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Alkaline phosphatase, tissue-nonspecific isozyme (AP-TNAP) (TNSALP) (EC 3.1.3.1) (Alkaline phosphatase liver/bone/kidney isozyme)

 PPBT_HUMAN              Reviewed;         524 AA.
P05186; A1A4E7; B2RMP8; B7Z387; B7Z4Y6; O75090; Q2TAI7; Q59EJ7;
Q5BKZ5; Q5VTG5; Q6NZI8; Q8WU32; Q9UBK0;
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
21-JUN-2005, sequence version 4.
30-AUG-2017, entry version 205.
RecName: Full=Alkaline phosphatase, tissue-nonspecific isozyme;
Short=AP-TNAP;
Short=TNSALP;
EC=3.1.3.1 {ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064};
AltName: Full=Alkaline phosphatase liver/bone/kidney isozyme;
Flags: Precursor;
Name=ALPL;
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).
TISSUE=Osteosarcoma;
PubMed=3532105; DOI=10.1073/pnas.83.19.7182;
Weiss M.J., Henthorn P.S., Lafferty M.A., Slaughter C., Raducha M.,
Harris H.;
"Isolation and characterization of a cDNA encoding a human
liver/bone/kidney-type alkaline phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 83:7182-7186(1986).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Osteosarcoma;
PubMed=3165380;
Weiss M.J., Ray K., Henthorn P.S., Lamb B., Kadesch T., Harris H.;
"Structure of the human liver/bone/kidney alkaline phosphatase gene.";
J. Biol. Chem. 263:12002-12010(1988).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HIS-263.
TISSUE=Liver;
PubMed=2928120; DOI=10.1093/nar/17.5.2129;
Kishi F., Matsuura S., Kajii T.;
"Nucleotide sequence of the human liver-type alkaline phosphatase
cDNA.";
Nucleic Acids Res. 17:2129-2129(1989).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT HOPS PHE-289.
PubMed=9747027; DOI=10.1007/s100380050061;
Sugimoto N., Iwamoto S., Hoshino Y., Kajii E.;
"A novel missense mutation of the tissue-nonspecific alkaline
phosphatase gene detected in a patient with hypophosphatasia.";
J. Hum. Genet. 43:160-164(1998).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
TISSUE=Hippocampus;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-152.
TISSUE=Brain;
Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
Ohara O., Nagase T., Kikuno R.F.;
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton 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]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
HIS-263.
TISSUE=Brain, Cerebellum, Lymphoma, and Peripheral nerve;
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).
[10]
PROTEIN SEQUENCE OF 18-49.
TISSUE=Liver;
PubMed=3954357; DOI=10.1016/0003-9861(86)90223-7;
Garattini E., Hua J.-C., Pan Y.C.E., Udenfriend S.;
"Human liver alkaline phosphatase, purification and partial
sequencing: homology with the placental isozyme.";
Arch. Biochem. Biophys. 245:331-337(1986).
[11]
PROTEIN SEQUENCE OF 18-32, AND GLYCOSYLATION.
PubMed=1458595;
Nishihara Y., Hayashi Y., Adachi T., Koyama I., Stigbrand T.,
Hirano K.;
"Chemical nature of intestinal-type alkaline phosphatase in human
kidney.";
Clin. Chem. 38:2539-2542(1992).
[12]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=14517339; DOI=10.1074/mcp.M300079-MCP200;
Elortza F., Nuehse T.S., Foster L.J., Stensballe A., Peck S.C.,
Jensen O.N.;
"Proteomic analysis of glycosylphosphatidylinositol-anchored membrane
proteins.";
Mol. Cell. Proteomics 2:1261-1270(2003).
[13]
GPI-ANCHOR [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16602701; DOI=10.1021/pr050419u;
Elortza F., Mohammed S., Bunkenborg J., Foster L.J., Nuehse T.S.,
Brodbeck U., Peck S.C., Jensen O.N.;
"Modification-specific proteomics of plasma membrane proteins:
identification and characterization of glycosylphosphatidylinositol-
anchored proteins released upon phospholipase D treatment.";
J. Proteome Res. 5:935-943(2006).
[14]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-430.
TISSUE=Liver;
PubMed=19159218; DOI=10.1021/pr8008012;
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
"Glycoproteomics analysis of human liver tissue by combination of
multiple enzyme digestion and hydrazide chemistry.";
J. Proteome Res. 8:651-661(2009).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[16]
VARIANT HOPS THR-179.
PubMed=3174660; DOI=10.1073/pnas.85.20.7666;
Weiss M.J., Cole D.E.C., Ray K., Whyte M.P., Lafferty M.A.,
Mulivor R.A., Harris H.;
"A missense mutation in the human liver/bone/kidney alkaline
phosphatase gene causing a lethal form of hypophosphatasia.";
Proc. Natl. Acad. Sci. U.S.A. 85:7666-7669(1988).
[17]
VARIANTS HOPS VAL-33; CYS-71; PRO-71; LYS-191; PRO-207; ALA-294;
VAL-378 AND HIS-436, AND VARIANT HIS-263.
PubMed=1409720; DOI=10.1073/pnas.89.20.9924;
Henthorn P.S., Raducha M., Fedde K.N., Lafferty M.A., Whyte M.P.;
"Different missense mutations at the tissue-nonspecific alkaline
phosphatase gene locus in autosomal recessively inherited forms of
mild and severe hypophosphatasia.";
Proc. Natl. Acad. Sci. U.S.A. 89:9924-9928(1992).
[18]
VARIANT HOPS ASP-334.
PubMed=8406453; DOI=10.1006/geno.1993.1305;
Greenberg C.R., Taylor C.L., Haworth J.C., Seargeant L.E.,
Philipps S., Triggs-Raine B., Chodirker B.N.;
"A homoallelic Gly317-->Asp mutation in ALPL causes the perinatal
(lethal) form of hypophosphatasia in Canadian mennonites.";
Genomics 17:215-217(1993).
[19]
INVOLVEMENT IN HOPSI, AND VARIANT HOPSI LYS-298.
PubMed=7833929; DOI=10.1093/hmg/3.9.1683;
Orimo H., Hayashi Z., Watanabe A., Hirayama T., Hirayama T.,
Shimada T.;
"Novel missense and frameshift mutations in the tissue-nonspecific
alkaline phosphatase gene in a Japanese patient with
hypophosphatasia.";
Hum. Mol. Genet. 3:1683-1684(1994).
[20]
INVOLVEMENT IN HOPSI, AND VARIANTS HOPSI LEU-327 AND ARG-456.
PubMed=8954059; DOI=10.1210/jcem.81.12.8954059;
Ozono K., Yamagata M., Michigami T., Nakajima S., Sakai N., Cai G.,
Satomura K., Yasui N., Okada S., Nakayama M.;
"Identification of novel missense mutations (Phe310Leu and Gly439Arg)
in a neonatal case of hypophosphatasia.";
J. Clin. Endocrinol. Metab. 81:4458-4461(1996).
[21]
VARIANTS HOPS PHE-17; VAL-40; SER-75; ARG-120; ARG-129; ASP-170;
TRP-184; LYS-191; TRP-223; LYS-291; ASP-334; PRO-445; CYS-450; SER-473
AND ARG-491, AND VARIANT HIS-263.
PubMed=9781036; DOI=10.1038/sj.ejhg.5200190;
Mornet E., Taillandier A., Peyramaure S., Kaper F., Muller F.,
Brenner R., Bussiere P., Freisinger P., Godard J., Le Merrer M.,
Oury J.F., Plauchu H., Puddu R., Rival J.M., Superti-Furga A.,
Touraine R.L., Serre J.L., Simon-Bouy B.;
"Identification of fifteen novel mutations in the tissue-nonspecific
alkaline phosphatase (TNSALP) gene in European patients with severe
hypophosphatasia.";
Eur. J. Hum. Genet. 6:308-314(1998).
[22]
VARIANTS HOPS THR-111; THR-177; GLY-191; LEU-327 AND ILE-382.
PubMed=9452105;
Goseki-Sone M., Orimo H., Iimura T., Takagi Y., Watanabe H.,
Taketa K., Sato S., Mayanagi H., Shimada T., Oida S.;
"Hypophosphatasia: identification of five novel missense mutations
(G507A, G705A, A748G, T1155C, G1320A) in the tissue-nonspecific
alkaline phosphatase gene among Japanese patients.";
Hum. Mutat. Suppl. 1:S263-S267(1998).
[23]
VARIANTS HOPS VAL-40; LEU-62; SER-75; THR-111; ARG-120; ARG-129;
HIS-136; VAL-162; ASP-170; TYR-171; TRP-184; LYS-191; TRP-223;
VAL-249; LYS-291; VAL-306; ASP-334; CYS-391; PRO-445; CYS-450;
SER-473; LYS-476 AND ARG-491, 3D-STRUCTURE MODELING, AND
CHARACTERIZATION OF VARIANTS.
PubMed=10332035; DOI=10.1093/hmg/8.6.1039;
Zurutuza L., Muller F., Gibrat J.F., Taillandier A., Simon-Bouy B.,
Serre J.L., Mornet E.;
"Correlations of genotype and phenotype in hypophosphatasia.";
Hum. Mol. Genet. 8:1039-1046(1999).
[24]
VARIANTS HOPS LEU-62; HIS-136; VAL-162; TYR-171; LYS-191; TYR-201;
VAL-249; VAL-306 AND LYS-476.
PubMed=10094560;
DOI=10.1002/(SICI)1098-1004(1999)13:2<171::AID-HUMU16>3.0.CO;2-T;
Taillandier A., Zurutuza L., Muller F., Simon-Bouy B., Serre J.L.,
Bird L., Brenner R., Boute O., Cousin J., Gaillard D., Heidemann P.H.,
Steinmann B., Wallot M., Mornet E.;
"Characterization of eleven novel mutations (M45L, R119H, 544delG,
G145V, H154Y, C184Y, D289V, 862+5A, 1172delC, R411X, E459K) in the
tissue-nonspecific alkaline phosphatase (TNSALP) gene in patients with
severe hypophosphatasia.";
Hum. Mutat. 13:171-172(1999).
[25]
VARIANTS HOPSI GLU-224 AND CYS-426.
PubMed=10834525; DOI=10.1007/s004310051290;
Mochizuki H., Saito M., Michigami T., Ohashi H., Koda N.,
Yamaguchi S., Ozono K.;
"Severe hypercalcaemia and respiratory insufficiency associated with
infantile hypophosphatasia caused by two novel mutations of the
tissue-nonspecific alkaline phosphatase gene.";
Eur. J. Pediatr. 159:375-379(2000).
[26]
VARIANTS HOPS VAL-40; THR-111; ASN-134; THR-176; LYS-191; TYR-201;
SER-246; THR-348; ARG-381; GLY-406; HIS-450; ILE-478 AND SER-489.
PubMed=10679946;
DOI=10.1002/(SICI)1098-1004(200003)15:3<293::AID-HUMU11>3.0.CO;2-Q;
Taillandier A., Cozien E., Muller F., Merrien Y., Bonnin E.,
Fribourg C., Simon-Bouy B., Serre J.L., Bieth E., Brenner R.,
Cordier M.P., De Bie S., Fellmann F., Freisinger P., Hesse V.,
Hennekam R.C.M., Josifova D., Kerzin-Storrar L., Leporrier N.,
Zabot M.-T., Mornet E.;
"Fifteen new mutations (-195C>T, L-12X, 298-2A>G, T117N, A159T, R229S,
997+2T>A, E274X, A331T, H364R, D389G, 1256delC, R433H, N461I, C472S)
in the tissue-nonspecific alkaline phosphatase (TNSALP) gene in
patients with hypophosphatasia.";
Hum. Mutat. 15:293-293(2000).
[27]
VARIANT HOPS VAL-378, AND VARIANT ALA-522.
PubMed=10690885; DOI=10.1210/jcem.85.2.6373;
Mueller H.L., Yamazaki M., Michigami T., Kageyama T., Schoenau E.,
Schneider P., Ozono K.;
"Asp361Val mutant of alkaline phosphatase found in patients with
dominantly inherited hypophosphatasia inhibits the activity of the
wild-type enzyme.";
J. Clin. Endocrinol. Metab. 85:743-747(2000).
[28]
VARIANT HOPS SER-417.
PubMed=11745997; DOI=10.1002/ajmg.1541.abs;
Sergi C., Mornet E., Troeger J., Voigtlaender T.;
"Perinatal hypophosphatasia: radiology, pathology and molecular
biology studies in a family harboring a splicing mutation (648+1A) and
a novel missense mutation (N400S) in the tissue-nonspecific alkaline
phosphatase (TNSALP) gene.";
Am. J. Med. Genet. 103:235-240(2001).
[29]
CHARACTERIZATION OF VARIANTS HOPS VAL-40; VAL-63; THR-116; LEU-181;
TRP-184; TRP-223; VAL-249; VAL-378; ILE-478 AND PHE-490.
PubMed=11479741; DOI=10.1007/s004390100546;
Lia-Baldini A.S., Muller F., Taillandier A., Gibrat J.F., Mouchard M.,
Robin B., Simon-Bouy B., Serre J.L., Aylsworth A.S., Bieth E.,
Delanote S., Freisinger P., Hu J.C.-C., Krohn H.-P., Nunes M.E.,
Mornet E.;
"A molecular approach to dominance in hypophosphatasia.";
Hum. Genet. 109:99-108(2001).
[30]
VARIANTS HOPSI CYS-28 AND MET-459, AND VARIANTS HOPS VAL-40; VAL-51;
HIS-71; THR-116; HIS-136; HIS-152; THR-176; THR-179; LYS-191; ASP-211;
VAL-220; GLY-235; TYR-294; GLY-327; SER-399 AND ALA-423.
PubMed=11438998; DOI=10.1002/humu.1154;
Taillandier A., Lia-Baldini A.S., Mouchard M., Robin B., Muller F.,
Simon-Bouy B., Serre J.L., Bera-Louville A., Bonduelle M.,
Eckhardt J., Gaillard D., Myhre A.G., Koertge-Jung S., Larget-Piet L.,
Malou E., Sillence D., Temple I.K., Viot G., Mornet E.;
"Twelve novel mutations in the tissue-nonspecific alkaline phosphatase
gene (ALPL) in patients with various forms of hypophosphatasia.";
Hum. Mutat. 18:83-84(2001).
[31]
INVOLVEMENT IN HOPSC, VARIANTS HOPSC MET-68; SER-71; THR-177; TRP-223;
PRO-275 AND HIS-391, CHARACTERIZATION OF VARIANTS HOPSC MET-68;
SER-71; THR-177; TRP-223; PRO-275 AND HIS-391, VARIANT ALA-522, AND
CHARACTERIZATION OF VARIANT ALA-522.
PubMed=11760847; DOI=10.1359/jbmr.2001.16.12.2313;
Orimo H., Girschick H.J., Goseki-Sone M., Ito M., Oda K., Shimada T.;
"Mutational analysis and functional correlation with phenotype in
German patients with childhood-type hypophosphatasia.";
J. Bone Miner. Res. 16:2313-2319(2001).
[32]
VARIANT HOPS VAL-132.
PubMed=11834095; DOI=10.1034/j.1601-0825.2001.00740.x;
Watanabe H., Hashimoto-Uoshima M., Goseki-Sone M., Orimo H.,
Ishikawa I.;
"A novel point mutation (C571T) in the tissue-non-specific alkaline
phosphatase gene in a case of adult-type hypophosphatasia.";
Oral Dis. 7:331-335(2001).
[33]
VARIANTS HOPS LYS-291 AND ARG-326.
PubMed=11999978; DOI=10.1023/A:1015121414782;
Litmanovitz I., Reish O., Dolfin T., Arnon S., Regev R., Grinshpan G.,
Yamazaki M., Ozono K.;
"Glu274Lys/Gly309Arg mutation of the tissue-nonspecific alkaline
phosphatase gene in neonatal hypophosphatasia associated with
convulsions.";
J. Inherit. Metab. Dis. 25:35-40(2002).
[34]
VARIANTS HOPS SER-51; HIS-71; THR-111; MET-128; HIS-134; HIS-136;
THR-176; LYS-191; GLN-223; TRP-223; SER-246; ALA-294; PRO-299; PHE-327
DEL; ARG-339; THR-348; VAL-378; MET-414; ASP-426 AND LYS-476, AND
VARIANTS HIS-263 AND ALA-522.
PubMed=11855933; DOI=10.1006/mgme.2001.3283;
Mumm S., Jones J., Finnegan P., Henthorn P.S., Podgornik M.N.,
Whyte M.P.;
"Denaturing gradient gel electrophoresis analysis of the tissue
nonspecific alkaline phosphatase isoenzyme gene in hypophosphatasia.";
Mol. Genet. Metab. 75:143-153(2002).
[35]
VARIANTS HOPS VAL-62; ARG-63; THR-111; ILE-148; SER-162; GLU-189;
ALA-220; LEU-272; GLY-293-294-ASP DEL; LYS-311; LYS-452 AND THR-468.
PubMed=12815606; DOI=10.1002/humu.9159;
Spentchian M., Merrien Y., Herasse M., Dobbie Z., Glaeser D.,
Holder S.E., Ivarsson S.-A., Kostiner D., Mansour S., Norman A.,
Roth J., Stipoljev F., Taillemite J.-L., van der Smagt J.J.,
Serre J.-L., Simon-Bouy B., Taillandier A., Mornet E.;
"Severe hypophosphatasia: characterization of fifteen novel mutations
in the ALPL gene.";
Hum. Mutat. 22:105-106(2003).
[36]
VARIANTS HOPS LEU-108; THR-116 AND MET-414, AND CHARACTERIZATION OF
VARIANT HOPS LEU-108.
PubMed=12920074; DOI=10.1136/jmg.40.8.605;
Herasse M., Spentchian M., Taillandier A., Keppler-Noreuil K.,
Fliorito A.N.M., Bergoffen J., Wallerstein R., Muti C., Simon-Bouy B.,
Mornet E.;
"Molecular study of three cases of odontohypophosphatasia resulting
from heterozygosity for mutations in the tissue non-specific alkaline
phosphatase gene.";
J. Med. Genet. 40:605-609(2003).
[37]
VARIANT HOPS GLY-114.
PubMed=15135428; DOI=10.1016/j.arcped.2004.02.018;
Draguet C., Gillerot Y., Mornet E.;
"Childhood hypophosphatasia: a case report due to a novel mutation.";
Arch. Pediatr. 11:440-443(2004).
[38]
VARIANTS HOPS VAL-33; HIS-136; GLN-223; TRP-223; HIS-272; THR-292;
ALA-294; THR-295; ASP-297; ASP-334 AND ALA-411, AND CHARACTERIZATION
OF VARIANTS HOPS VAL-33; HIS-272; THR-292; THR-295; ASP-297 AND
ALA-411.
PubMed=15694177; DOI=10.1016/j.ymgme.2004.11.003;
Brun-Heath I., Taillandier A., Serre J.-L., Mornet E.;
"Characterization of 11 novel mutations in the tissue non-specific
alkaline phosphatase gene responsible for hypophosphatasia and
genotype-phenotype correlations.";
Mol. Genet. Metab. 84:273-277(2005).
[39]
VARIANTS HOPS CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334;
ASP-334; ARG-339; ILE-382; CYS-391; HIS-391; MET-414; ALA-420;
LYS-452; LEU-459 AND ALA-476, AND CHARACTERIZATION OF VARIANTS HOPS
CYS-71; HIS-71; THR-111; THR-176; LYS-191; ARG-334; ASP-334; ARG-339;
ILE-382; CYS-391; HIS-391; MET-414; LYS-452; LEU-459 AND ALA-476.
PubMed=19500388; DOI=10.1186/1471-2350-10-51;
Fauvert D., Brun-Heath I., Lia-Baldini A.S., Bellazi L.,
Taillandier A., Serre J.L., de Mazancourt P., Mornet E.;
"Mild forms of hypophosphatasia mostly result from dominant negative
effect of severe alleles or from compound heterozygosity for severe
and moderate alleles.";
BMC Med. Genet. 10:51-51(2009).
[40]
VARIANTS HOPS TYR-201 AND SER-489, AND CHARACTERIZATION OF VARIANTS
HOPS TYR-201 AND SER-489.
PubMed=22266140; DOI=10.1016/j.bbadis.2012.01.007;
Satou Y., Al-Shawafi H.A., Sultana S., Makita S., Sohda M., Oda K.;
"Disulfide bonds are critical for tissue-nonspecific alkaline
phosphatase function revealed by analysis of mutant proteins bearing a
C(201)-Y or C(489)-S substitution associated with severe
hypophosphatasia.";
Biochim. Biophys. Acta 1822:581-588(2012).
[41]
CHARACTERIZATION OF VARIANTS HOPS SER-420 AND ALA-420.
PubMed=23039266; DOI=10.1111/febs.12022;
Makita S., Al-Shawafi H.A., Sultana S., Sohda M., Nomura S., Oda K.;
"A dimerization defect caused by a glycine substitution at position
420 by serine in tissue-nonspecific alkaline phosphatase associated
with perinatal hypophosphatasia.";
FEBS J. 279:4327-4337(2012).
[42]
CHARACTERIZATION OF VARIANT HOPS SER-417, SUBUNIT, SUBCELLULAR
LOCATION, AND CATALYTIC ACTIVITY.
PubMed=23688511; DOI=10.1016/j.ymgme.2013.04.016;
Sultana S., Al-Shawafi H.A., Makita S., Sohda M., Amizuka N.,
Takagi R., Oda K.;
"An asparagine at position 417 of tissue-nonspecific alkaline
phosphatase is essential for its structure and function as revealed by
analysis of the N417S mutation associated with severe
hypophosphatasia.";
Mol. Genet. Metab. 109:282-288(2013).
[43]
CHARACTERIZATION OF VARIANT HOPS LEU-108, SUBCELLULAR LOCATION,
SUBUNIT, AND CATALYTIC ACTIVITY.
PubMed=25982064; DOI=10.1016/j.ymgme.2015.05.006;
Numa-Kinjoh N., Komaru K., Ishida Y., Sohda M., Oda K.;
"Molecular phenotype of tissue-nonspecific alkaline phosphatase with a
proline (108) to leucine substitution associated with dominant
odontohypophosphatasia.";
Mol. Genet. Metab. 115:180-185(2015).
-!- FUNCTION: This isozyme may play a role in skeletal mineralization.
-!- CATALYTIC ACTIVITY: A phosphate monoester + H(2)O = an alcohol +
phosphate. {ECO:0000255|PROSITE-ProRule:PRU10042,
ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000250|UniProtKB:P05187};
Note=Binds 1 Mg(2+) ion. {ECO:0000250|UniProtKB:P05187};
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:P05187};
Note=Binds 2 Zn(2+) ions. {ECO:0000250|UniProtKB:P05187};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23688511,
ECO:0000269|PubMed:25982064}.
-!- INTERACTION:
Q99558:MAP3K14; NbExp=4; IntAct=EBI-1054354, EBI-358011;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23688511,
ECO:0000269|PubMed:25982064}; Lipid-anchor, GPI-anchor
{ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=P05186-1; Sequence=Displayed;
Name=2;
IsoId=P05186-2; Sequence=VSP_042711;
Note=No experimental confirmation available.;
Name=3;
IsoId=P05186-3; Sequence=VSP_044228;
-!- PTM: N-glycosylated. {ECO:0000269|PubMed:1458595,
ECO:0000269|PubMed:19159218}.
-!- DISEASE: Hypophosphatasia (HOPS) [MIM:146300]: A metabolic bone
disease characterized by defective skeletal mineralization and
biochemically by deficient activity of the tissue non-specific
isoenzyme of alkaline phosphatase. Four forms are distinguished,
depending on the age of onset: perinatal, infantile, childhood and
adult type. The perinatal form is the most severe and is almost
always fatal. The adult form is mild and characterized by
recurrent fractures, osteomalacia, rickets, and loss of teeth.
Some cases are asymptomatic, while some patients manifest dental
features without skeletal manifestations (odontohypophosphatasia).
{ECO:0000269|PubMed:10094560, ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:10679946, ECO:0000269|PubMed:10690885,
ECO:0000269|PubMed:10834525, ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11479741, ECO:0000269|PubMed:11745997,
ECO:0000269|PubMed:11760847, ECO:0000269|PubMed:11834095,
ECO:0000269|PubMed:11855933, ECO:0000269|PubMed:11999978,
ECO:0000269|PubMed:12815606, ECO:0000269|PubMed:12920074,
ECO:0000269|PubMed:1409720, ECO:0000269|PubMed:15135428,
ECO:0000269|PubMed:15694177, ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:22266140, ECO:0000269|PubMed:23039266,
ECO:0000269|PubMed:23688511, ECO:0000269|PubMed:25982064,
ECO:0000269|PubMed:3174660, ECO:0000269|PubMed:7833929,
ECO:0000269|PubMed:8406453, ECO:0000269|PubMed:8954059,
ECO:0000269|PubMed:9452105, ECO:0000269|PubMed:9747027,
ECO:0000269|PubMed:9781036}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Hypophosphatasia childhood type (HOPSC) [MIM:241510]: A
bone disease characterized by defective skeletal mineralization
and biochemically by deficient activity of the tissue non-specific
isoenzyme of alkaline phosphatase. {ECO:0000269|PubMed:11760847}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Hypophosphatasia infantile type (HOPSI) [MIM:241500]: A
severe bone disease characterized by defective skeletal
mineralization and biochemically by deficient activity of the
tissue non-specific isoenzyme of alkaline phosphatase. Three more
or less distinct types of infantile hypophosphatasia can be
identified: (1) type 1 with onset in utero or in early postnatal
life, craniostenosis, severe skeletal abnormalities,
hypercalcemia, and death in the first year or so of life; (2) type
2 with later, more gradual development of symptoms, moderately
severe 'rachitic' skeletal changes and premature loss of teeth;
(3) type 3 with no symptoms, the condition being determined on
routine studies. {ECO:0000269|PubMed:10834525,
ECO:0000269|PubMed:11438998, ECO:0000269|PubMed:7833929,
ECO:0000269|PubMed:8954059}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the alkaline phosphatase family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAD93051.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=ALPL; Note=Tissue nonspecific alkaline
phosphatase gene mutations database;
URL="http://www.sesep.uvsq.fr/Database.html";
-!- WEB RESOURCE: Name=Wikipedia; Note=Alkaline phosphatase entry;
URL="https://en.wikipedia.org/wiki/Alkaline_phosphatase";
-----------------------------------------------------------------------
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EMBL; M24439; AAB59378.1; -; Genomic_DNA.
EMBL; M24429; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24430; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24431; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24432; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24433; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24434; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24435; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24436; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24437; AAB59378.1; JOINED; Genomic_DNA.
EMBL; M24438; AAB59378.1; JOINED; Genomic_DNA.
EMBL; X14174; CAA32376.1; -; mRNA.
EMBL; AB011406; BAA32129.1; -; mRNA.
EMBL; AK295608; BAH12123.1; -; mRNA.
EMBL; AK298085; BAH12722.1; -; mRNA.
EMBL; AB209814; BAD93051.1; ALT_INIT; mRNA.
EMBL; AL592309; CAH72079.1; -; Genomic_DNA.
EMBL; AL359815; CAH72079.1; JOINED; Genomic_DNA.
EMBL; AL359815; CAI16259.1; -; Genomic_DNA.
EMBL; AL592309; CAI16259.1; JOINED; Genomic_DNA.
EMBL; CH471134; EAW94977.1; -; Genomic_DNA.
EMBL; BC021289; AAH21289.3; -; mRNA.
EMBL; BC066116; AAH66116.2; -; mRNA.
EMBL; BC090861; AAH90861.2; -; mRNA.
EMBL; BC110909; AAI10910.2; -; mRNA.
EMBL; BC126165; AAI26166.1; -; mRNA.
EMBL; BC136325; AAI36326.1; -; mRNA.
CCDS; CCDS217.1; -. [P05186-1]
CCDS; CCDS53274.1; -. [P05186-2]
CCDS; CCDS53275.1; -. [P05186-3]
PIR; S03613; PAHUH.
RefSeq; NP_000469.3; NM_000478.5. [P05186-1]
RefSeq; NP_001120973.2; NM_001127501.3. [P05186-3]
RefSeq; NP_001170991.1; NM_001177520.2. [P05186-2]
RefSeq; XP_005245875.1; XM_005245818.1. [P05186-1]
RefSeq; XP_006710609.1; XM_006710546.2. [P05186-1]
UniGene; Hs.75431; -.
ProteinModelPortal; P05186; -.
SMR; P05186; -.
BioGrid; 106750; 7.
IntAct; P05186; 6.
STRING; 9606.ENSP00000363965; -.
BindingDB; P05186; -.
ChEMBL; CHEMBL5979; -.
DrugBank; DB01143; Amifostine.
DrugBank; DB06716; Fospropofol.
DEPOD; P05186; -.
iPTMnet; P05186; -.
PhosphoSitePlus; P05186; -.
BioMuta; ALPL; -.
DMDM; 68067533; -.
EPD; P05186; -.
MaxQB; P05186; -.
PaxDb; P05186; -.
PeptideAtlas; P05186; -.
PRIDE; P05186; -.
DNASU; 249; -.
Ensembl; ENST00000374832; ENSP00000363965; ENSG00000162551. [P05186-1]
Ensembl; ENST00000374840; ENSP00000363973; ENSG00000162551. [P05186-1]
Ensembl; ENST00000539907; ENSP00000437674; ENSG00000162551. [P05186-2]
Ensembl; ENST00000540617; ENSP00000442672; ENSG00000162551. [P05186-3]
GeneID; 249; -.
KEGG; hsa:249; -.
UCSC; uc001bet.4; human. [P05186-1]
CTD; 249; -.
DisGeNET; 249; -.
GeneCards; ALPL; -.
GeneReviews; ALPL; -.
HGNC; HGNC:438; ALPL.
HPA; CAB020829; -.
HPA; HPA007105; -.
HPA; HPA008765; -.
MalaCards; ALPL; -.
MIM; 146300; phenotype.
MIM; 171760; gene.
MIM; 241500; phenotype.
MIM; 241510; phenotype.
neXtProt; NX_P05186; -.
OpenTargets; ENSG00000162551; -.
Orphanet; 247676; Adult hypophosphatasia.
Orphanet; 247667; Childhood-onset hypophosphatasia.
Orphanet; 247651; Infantile hypophosphatasia.
Orphanet; 247685; Odontohypophosphatasia.
Orphanet; 247623; Perinatal lethal hypophosphatasia.
Orphanet; 247638; Prenatal benign hypophosphatasia.
PharmGKB; PA24729; -.
eggNOG; KOG4126; Eukaryota.
eggNOG; COG1785; LUCA.
GeneTree; ENSGT00390000008704; -.
HOVERGEN; HBG007345; -.
InParanoid; P05186; -.
KO; K01077; -.
OMA; EHTGTQL; -.
OrthoDB; EOG091G067H; -.
PhylomeDB; P05186; -.
TreeFam; TF323513; -.
BRENDA; 3.1.3.1; 2681.
Reactome; R-HSA-163125; Post-translational modification: synthesis of GPI-anchored proteins.
SABIO-RK; P05186; -.
SIGNOR; P05186; -.
ChiTaRS; ALPL; human.
GeneWiki; ALPL; -.
GenomeRNAi; 249; -.
PRO; PR:P05186; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000162551; -.
ExpressionAtlas; P05186; baseline and differential.
Genevisible; P05186; HS.
GO; GO:0031225; C:anchored component of membrane; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0065010; C:extracellular membrane-bounded organelle; IEA:Ensembl.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005578; C:proteinaceous extracellular matrix; IEA:Ensembl.
GO; GO:0004035; F:alkaline phosphatase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0016462; F:pyrophosphatase activity; IDA:MGI.
GO; GO:0006501; P:C-terminal protein lipidation; TAS:Reactome.
GO; GO:0071407; P:cellular response to organic cyclic compound; IEA:Ensembl.
GO; GO:0071529; P:cementum mineralization; IEA:Ensembl.
GO; GO:0003006; P:developmental process involved in reproduction; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0001649; P:osteoblast differentiation; IDA:UniProtKB.
GO; GO:0046677; P:response to antibiotic; IEA:Ensembl.
GO; GO:0051384; P:response to glucocorticoid; IEA:Ensembl.
GO; GO:0032496; P:response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0033280; P:response to vitamin D; IEP:BHF-UCL.
GO; GO:0001501; P:skeletal system development; TAS:ProtInc.
CDD; cd16012; ALP; 1.
Gene3D; 3.40.720.10; -; 1.
InterPro; IPR017849; Alkaline_Pase-like_a/b/a.
InterPro; IPR001952; Alkaline_phosphatase.
InterPro; IPR018299; Alkaline_phosphatase_AS.
InterPro; IPR017850; Alkaline_phosphatase_core.
PANTHER; PTHR11596; PTHR11596; 1.
Pfam; PF00245; Alk_phosphatase; 1.
PRINTS; PR00113; ALKPHPHTASE.
SMART; SM00098; alkPPc; 1.
SUPFAM; SSF53649; SSF53649; 1.
PROSITE; PS00123; ALKALINE_PHOSPHATASE; 1.
1: Evidence at protein level;
Alternative splicing; Biomineralization; Cell membrane;
Complete proteome; Direct protein sequencing; Disease mutation;
Disulfide bond; Glycoprotein; GPI-anchor; Hydrolase; Lipoprotein;
Magnesium; Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Signal; Transmembrane; Zinc.
SIGNAL 1 17 {ECO:0000269|PubMed:1458595,
ECO:0000269|PubMed:3954357}.
CHAIN 18 501 Alkaline phosphatase, tissue-nonspecific
isozyme.
/FTId=PRO_0000024023.
PROPEP 502 524 Removed in mature form. {ECO:0000305}.
/FTId=PRO_0000024024.
ACT_SITE 110 110 Phosphoserine intermediate.
{ECO:0000250|UniProtKB:P05187}.
METAL 60 60 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 60 60 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 110 110 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 173 173 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 332 332 Magnesium.
{ECO:0000250|UniProtKB:P05187}.
METAL 337 337 Zinc 2. {ECO:0000250|UniProtKB:P05187}.
METAL 341 341 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
METAL 378 378 Zinc 1. {ECO:0000250|UniProtKB:P05187}.
METAL 379 379 Zinc 1; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
METAL 454 454 Zinc 2; via tele nitrogen.
{ECO:0000250|UniProtKB:P05187}.
MOD_RES 110 110 Phosphoserine.
{ECO:0000250|UniProtKB:P09242}.
LIPID 501 501 GPI-anchor amidated serine.
{ECO:0000255}.
CARBOHYD 140 140 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 230 230 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 271 271 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 303 303 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 430 430 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218}.
DISULFID 139 201 {ECO:0000250|UniProtKB:P05187}.
DISULFID 489 497 {ECO:0000250|UniProtKB:P05187}.
VAR_SEQ 1 99 MISPFLVLAIGTCLTNSLVPEKEKDPKYWRDQAQETLKYAL
ELQKLNTNVAKNVIMFLGDGMGVSTVTAARILKGQLHHNPG
EETRLEMDKFPFVALSK -> MPWSFRSSTPTWLRMSSCSW
EM (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042711.
VAR_SEQ 1 55 Missing (in isoform 3).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044228.
VARIANT 17 17 S -> F (in HOPS).
{ECO:0000269|PubMed:9781036}.
/FTId=VAR_025903.
VARIANT 28 28 Y -> C (in HOPSI; 7% of activity).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013972.
VARIANT 33 33 A -> V (in HOPS; 7.2% of wild-type
activity; dbSNP:rs121918005).
{ECO:0000269|PubMed:1409720,
ECO:0000269|PubMed:15694177}.
/FTId=VAR_006147.
VARIANT 40 40 A -> V (in HOPS; 2% of activity;
dbSNP:rs770093969).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11479741,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_011081.
VARIANT 51 51 A -> S (in HOPS).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025904.
VARIANT 51 51 A -> V (in HOPS).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013973.
VARIANT 62 62 M -> L (in HOPS; moderate; 27% of
activity). {ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035}.
/FTId=VAR_006148.
VARIANT 62 62 M -> V (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025905.
VARIANT 63 63 G -> R (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025906.
VARIANT 63 63 G -> V (in HOPS; loss of activity).
{ECO:0000269|PubMed:11479741}.
/FTId=VAR_013974.
VARIANT 68 68 T -> M (in HOPSC; severe allele).
{ECO:0000269|PubMed:11760847}.
/FTId=VAR_025907.
VARIANT 71 71 R -> C (in HOPS; 35% of alkaline
phosphatase activity; dbSNP:rs121918001).
{ECO:0000269|PubMed:1409720,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_006149.
VARIANT 71 71 R -> H (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_013975.
VARIANT 71 71 R -> P (in HOPS; dbSNP:rs121918003).
{ECO:0000269|PubMed:1409720}.
/FTId=VAR_006150.
VARIANT 71 71 R -> S (in HOPSC; severe allele;
dbSNP:rs121918001).
{ECO:0000269|PubMed:11760847}.
/FTId=VAR_025908.
VARIANT 75 75 G -> S (in HOPS; severe; 3.5% of
activity). {ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013976.
VARIANT 76 76 Q -> R (in HOPS).
/FTId=VAR_025909.
VARIANT 108 108 P -> L (in HOPS; 0.4% of alkaline
phosphatase activity; severe allele; no
effect on subcellular location; fails to
assemble into dimeric structure; dominant
negative effect; dbSNP:rs121918015).
{ECO:0000269|PubMed:12920074,
ECO:0000269|PubMed:25982064}.
/FTId=VAR_025910.
VARIANT 111 111 A -> T (in HOPS; odonto; 50% of alkaline
phosphatase activity; dbSNP:rs773257111).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:12815606,
ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:9452105}.
/FTId=VAR_006151.
VARIANT 114 114 A -> G (in HOPS).
{ECO:0000269|PubMed:15135428}.
/FTId=VAR_025911.
VARIANT 116 116 A -> T (in HOPS; loss of alkaline
phosphatase activity; dbSNP:rs121918013).
{ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11479741,
ECO:0000269|PubMed:12920074,
ECO:0000269|PubMed:25982064}.
/FTId=VAR_013977.
VARIANT 120 120 G -> R (in HOPS).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013978.
VARIANT 128 128 V -> M (in HOPS).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025912.
VARIANT 129 129 G -> R (in HOPS).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013979.
VARIANT 132 132 A -> V (in HOPS).
{ECO:0000269|PubMed:11834095}.
/FTId=VAR_013146.
VARIANT 134 134 T -> H (in HOPS; requires 2 nucleotide
substitutions; dbSNP:rs786204530).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025913.
VARIANT 134 134 T -> N (in HOPS; 9% of activity;
dbSNP:rs780583917).
{ECO:0000269|PubMed:10679946}.
/FTId=VAR_011082.
VARIANT 136 136 R -> H (in HOPS; moderate; 33% of
activity; dbSNP:rs121918011).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:15694177}.
/FTId=VAR_006152.
VARIANT 148 148 T -> I (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025914.
VARIANT 152 152 R -> H (in HOPS; dbSNP:rs149344982).
{ECO:0000269|PubMed:11438998,
ECO:0000269|Ref.6}.
/FTId=VAR_013980.
VARIANT 162 162 G -> S (in HOPS; dbSNP:rs760029254).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025915.
VARIANT 162 162 G -> V (in HOPS; severe; 1% of activity;
dbSNP:rs121918012).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035}.
/FTId=VAR_006153.
VARIANT 170 170 N -> D (in HOPS).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013981.
VARIANT 171 171 H -> R (in HOPS; dbSNP:rs778232217).
/FTId=VAR_025916.
VARIANT 171 171 H -> Y (in HOPS; severe; 2% of activity).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035}.
/FTId=VAR_006154.
VARIANT 176 176 A -> T (in HOPS; 30% of alkaline
phosphatase activity; dbSNP:rs121918019).
{ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_011083.
VARIANT 177 177 A -> T (in HOPS and HOPSC; moderate
allele; dbSNP:rs199669988).
{ECO:0000269|PubMed:11760847,
ECO:0000269|PubMed:9452105}.
/FTId=VAR_006155.
VARIANT 179 179 A -> T (in HOPS; dbSNP:rs121918000).
{ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:3174660}.
/FTId=VAR_006156.
VARIANT 181 181 S -> L (in HOPS; 1% of activity;
dbSNP:rs199590449).
{ECO:0000269|PubMed:11479741}.
/FTId=VAR_013982.
VARIANT 184 184 R -> W (in HOPS; loss of activity;
dbSNP:rs763159520).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11479741,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013983.
VARIANT 189 189 D -> E (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025917.
VARIANT 191 191 E -> G (in HOPS; odonto).
{ECO:0000269|PubMed:9452105}.
/FTId=VAR_006157.
VARIANT 191 191 E -> K (in HOPS; moderate; frequent
mutation in European countries; 56% of
alkaline phosphatase activity;
dbSNP:rs121918007).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:1409720,
ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_006158.
VARIANT 201 201 C -> Y (in HOPS; weak alkaline
phosphatase activity; severely affects
homodimerization; reduced cell surface
expression).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:22266140}.
/FTId=VAR_006159.
VARIANT 207 207 Q -> P (in HOPS; dbSNP:rs121918004).
{ECO:0000269|PubMed:1409720}.
/FTId=VAR_006160.
VARIANT 211 211 N -> D (in HOPS).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013984.
VARIANT 212 212 I -> F (in HOPS).
/FTId=VAR_025918.
VARIANT 220 220 G -> A (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025919.
VARIANT 220 220 G -> V (in HOPS; odonto).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013985.
VARIANT 223 223 R -> Q (in HOPS; dbSNP:rs199665722).
{ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:15694177}.
/FTId=VAR_025920.
VARIANT 223 223 R -> W (in HOPS and HOPSC; 3% of
activity; severe allele;
dbSNP:rs766076920).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11479741,
ECO:0000269|PubMed:11760847,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:15694177,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013986.
VARIANT 224 224 K -> E (in HOPSI; partial loss of
activity). {ECO:0000269|PubMed:10834525}.
/FTId=VAR_011084.
VARIANT 235 235 E -> G (in HOPS).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013987.
VARIANT 246 246 R -> S (in HOPS; 4% of activity).
{ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11855933}.
/FTId=VAR_011085.
VARIANT 249 249 G -> V (in HOPS; partial loss of
activity; dbSNP:rs121918018).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11479741}.
/FTId=VAR_013988.
VARIANT 263 263 Y -> H (common polymorphism;
dbSNP:rs3200254).
{ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:1409720,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2928120,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_006161.
VARIANT 272 272 R -> H (in HOPS; 6.8% of wild-type
activity; dbSNP:rs781272386).
{ECO:0000269|PubMed:15694177}.
/FTId=VAR_025921.
VARIANT 272 272 R -> L (in HOPS; dbSNP:rs781272386).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025922.
VARIANT 275 275 L -> P (in HOPSC; severe allele).
{ECO:0000269|PubMed:11760847}.
/FTId=VAR_025923.
VARIANT 289 289 L -> F (in HOPS).
{ECO:0000269|PubMed:9747027}.
/FTId=VAR_006162.
VARIANT 291 291 E -> K (in HOPS; moderate; 8% of
activity; dbSNP:rs786204473).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11999978,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013989.
VARIANT 292 292 P -> T (in HOPS; 4% of wild-type
activity; dbSNP:rs765458125).
{ECO:0000269|PubMed:15694177}.
/FTId=VAR_025924.
VARIANT 293 294 Missing (in HOPS).
/FTId=VAR_025925.
VARIANT 294 294 D -> A (in HOPS; dbSNP:rs121918002).
{ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:1409720,
ECO:0000269|PubMed:15694177}.
/FTId=VAR_006163.
VARIANT 294 294 D -> Y (in HOPS).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013990.
VARIANT 295 295 M -> T (in HOPS; 8.5% of wild-type
activity). {ECO:0000269|PubMed:15694177}.
/FTId=VAR_025926.
VARIANT 297 297 Y -> D (in HOPS; 1.3% of wild-type
activity). {ECO:0000269|PubMed:15694177}.
/FTId=VAR_025927.
VARIANT 298 298 E -> K (in HOPSI; dbSNP:rs121918017).
{ECO:0000269|PubMed:7833929}.
/FTId=VAR_025928.
VARIANT 299 299 L -> P (in HOPS).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025929.
VARIANT 306 306 D -> V (in HOPS).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035}.
/FTId=VAR_006164.
VARIANT 311 311 E -> K (in HOPS; dbSNP:rs763457259).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025930.
VARIANT 326 326 G -> R (in HOPS; in a patient carrying
also K-291).
{ECO:0000269|PubMed:11999978}.
/FTId=VAR_013991.
VARIANT 327 327 F -> G (in HOPS; requires 2 nucleotide
substitutions).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013992.
VARIANT 327 327 F -> L (in HOPS and HOPSI;
dbSNP:rs121918010).
{ECO:0000269|PubMed:8954059,
ECO:0000269|PubMed:9452105}.
/FTId=VAR_006165.
VARIANT 327 327 Missing (in HOPS).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025931.
VARIANT 334 334 G -> D (in HOPS; loss of alkaline
phosphatase activity; dbSNP:rs121918009).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:15694177,
ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:8406453,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_006166.
VARIANT 334 334 G -> R (in HOPS; weak alkaline
phosphatase activity).
{ECO:0000269|PubMed:19500388}.
/FTId=VAR_075557.
VARIANT 339 339 G -> R (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_025932.
VARIANT 348 348 A -> T (in HOPS).
{ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11855933}.
/FTId=VAR_011086.
VARIANT 354 354 E -> D (in HOPS).
/FTId=VAR_025933.
VARIANT 378 378 D -> V (in HOPS; loss of activity;
dbSNP:rs121918008).
{ECO:0000269|PubMed:10690885,
ECO:0000269|PubMed:11479741,
ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:1409720}.
/FTId=VAR_006167.
VARIANT 381 381 H -> R (in HOPS).
{ECO:0000269|PubMed:10679946}.
/FTId=VAR_011087.
VARIANT 382 382 V -> I (in HOPS; loss of alkaline
phosphatase activity; dbSNP:rs771540767).
{ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:9452105}.
/FTId=VAR_006168.
VARIANT 391 391 R -> C (in HOPS; moderate; 4-10% of
alkaline phosphatase activity;
dbSNP:rs371243939).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_013993.
VARIANT 391 391 R -> H (in HOPSC and HOPS; severe allele;
loss of alkaline phosphatase activity).
{ECO:0000269|PubMed:11760847,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_025934.
VARIANT 399 399 A -> S (in HOPS).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013994.
VARIANT 406 406 D -> G (in HOPS; 15% of activity).
{ECO:0000269|PubMed:10679946}.
/FTId=VAR_011088.
VARIANT 411 411 T -> A (in HOPS; absence of residual
enzymatic activity).
{ECO:0000269|PubMed:15694177}.
/FTId=VAR_025935.
VARIANT 414 414 L -> M (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:11855933,
ECO:0000269|PubMed:12920074,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_025936.
VARIANT 417 417 N -> S (in HOPS; very low alkaline
phosphatase activity; does not affect
subcellular location; fails to assemble
into dimeric structure;
dbSNP:rs121918014).
{ECO:0000269|PubMed:11745997,
ECO:0000269|PubMed:23688511}.
/FTId=VAR_025937.
VARIANT 420 420 G -> A (in HOPS; very low alkaline
phosphatase activity; does not affect
subcellular location).
{ECO:0000269|PubMed:19500388,
ECO:0000269|PubMed:23039266}.
/FTId=VAR_075558.
VARIANT 420 420 G -> S (in HOPS; very low alkaline
phosphatase activity; does not affect
subcellular location).
{ECO:0000269|PubMed:23039266}.
/FTId=VAR_075559.
VARIANT 423 423 V -> A (in HOPS; 16% alkaline of
phosphatase activity).
{ECO:0000269|PubMed:11438998,
ECO:0000269|PubMed:23039266}.
/FTId=VAR_013995.
VARIANT 426 426 G -> C (in HOPSI; partial loss of
activity). {ECO:0000269|PubMed:10834525}.
/FTId=VAR_011089.
VARIANT 426 426 G -> D (in HOPS).
{ECO:0000269|PubMed:11855933}.
/FTId=VAR_025938.
VARIANT 436 436 Y -> H (in HOPS; dbSNP:rs121918006).
{ECO:0000269|PubMed:1409720}.
/FTId=VAR_006169.
VARIANT 445 445 S -> P (in HOPS; severe; 2% of activity).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013996.
VARIANT 450 450 R -> C (in HOPS; severe; 4% of activity;
dbSNP:rs138690664).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013997.
VARIANT 450 450 R -> H (in HOPS; dbSNP:rs150799088).
{ECO:0000269|PubMed:10679946}.
/FTId=VAR_011090.
VARIANT 452 452 E -> K (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:12815606,
ECO:0000269|PubMed:19500388}.
/FTId=VAR_025939.
VARIANT 456 456 G -> R (in HOPSI; loss of activity;
dbSNP:rs121918016).
{ECO:0000269|PubMed:8954059}.
/FTId=VAR_011091.
VARIANT 459 459 V -> L (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:19500388}.
/FTId=VAR_075560.
VARIANT 459 459 V -> M (in HOPSI).
{ECO:0000269|PubMed:11438998}.
/FTId=VAR_013998.
VARIANT 468 468 A -> T (in HOPS).
{ECO:0000269|PubMed:12815606}.
/FTId=VAR_025940.
VARIANT 473 473 G -> S (in HOPS).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_013999.
VARIANT 476 476 E -> A (in HOPS; loss of alkaline
phosphatase activity).
{ECO:0000269|PubMed:19500388}.
/FTId=VAR_075561.
VARIANT 476 476 E -> K (in HOPS).
{ECO:0000269|PubMed:10094560,
ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:11855933}.
/FTId=VAR_006170.
VARIANT 478 478 N -> I (in HOPS; 9% of activity).
{ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:11479741}.
/FTId=VAR_011092.
VARIANT 489 489 C -> S (in HOPS; reduces alkaline
phosphatase activity).
{ECO:0000269|PubMed:10679946,
ECO:0000269|PubMed:22266140}.
/FTId=VAR_011093.
VARIANT 490 490 I -> F (in HOPS; odonto; partial loss of
activity). {ECO:0000269|PubMed:11479741}.
/FTId=VAR_014000.
VARIANT 491 491 G -> R (in HOPS).
{ECO:0000269|PubMed:10332035,
ECO:0000269|PubMed:9781036}.
/FTId=VAR_014001.
VARIANT 522 522 V -> A (in dbSNP:rs34605986).
{ECO:0000269|PubMed:10690885,
ECO:0000269|PubMed:11760847,
ECO:0000269|PubMed:11855933}.
/FTId=VAR_011094.
CONFLICT 29 29 W -> A (in Ref. 10; AA sequence).
{ECO:0000305}.
CONFLICT 104 104 N -> K (in Ref. 3; CAA32376).
{ECO:0000305}.
CONFLICT 361 361 Q -> H (in Ref. 1; BAA32129).
{ECO:0000305}.
CONFLICT 446 446 A -> P (in Ref. 1; BAA32129).
{ECO:0000305}.
SEQUENCE 524 AA; 57305 MW; 71B45F17F6211900 CRC64;
MISPFLVLAI GTCLTNSLVP EKEKDPKYWR DQAQETLKYA LELQKLNTNV AKNVIMFLGD
GMGVSTVTAA RILKGQLHHN PGEETRLEMD KFPFVALSKT YNTNAQVPDS AGTATAYLCG
VKANEGTVGV SAATERSRCN TTQGNEVTSI LRWAKDAGKS VGIVTTTRVN HATPSAAYAH
SADRDWYSDN EMPPEALSQG CKDIAYQLMH NIRDIDVIMG GGRKYMYPKN KTDVEYESDE
KARGTRLDGL DLVDTWKSFK PRYKHSHFIW NRTELLTLDP HNVDYLLGLF EPGDMQYELN
RNNVTDPSLS EMVVVAIQIL RKNPKGFFLL VEGGRIDHGH HEGKAKQALH EAVEMDRAIG
QAGSLTSSED TLTVVTADHS HVFTFGGYTP RGNSIFGLAP MLSDTDKKPF TAILYGNGPG
YKVVGGEREN VSMVDYAHNN YQAQSAVPLR HETHGGEDVA VFSKGPMAHL LHGVHEQNYV
PHVMAYAACI GANLGHCAPA SSAGSLAAGP LLLALALYPL SVLF


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