GO; GO:0090080; P:positive regulation of MAPKKK cascade by fibroblast growth factor receptor signaling pathway; IGI:MGI.
InterPro; IPR001360; Glyco_hydro_1.
InterPro; IPR033132; Glyco_hydro_1_N_CS.
InterPro; IPR017853; Glycoside_hydrolase_SF.
InterPro; IPR028546; Klotho.
PANTHER; PTHR10353; PTHR10353; 6.
PANTHER; PTHR10353:SF10; PTHR10353:SF10; 6.
Pfam; PF00232; Glyco_hydro_1; 3.
PRINTS; PR00131; GLHYDRLASE1.
SUPFAM; SSF51445; SSF51445; 2.
PROSITE; PS00653; GLYCOSYL_HYDROL_F1_2; 1.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome; Glycoprotein;
Glycosidase; Hydrolase; Membrane; Reference proteome; Repeat;
Secreted; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 34 {ECO:0000255}.
CHAIN 35 1014 Klotho.
/FTId=PRO_0000042247.
CHAIN 35 ? Klotho peptide.
/FTId=PRO_0000042248.
TOPO_DOM 35 982 Extracellular. {ECO:0000255}.
TRANSMEM 983 1003 Helical. {ECO:0000255}.
TOPO_DOM 1004 1014 Cytoplasmic. {ECO:0000255}.
REGION 59 508 Glycosyl hydrolase-1 1.
REGION 517 955 Glycosyl hydrolase-1 2.
CARBOHYD 161 161 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 346 346 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 609 609 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 696 696 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 537 550 DTTLSQFTDPNVYL -> SPLTKPSVGLLLPH (in
isoform 2). {ECO:0000303|PubMed:9363890}.
/FTId=VSP_015828.
VAR_SEQ 551 1014 Missing (in isoform 2).
{ECO:0000303|PubMed:9363890}.
/FTId=VSP_015829.
CONFLICT 854 854 L -> V (in Ref. 2; BAA25308).
{ECO:0000305}.
CONFLICT 948 948 K -> R (in Ref. 1; BAA23381 and 2;
BAA25308). {ECO:0000305}.
SEQUENCE 1014 AA; 116398 MW; 24BD772A1F81B8EC CRC64;
MLARAPPRRP PRLVLLRLLL LHLLLLALRA RCLSAEPGQG AQTWARFARA PAPEAAGLLH
DTFPDGFLWA VGSAAYQTEG GWRQHGKGAS IWDTFTHHSG AAPSDSPIVV APSGAPSPPL
SSTGDVASDS YNNVYRDTEG LRELGVTHYR FSISWARVLP NGTAGTPNRE GLRYYRRLLE
RLRELGVQPV VTLYHWDLPQ RLQDTYGGWA NRALADHFRD YAELCFRHFG GQVKYWITID
NPYVVAWHGY ATGRLAPGVR GSSRLGYLVA HNLLLAHAKV WHLYNTSFRP TQGGRVSIAL
SSHWINPRRM TDYNIRECQK SLDFVLGWFA KPIFIDGDYP ESMKNNLSSL LPDFTESEKR
LIRGTADFFA LSFGPTLSFQ LLDPNMKFRQ LESPNLRQLL SWIDLEYNHP PIFIVENGWF
VSGTTKRDDA KYMYYLKKFI METLKAIRLD GVDVIGYTAW SLMDGFEWHR GYSIRRGLFY
VDFLSQDKEL LPKSSALFYQ KLIEDNGFPP LPENQPLEGT FPCDFAWGVV DNYVQVDTTL
SQFTDPNVYL WDVHHSKRLI KVDGVVAKKR KPYCVDFSAI RPQITLLREM RVTHFRFSLD
WALILPLGNQ TQVNHTVLHF YRCMISELVH ANITPVVALW QPAAPHQGLP HALAKHGAWE
NPHTALAFAD YANLCFKELG HWVNLWITMN EPNTRNMTYR AGHHLLRAHA LAWHLYDDKF
RAAQKGKISI ALQADWIEPA CPFSQNDKEV AERVLEFDIG WLAEPIFGSG DYPRVMRDWL
NQKNNFLLPY FTEDEKKLVR GSFDFLAVSH YTTILVDWEK EDPMKYNDYL EVQEMTDITW
LNSPSQVAVV PWGLRKVLNW LRFKYGDLPM YVTANGIDDD PHAEQDSLRI YYIKNYVNEA
LKAYVLDDIN LCGYFAYSLS DRSAPKSGFY RYAANQFEPK PSMKHYRKII DSNGFLGSGT
LGRFCPEEYT VCTECGFFQT RKSLLVFISF LVFTFIISLA LIFHYSKKGQ RSYK


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Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
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GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
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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
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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
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IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
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ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
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e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


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81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

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GENTAUR Italy
SRL IVA IT03841300167
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Fax 02 36 00 65 94
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