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A disintegrin and metalloproteinase with thrombospondin motifs 13 (ADAM-TS 13) (ADAM-TS13) (ADAMTS-13) (EC 3.4.24.87) (von Willebrand factor-cleaving protease) (vWF-CP) (vWF-cleaving protease)

 ATS13_HUMAN             Reviewed;        1427 AA.
Q76LX8; Q6UY16; Q710F6; Q711T8; Q96L37; Q9H0G3; Q9UGQ1;
25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 1.
27-SEP-2017, entry version 141.
RecName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 13;
Short=ADAM-TS 13;
Short=ADAM-TS13;
Short=ADAMTS-13;
EC=3.4.24.87 {ECO:0000269|PubMed:11535495};
AltName: Full=von Willebrand factor-cleaving protease;
Short=vWF-CP;
Short=vWF-cleaving protease;
Flags: Precursor;
Name=ADAMTS13; Synonyms=C9orf8; ORFNames=UNQ6102/PRO20085;
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), PROTEIN SEQUENCE OF 75-103,
AND TISSUE SPECIFICITY.
TISSUE=Liver;
PubMed=11574066; DOI=10.1093/oxfordjournals.jbchem.a003009;
Soejima K., Mimura N., Hirashima M., Maeda H., Hamamoto T.,
Nakagaki T., Nozaki C.;
"A novel human metalloprotease synthesized in the liver and secreted
into the blood: possibly, the von Willebrand factor-cleaving
protease?";
J. Biochem. 130:475-480(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, AND VARIANT
VAL-900.
TISSUE=Liver;
PubMed=11557746; DOI=10.1074/jbc.C100515200;
Zheng X., Chung D., Takayama T.K., Majerus E.M., Sadler J.E.,
Fujikawa K.;
"Structure of von Willebrand factor-cleaving protease (ADAMTS13), a
metalloprotease involved in thrombotic thrombocytopenic purpura.";
J. Biol. Chem. 276:41059-41063(2001).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN THROMBOTIC
THROMBOCYTOPENIC PURPURA, VARIANTS TTP ASP-96; CYS-102; ILE-196;
HIS-398; GLY-528; CYS-692; GLY-951; GLY-1024 AND TYR-1213, AND
VARIANTS TRP-7; GLU-448; ALA-618; HIS-625; VAL-732; VAL-900 AND
THR-1033.
TISSUE=Liver;
PubMed=11586351; DOI=10.1038/35097008;
Levy G.G., Nichols W.C., Lian E.C., Foroud T., McClintick J.N.,
McGee B.M., Yang A.Y., Siemieniak D.R., Stark K.R., Gruppo R.,
Sarode R., Shurin S.B., Chandrasekaran V., Stabler S.P., Sabio H.,
Bouhassira E.E., Upshaw J.D. Jr., Ginsburg D., Tsai H.-M.;
"Mutations in a member of the ADAMTS gene family cause thrombotic
thrombocytopenic purpura.";
Nature 413:488-494(2001).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3).
TISSUE=Liver;
PubMed=11867212; DOI=10.1016/S0378-1119(01)00861-7;
Cal S., Obaya A.J., Llamazares M., Garabaya C., Quesada V.,
Lopez-Otin C.;
"Cloning, expression analysis, and structural characterization of
seven novel human ADAMTSs, a family of metalloproteinases with
disintegrin and thrombospondin-1 domains.";
Gene 283:49-62(2002).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
TISSUE=Brain;
Young J.M., Woodward K.J., Aziz S., Burley M., Kwiatkowski D.J.,
Povey S.;
"Cloning of a sugar transporter gene, a G-beta subunit like gene and
three novel genes in human chromosome 9q34.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS TRP-7; GLU-448;
HIS-456; LEU-457; ALA-618; HIS-625; LYS-740; VAL-900; ARG-982;
THR-1033 AND ILE-1226.
SeattleSNPs variation discovery resource;
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[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] OF 275-1427, AND VARIANT
GLU-448.
PubMed=12975309; DOI=10.1101/gr.1293003;
Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S.,
Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
Wood W.I., Godowski P.J., Gray A.M.;
"The secreted protein discovery initiative (SPDI), a large-scale
effort to identify novel human secreted and transmembrane proteins: a
bioinformatics assessment.";
Genome Res. 13:2265-2270(2003).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1191-1427.
TISSUE=Testis;
PubMed=11230166; DOI=10.1101/gr.GR1547R;
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H.,
Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
Wambutt R., Korn B., Klein M., Poustka A.;
"Towards a catalog of human genes and proteins: sequencing and
analysis of 500 novel complete protein coding human cDNAs.";
Genome Res. 11:422-435(2001).
[11]
PROTEIN SEQUENCE OF 75-89.
PubMed=11535494; DOI=10.1182/blood.V98.6.1654;
Gerritsen H.E., Robles R., Laemmle B., Furlan M.;
"Partial amino acid sequence of purified von Willebrand factor-
cleaving protease.";
Blood 98:1654-1661(2001).
[12]
PROTEIN SEQUENCE OF 75-94, AND CATALYTIC ACTIVITY.
PubMed=11535495; DOI=10.1182/blood.V98.6.1662;
Fujikawa K., Suzuki H., McMullen B., Chung D.;
"Purification of human von Willebrand factor-cleaving protease and its
identification as a new member of the metalloproteinase family.";
Blood 98:1662-1666(2001).
[13]
CHARACTERIZATION, AND SUBCELLULAR LOCATION.
PubMed=12791682; DOI=10.1074/jbc.M305331200;
Zheng X., Nishio K., Majerus E.M., Sadler J.E.;
"Cleavage of von Willebrand factor requires the spacer domain of the
metalloprotease ADAMTS13.";
J. Biol. Chem. 278:30136-30141(2003).
[14]
ENZYME REGULATION, AND MUTAGENESIS OF ARG-71 AND ARG-73.
PubMed=12975358; DOI=10.1074/jbc.M309872200;
Majerus E.M., Zheng X., Tuley E.A., Sadler J.E.;
"Cleavage of the ADAMTS13 propeptide is not required for protease
activity.";
J. Biol. Chem. 278:46643-46648(2003).
[15]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-614; ASN-667 AND ASN-1354.
TISSUE=Plasma;
PubMed=16335952; DOI=10.1021/pr0502065;
Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E.,
Moore R.J., Smith R.D.;
"Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
hydrazide chemistry, and mass spectrometry.";
J. Proteome Res. 4:2070-2080(2005).
[16]
ENZYME REGULATION.
PubMed=16286459; DOI=10.1074/jbc.M504540200;
Anderson P.J., Kokame K., Sadler J.E.;
"Zinc and calcium ions cooperatively modulate ADAMTS13 activity.";
J. Biol. Chem. 281:850-857(2006).
[17]
GLYCOSYLATION AT SER-698; SER-757; SER-907; SER-965; SER-1027 AND
SER-1087, IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF
SER-399; SER-698; SER-757; SER-907; SER-965; SER-1027 AND SER-1087.
PubMed=17395589; DOI=10.1074/jbc.M700317200;
Ricketts L.M., Dlugosz M., Luther K.B., Haltiwanger R.S.,
Majerus E.M.;
"O-fucosylation is required for ADAMTS13 secretion.";
J. Biol. Chem. 282:17014-17023(2007).
[18]
ENZYME REGULATION, CALCIUM-BINDING SITES, AND MUTAGENESIS OF GLU-83;
ASP-173; GLU-184; ASP-187 AND GLU-212.
PubMed=19047683; DOI=10.1182/blood-2008-03-144683;
Gardner M.D., Chion C.K., de Groot R., Shah A., Crawley J.T.,
Lane D.A.;
"A functional calcium-binding site in the metalloprotease domain of
ADAMTS13.";
Blood 113:1149-1157(2009).
[19]
GLYCOSYLATION AT ASN-667 AND ASN-707.
PubMed=19139490; DOI=10.1074/mcp.M800504-MCP200;
Jia W., Lu Z., Fu Y., Wang H.P., Wang L.H., Chi H., Yuan Z.F.,
Zheng Z.B., Song L.N., Han H.H., Liang Y.M., Wang J.L., Cai Y.,
Zhang Y.K., Deng Y.L., Ying W.T., He S.M., Qian X.H.;
"A strategy for precise and large scale identification of core
fucosylated glycoproteins.";
Mol. Cell. Proteomics 8:913-923(2009).
[20]
REVIEW ON VARIANTS.
PubMed=19847791; DOI=10.1002/humu.21143;
Lotta L.A., Garagiola I., Palla R., Cairo A., Peyvandi F.;
"ADAMTS13 mutations and polymorphisms in congenital thrombotic
thrombocytopenic purpura.";
Hum. Mutat. 31:11-19(2010).
[21]
X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) OF 287-685, FUNCTION,
GLYCOSYLATION AT TRP-387; SER-399; ASN-552 AND ASN-614, SPACER DOMAIN,
AND DISULFIDE BONDS.
PubMed=19880749; DOI=10.1073/pnas.0909755106;
Akiyama M., Takeda S., Kokame K., Takagi J., Miyata T.;
"Crystal structures of the noncatalytic domains of ADAMTS13 reveal
multiple discontinuous exosites for von Willebrand factor.";
Proc. Natl. Acad. Sci. U.S.A. 106:19274-19279(2009).
[22]
VARIANTS TTP PRO-268 AND TYR-508, VARIANTS GLU-448 AND SER-475,
CHARACTERIZATION OF VARIANTS TTP PRO-268 AND TYR-508, AND
CHARACTERIZATION OF VARIANTS GLU-448 AND SER-475.
PubMed=12181489; DOI=10.1073/pnas.172277399;
Kokame K., Matsumoto M., Soejima K., Yagi H., Ishizashi H., Funato M.,
Tamai H., Konno M., Kamide K., Kawano Y., Miyata T., Fujimura Y.;
"Mutations and common polymorphisms in ADAMTS13 gene responsible for
von Willebrand factor-cleaving protease activity.";
Proc. Natl. Acad. Sci. U.S.A. 99:11902-11907(2002).
[23]
VARIANTS TTP GLN-232; CYS-263 AND LEU-353.
PubMed=12393505; DOI=10.1182/blood-2002-08-2399;
Schneppenheim R., Budde U., Oyen F., Angerhaus D., Aumann V.,
Drewke E., Hassenpflug W., Haberle J., Kentouche K., Kohne E.,
Kurnik K., Mueller-Wiefel D., Obser T., Santer R., Sykora K.W.;
"von Willebrand factor cleaving protease and ADAMTS13 mutations in
childhood TTP.";
Blood 101:1845-1850(2003).
[24]
VARIANT TTP TRP-1336, AND VARIANT VAL-732.
PubMed=12614216; DOI=10.1046/j.1365-2141.2003.04183.x;
Antoine G., Zimmermann K., Plaimauer B., Grillowitzer M., Studt J.D.,
Lammle B., Scheiflinger F.;
"ADAMTS13 gene defects in two brothers with constitutional thrombotic
thrombocytopenic purpura and normalization of von Willebrand factor-
cleaving protease activity by recombinant human ADAMTS13.";
Br. J. Haematol. 120:821-824(2003).
[25]
VARIANTS TTP HIS-235; TYR-311 AND LEU-353, AND VARIANT LEU-457.
PubMed=12753286; DOI=10.1046/j.1523-1755.63.6s.1.x;
Assink K., Schiphorst R., Allford S., Karpman D., Etzioni A.,
Brichard B., van de Kar N., Monnens L., van den Heuvel L.;
"Mutation analysis and clinical implications of von Willebrand factor-
cleaving protease deficiency.";
Kidney Int. 63:1995-1999(2003).
[26]
VARIANT TTP ILE-196, AND VARIANT GLU-448.
PubMed=14512317; DOI=10.1182/blood-2003-04-1346;
Pimanda J.E., Maekawa A., Wind T., Paxton J., Chesterman C.N.,
Hogg P.J.;
"Congenital thrombotic thrombocytopenic purpura in association with a
mutation in the second CUB domain of ADAMTS13.";
Blood 103:627-629(2004).
[27]
VARIANTS TTP TRP-193; PHE-673; TYR-908 AND CYS-1123, VARIANT GLU-448,
AND CHARACTERIZATION OF VARIANTS TTP TRP-193; PHE-673; TYR-908 AND
CYS-1123.
PubMed=14563640; DOI=10.1182/blood-2003-06-1796;
Matsumoto M., Kokame K., Soejima K., Miura M., Hayashi S., Fujii Y.,
Iwai A., Ito E., Tsuji Y., Takeda-Shitaka M., Iwadate M., Umeyama H.,
Yagi H., Ishizashi H., Banno F., Nakagaki T., Miyata T., Fujimura Y.;
"Molecular characterization of ADAMTS13 gene mutations in Japanese
patients with Upshaw-Schulman syndrome.";
Blood 103:1305-1310(2004).
[28]
VARIANT TTP VAL-250, AND CHARACTERIZATION OF VARIANT TTP VAL-250.
PubMed=15126318; DOI=10.1182/blood-2004-02-0715;
Uchida T., Wada H., Mizutani M., Iwashita M., Ishihara H., Shibano T.,
Suzuki M., Matsubara Y., Soejima K., Matsumoto M., Fujimura Y.,
Ikeda Y., Murata M.;
"Identification of novel mutations in ADAMTS13 in an adult patient
with congenital thrombotic thrombocytopenic purpura.";
Blood 104:2081-2083(2004).
[29]
VARIANTS TTP MET-79; PRO-203; PRO-268; GLN-507; VAL-596; ARG-758 AND
SER-908.
PubMed=15009458; DOI=10.1111/j.1538-7933.2004.00623.x;
Veyradier A., Lavergne J.M., Ribba A.S., Obert B., Loirat C.,
Meyer D., Girma J.P.;
"Ten candidate ADAMTS13 mutations in six French families with
congenital thrombotic thrombocytopenic purpura (Upshaw-Schulman
syndrome).";
J. Thromb. Haemost. 2:424-429(2004).
[30]
VARIANT TTP CYS-390.
PubMed=15327386; DOI=10.1111/j.1523-1755.2004.00841.x;
Licht C., Stapenhorst L., Simon T., Budde U., Schneppenheim R.,
Hoppe B.;
"Two novel ADAMTS13 gene mutations in thrombotic thrombocytopenic
purpura/hemolytic-uremic syndrome (TTP/HUS).";
Kidney Int. 66:955-958(2004).
[31]
VARIANTS LEU-903 AND TRP-1095.
PubMed=16468327;
Liu F., Jin J., Dong N.Z., Wang Y.G., Ruan C.G.;
"Identification of two novel mutations in ADAMTS13 gene in a patient
with hereditary thrombotic thrombocytopenic purpura.";
Zhonghua Xue Ye Xue Za Zhi 26:521-524(2005).
[32]
CHARACTERIZATION OF VARIANTS TRP-7; GLU-448; ALA-618 AND VAL-732,
CHARACTERIZATION OF VARIANT TTP TRP-1336, AND DISCUSSION OF MUTUAL
MODULATORY EFFECTS OF POLYMORPHISMS.
PubMed=16160007; DOI=10.1182/blood-2005-06-2482;
Plaimauer B., Fuhrmann J., Mohr G., Wernhart W., Bruno K., Ferrari S.,
Konetschny C., Antoine G., Rieger M., Scheiflinger F.;
"Modulation of ADAMTS13 secretion and specific activity by a
combination of common amino acid polymorphisms and a missense
mutation.";
Blood 107:118-125(2006).
[33]
VARIANTS TTP MET-88 AND VAL-1239, AND CHARACTERIZATION OF VARIANTS TTP
MET-88 AND VAL-1239.
PubMed=16453338; DOI=10.1002/humu.20267;
Peyvandi F., Lavoretano S., Palla R., Valsecchi C., Merati G.,
De Cristofaro R., Rossi E., Mannuccio Mannucci P.;
"Mechanisms of the interaction between two ADAMTS13 gene mutations
leading to severe deficiency of enzymatic activity.";
Hum. Mutat. 27:330-336(2006).
[34]
VARIANT TTP TRP-1060, AND CHARACTERIZATION OF VARIANTS TTP TRP-1060.
PubMed=16796708; DOI=10.1111/j.1538-7836.2006.02098.x;
Tao Z., Anthony K., Peng Y., Choi H., Nolasco L., Rice L., Moake J.L.,
Dong J.F.;
"Novel ADAMTS-13 mutations in an adult with delayed onset thrombotic
thrombocytopenic purpura.";
J. Thromb. Haemost. 4:1931-1935(2006).
[35]
VARIANT TTP GLN-234, AND VARIANT LEU-903.
PubMed=16449289; DOI=10.1093/ndt/gfk072;
Shibagaki Y., Matsumoto M., Kokame K., Ohba S., Miyata T.,
Fujimura Y., Fujita T.;
"Novel compound heterozygote mutations (H234Q/R1206X) of the ADAMTS13
gene in an adult patient with Upshaw-Schulman syndrome showing
predominant episodes of repeated acute renal failure.";
Nephrol. Dial. Transplant. 21:1289-1292(2006).
[36]
VARIANTS TTP ILE-196; CYS-263; SER-347; LEU-353; GLN-507; LEU-671 AND
TRP-1060.
PubMed=16807643; DOI=10.1160/TH05-12-0817;
Schneppenheim R., Kremer Hovinga J.A., Becker T., Budde U.,
Karpman D., Brockhaus W., Hrachovinova I., Korczowski B., Oyen F.,
Rittich S., von Rosen J., Tjonnfjord G.E., Pimanda J.E., Wienker T.F.,
Lammle B.;
"A common origin of the 4143insA ADAMTS13 mutation.";
Thromb. Haemost. 96:3-6(2006).
[37]
VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, CHARACTERIZATION OF
VARIANTS TTP TRP-1060; CYS-1123 AND TRP-1219, AND VARIANT GLU-448.
PubMed=17003922;
Donadelli R., Banterla F., Galbusera M., Capoferri C., Bucchioni S.,
Gastoldi S., Nosari S., Monteferrante G., Ruggeri Z.M., Bresin E.,
Scheiflinger F., Rossi E., Martinez C., Coppo R., Remuzzi G.,
Noris M.;
"In-vitro and in-vivo consequences of mutations in the von Willebrand
factor cleaving protease ADAMTS13 in thrombotic thrombocytopenic
purpura.";
Thromb. Haemost. 96:454-464(2006).
[38]
VARIANT TTP PHE-119.
PubMed=18443791; DOI=10.1007/s00277-008-0496-6;
Meyer S.C., Jeddi R., Meddeb B., Gouider E., Lammle B.,
Kremer Hovinga J.A.;
"A first case of congenital TTP on the African continent due to a new
homozygous mutation in the catalytic domain of ADAMTS13.";
Ann. Hematol. 87:663-666(2008).
[39]
VARIANTS TTP THR-178; TRP-193; CYS-304; CYS-349; ASP-525 AND PRO-606,
AND VARIANTS ARG-339; GLU-448 AND ALA-618.
PubMed=19055667; DOI=10.1111/j.1365-2141.2008.07515.x;
Fujimura Y., Matsumoto M., Kokame K., Isonishi A., Soejima K.,
Akiyama N., Tomiyama J., Natori K., Kuranishi Y., Imamura Y.,
Inoue N., Higasa S., Seike M., Kozuka T., Hara M., Wada H., Murata M.,
Ikeda Y., Miyata T., George J.N.;
"Pregnancy-induced thrombocytopenia and TTP, and the risk of fetal
death, in Upshaw-Schulman syndrome: a series of 15 pregnancies in 9
genotyped patients.";
Br. J. Haematol. 144:742-754(2009).
[40]
VARIANT TTP 977-CYS--ARG-979 DELINS TRP.
PubMed=19116307; DOI=10.3324/haematol.13524;
Palla R., Lavoretano S., Lombardi R., Garagiola I., Karimi M.,
Afrasiabi A., Ramzi M., De Cristofaro R., Peyvandi F.;
"The first deletion mutation in the TSP1-6 repeat domain of ADAMTS13
in a family with inherited thrombotic thrombocytopenic purpura.";
Haematologica 94:289-293(2009).
[41]
VARIANT TTP CYS-658.
PubMed=22075512;
Lee S.H., Park J.H., Park S.K., Lee E.H., Choi J.I., Visentin G.P.,
Park T.S., Oh S.H., Kim S.R.;
"A novel homozygous missense ADAMTS13 mutation Y658C in a patient with
recurrent thrombotic thrombocytopenic purpura.";
Ann. Clin. Lab. Sci. 41:273-276(2011).
[42]
VARIANT LEU-1314.
PubMed=21488199; DOI=10.3349/ymj.2011.52.3.530;
Choi H.S., Cheong H.I., Kim N.K., Oh D., Park H.W.;
"ADAMTS13 gene mutations in children with hemolytic uremic syndrome.";
Yonsei Med. J. 52:530-534(2011).
-!- FUNCTION: Cleaves the vWF multimers in plasma into smaller forms
thereby controlling vWF-mediated platelet thrombus formation.
{ECO:0000269|PubMed:19880749}.
-!- CATALYTIC ACTIVITY: The enzyme cleaves the von Willebrand factor
at bond 842-Tyr-|-Met-843 within the A2 domain.
{ECO:0000269|PubMed:11535495}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000250|UniProtKB:Q9UNA0};
Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q9UNA0};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Evidence={ECO:0000269|PubMed:19047683};
Note=Binds 4 Ca(2+) ions. {ECO:0000269|PubMed:19047683};
-!- ENZYME REGULATION: Zinc and calcium ions cooperatively modulate
enzyme activity. The cleavage of the pro-domain is not required
for protease activity. Dependence on calcium for proteolytic
activity is mediated by the high affinity site.
{ECO:0000269|PubMed:12975358, ECO:0000269|PubMed:16286459,
ECO:0000269|PubMed:19047683}.
-!- INTERACTION:
P04275:VWF; NbExp=17; IntAct=EBI-981764, EBI-981819;
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12791682}.
Note=Secretion enhanced by O-fucosylation of TSP type-1 repeats.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q76LX8-1; Sequence=Displayed;
Name=2;
IsoId=Q76LX8-2; Sequence=VSP_020003;
Name=3;
IsoId=Q76LX8-3; Sequence=VSP_020002, VSP_020003;
Name=4;
IsoId=Q76LX8-4; Sequence=VSP_055537, VSP_055538, VSP_055539;
-!- TISSUE SPECIFICITY: Plasma. Expressed primarily in liver.
{ECO:0000269|PubMed:11574066}.
-!- DOMAIN: The pro-domain is not required for folding or secretion
and does not perform the common function of maintening enzyme
latency.
-!- DOMAIN: The globular cysteineless spacer domain adopts a jelly-
roll topology, and is necessary to recognize and cleave vWF. The
C-terminal TSP type-1 and CUB domains may modulate this
interaction.
-!- PTM: Glycosylated. O-fucosylated by POFUT2 on a serine or a
threonine residue found within the consensus sequence C1-X(2)-
(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are
the first and second cysteine residue of the repeat, respectively.
Fucosylated repeats can then be further glycosylated by the
addition of a beta-1,3-glucose residue by the glucosyltransferase,
B3GALTL. Fucosylation mediates the efficient secretion of
ADAMTS13. May also be C-glycosylated on tryptophan residues within
the consensus sequence W-X-X-W of the TPRs, and also N-
glycosylated. These other glycosylations can also facilitate
secretion. {ECO:0000269|PubMed:11557746,
ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:17395589,
ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19880749}.
-!- PTM: The precursor is processed by a furin endopeptidase which
cleaves off the pro-domain.
-!- POLYMORPHISM: Genetic variations in ADAMTS13 coding region
influence plasmatic ADAMTS13 activity levels. Dependent on the
sequence context, the same polymorphisms might be either positive
or negative modifiers of gene expression, thereby altering the
phenotype of ADAMTS13 deficiency. {ECO:0000305|PubMed:16160007}.
-!- DISEASE: Thrombotic thrombocytopenic purpura congenital (TTP)
[MIM:274150]: A hematologic disease characterized by hemolytic
anemia with fragmentation of erythrocytes, thrombocytopenia,
diffuse and non-focal neurologic findings, decreased renal
function and fever. recessive. {ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:12181489, ECO:0000269|PubMed:12393505,
ECO:0000269|PubMed:12614216, ECO:0000269|PubMed:12753286,
ECO:0000269|PubMed:14512317, ECO:0000269|PubMed:14563640,
ECO:0000269|PubMed:15009458, ECO:0000269|PubMed:15126318,
ECO:0000269|PubMed:15327386, ECO:0000269|PubMed:16160007,
ECO:0000269|PubMed:16449289, ECO:0000269|PubMed:16453338,
ECO:0000269|PubMed:16796708, ECO:0000269|PubMed:16807643,
ECO:0000269|PubMed:17003922, ECO:0000269|PubMed:18443791,
ECO:0000269|PubMed:19055667, ECO:0000269|PubMed:19116307,
ECO:0000269|PubMed:22075512}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SEQUENCE CAUTION:
Sequence=AAQ88485.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=CAB66743.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Wikipedia; Note=ADAMTS13 entry;
URL="https://en.wikipedia.org/wiki/ADAMTS13";
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/adamts13/";
-!- WEB RESOURCE: Name=Mendelian genes ADAM metallopeptidase with
thrombospondin type 1 motif, 13 (ADAMTS13); Note=Leiden Open
Variation Database (LOVD);
URL="http://www.lovd.nl/ADAMTS13";
-----------------------------------------------------------------------
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EMBL; AB069698; BAB69487.2; -; mRNA.
EMBL; AY055376; AAL17652.1; -; mRNA.
EMBL; AF414401; AAL11095.1; -; mRNA.
EMBL; AJ305314; CAC83682.1; -; mRNA.
EMBL; AJ420810; CAD12729.1; -; mRNA.
EMBL; AJ011374; CAB66157.1; -; mRNA.
EMBL; DQ422807; ABD72606.1; -; Genomic_DNA.
EMBL; AL158826; CAI12850.1; -; Genomic_DNA.
EMBL; AL593848; CAI12850.1; JOINED; Genomic_DNA.
EMBL; AL158826; CAI12851.1; -; Genomic_DNA.
EMBL; AL593848; CAI12851.1; JOINED; Genomic_DNA.
EMBL; AL158826; CAI12852.1; -; Genomic_DNA.
EMBL; AL593848; CAI12852.1; JOINED; Genomic_DNA.
EMBL; CH471090; EAW88086.1; -; Genomic_DNA.
EMBL; AY358118; AAQ88485.1; ALT_INIT; mRNA.
EMBL; AL136809; CAB66743.1; ALT_INIT; mRNA.
CCDS; CCDS6970.1; -. [Q76LX8-1]
CCDS; CCDS6971.1; -. [Q76LX8-3]
CCDS; CCDS6972.1; -. [Q76LX8-2]
RefSeq; NP_620594.1; NM_139025.4. [Q76LX8-1]
RefSeq; NP_620595.1; NM_139026.4. [Q76LX8-3]
RefSeq; NP_620596.2; NM_139027.4. [Q76LX8-2]
UniGene; Hs.131433; -.
PDB; 3GHM; X-ray; 2.60 A; A=287-685.
PDB; 3GHN; X-ray; 2.80 A; A=287-685.
PDB; 3VN4; X-ray; 2.80 A; A=287-685.
PDBsum; 3GHM; -.
PDBsum; 3GHN; -.
PDBsum; 3VN4; -.
ProteinModelPortal; Q76LX8; -.
SMR; Q76LX8; -.
DIP; DIP-36050N; -.
IntAct; Q76LX8; 1.
MINT; MINT-4713142; -.
STRING; 9606.ENSP00000360997; -.
BindingDB; Q76LX8; -.
ChEMBL; CHEMBL2346492; -.
MEROPS; M12.241; -.
iPTMnet; Q76LX8; -.
PhosphoSitePlus; Q76LX8; -.
BioMuta; ADAMTS13; -.
DMDM; 74749836; -.
PaxDb; Q76LX8; -.
PeptideAtlas; Q76LX8; -.
PRIDE; Q76LX8; -.
DNASU; 11093; -.
Ensembl; ENST00000355699; ENSP00000347927; ENSG00000160323. [Q76LX8-2]
Ensembl; ENST00000356589; ENSP00000348997; ENSG00000160323. [Q76LX8-3]
Ensembl; ENST00000371929; ENSP00000360997; ENSG00000160323. [Q76LX8-1]
Ensembl; ENST00000626597; ENSP00000486201; ENSG00000281244. [Q76LX8-1]
Ensembl; ENST00000626744; ENSP00000486734; ENSG00000281244. [Q76LX8-2]
Ensembl; ENST00000630465; ENSP00000485989; ENSG00000281244. [Q76LX8-3]
GeneID; 11093; -.
KEGG; hsa:11093; -.
UCSC; uc004cdv.6; human. [Q76LX8-1]
CTD; 11093; -.
DisGeNET; 11093; -.
EuPathDB; HostDB:ENSG00000160323.18; -.
GeneCards; ADAMTS13; -.
HGNC; HGNC:1366; ADAMTS13.
HPA; HPA042014; -.
HPA; HPA042844; -.
MalaCards; ADAMTS13; -.
MIM; 274150; phenotype.
MIM; 604134; gene.
neXtProt; NX_Q76LX8; -.
OpenTargets; ENSG00000160323; -.
Orphanet; 93583; Congenital thrombotic thrombocytopenic purpura due to ADAMTS-13 deficiency.
PharmGKB; PA24539; -.
eggNOG; KOG3538; Eukaryota.
eggNOG; ENOG410XPKZ; LUCA.
GeneTree; ENSGT00760000118885; -.
HOGENOM; HOG000231627; -.
HOVERGEN; HBG080358; -.
InParanoid; Q76LX8; -.
KO; K08627; -.
OMA; QCRVAFG; -.
OrthoDB; EOG091G14M8; -.
PhylomeDB; Q76LX8; -.
TreeFam; TF313537; -.
BRENDA; 3.4.24.87; 2681.
Reactome; R-HSA-5083635; Defective B3GALTL causes Peters-plus syndrome (PpS).
Reactome; R-HSA-5173214; O-glycosylation of TSR domain-containing proteins.
SIGNOR; Q76LX8; -.
EvolutionaryTrace; Q76LX8; -.
GeneWiki; ADAMTS13; -.
GenomeRNAi; 11093; -.
PRO; PR:Q76LX8; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000160323; -.
CleanEx; HS_ADAMTS13; -.
ExpressionAtlas; Q76LX8; baseline and differential.
Genevisible; Q76LX8; HS.
GO; GO:0009986; C:cell surface; NAS:UniProtKB.
GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IEA:Ensembl.
GO; GO:0005578; C:proteinaceous extracellular matrix; TAS:UniProtKB.
GO; GO:0005509; F:calcium ion binding; TAS:UniProtKB.
GO; GO:0005178; F:integrin binding; TAS:UniProtKB.
GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
GO; GO:0008237; F:metallopeptidase activity; TAS:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; NAS:UniProtKB.
GO; GO:0071346; P:cellular response to interferon-gamma; IEA:Ensembl.
GO; GO:0071353; P:cellular response to interleukin-4; IEA:Ensembl.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0009100; P:glycoprotein metabolic process; NAS:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; NAS:UniProtKB.
GO; GO:0043171; P:peptide catabolic process; IDA:UniProtKB.
GO; GO:0030168; P:platelet activation; NAS:UniProtKB.
GO; GO:0036066; P:protein O-linked fucosylation; TAS:Reactome.
GO; GO:0016485; P:protein processing; TAS:UniProtKB.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:0014075; P:response to amine; IEA:Ensembl.
GO; GO:0035864; P:response to potassium ion; IEA:Ensembl.
GO; GO:0009636; P:response to toxic substance; IEA:Ensembl.
Gene3D; 2.20.100.10; -; 7.
Gene3D; 2.60.120.290; -; 2.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR000859; CUB_dom.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR013273; Peptidase_M12B_ADAM-TS.
InterPro; IPR000884; TSP1_rpt.
Pfam; PF01421; Reprolysin; 1.
Pfam; PF00090; TSP_1; 4.
PRINTS; PR01857; ADAMTSFAMILY.
SMART; SM00608; ACR; 1.
SMART; SM00209; TSP1; 7.
SUPFAM; SSF49854; SSF49854; 2.
SUPFAM; SSF82895; SSF82895; 5.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS50092; TSP1; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Blood coagulation; Calcium;
Cleavage on pair of basic residues; Complete proteome;
Direct protein sequencing; Disease mutation; Disulfide bond;
Glycoprotein; Hemostasis; Hydrolase; Metal-binding; Metalloprotease;
Polymorphism; Protease; Reference proteome; Repeat; Secreted; Signal;
Zinc; Zymogen.
SIGNAL 1 29 {ECO:0000255}.
PROPEP 30 74 {ECO:0000269|PubMed:11535494,
ECO:0000269|PubMed:11535495,
ECO:0000269|PubMed:11574066}.
/FTId=PRO_0000247510.
CHAIN 75 1427 A disintegrin and metalloproteinase with
thrombospondin motifs 13.
/FTId=PRO_0000247511.
DOMAIN 80 286 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 287 383 Disintegrin.
DOMAIN 384 439 TSP type-1 1. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 682 730 TSP type-1 2. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 742 805 TSP type-1 3. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 808 859 TSP type-1 4. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 896 950 TSP type-1 5. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 951 1011 TSP type-1 6. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1012 1068 TSP type-1 7. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1072 1131 TSP type-1 8. {ECO:0000255|PROSITE-
ProRule:PRU00210}.
DOMAIN 1192 1298 CUB 1.
DOMAIN 1299 1427 CUB 2.
REGION 440 556 Cysteine-rich.
REGION 556 685 Spacer.
MOTIF 498 500 Cell attachment site. {ECO:0000255}.
ACT_SITE 225 225 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 83 83 Calcium. {ECO:0000255}.
METAL 173 173 Calcium. {ECO:0000255}.
METAL 182 182 Calcium; high affinity.
{ECO:0000269|PubMed:19047683}.
METAL 184 184 Calcium; high affinity.
{ECO:0000269|PubMed:19047683}.
METAL 187 187 Calcium; high affinity.
{ECO:0000269|PubMed:19047683}.
METAL 212 212 Calcium; high affinity.
{ECO:0000269|PubMed:19047683}.
METAL 224 224 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
METAL 228 228 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
METAL 234 234 Zinc; catalytic.
{ECO:0000250|UniProtKB:Q9UNA0}.
METAL 281 281 Calcium. {ECO:0000255}.
METAL 284 284 Calcium. {ECO:0000255}.
CARBOHYD 142 142 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 146 146 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 387 387 C-linked (Man) tryptophan.
{ECO:0000244|PDB:3VN4}.
CARBOHYD 399 399 O-linked (Fuc...) serine.
{ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4}.
CARBOHYD 552 552 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
CARBOHYD 579 579 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 614 614 N-linked (GlcNAc...) asparagine.
{ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19880749}.
CARBOHYD 667 667 N-linked (GlcNAc...) (complex)
asparagine. {ECO:0000269|PubMed:16335952,
ECO:0000269|PubMed:19139490}.
CARBOHYD 698 698 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 707 707 N-linked (GlcNAc...) (complex)
asparagine.
{ECO:0000269|PubMed:19139490}.
CARBOHYD 757 757 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 828 828 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 907 907 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 965 965 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 1027 1027 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 1087 1087 O-linked (Fuc...) serine.
{ECO:0000269|PubMed:17395589}.
CARBOHYD 1235 1235 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1354 1354 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:16335952}.
DISULFID 155 208 {ECO:0000250}.
DISULFID 202 281 {ECO:0000250}.
DISULFID 242 265 {ECO:0000250}.
DISULFID 311 337 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 322 347 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 332 366 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 360 371 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 396 433 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 400 438 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 411 423 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 450 487 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4}.
DISULFID 483 522 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 508 527 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 532 548 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
DISULFID 545 555 {ECO:0000244|PDB:3GHM,
ECO:0000244|PDB:3GHN,
ECO:0000244|PDB:3VN4,
ECO:0000269|PubMed:19880749}.
VAR_SEQ 2 329 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_055537.
VAR_SEQ 275 305 Missing (in isoform 3).
{ECO:0000303|PubMed:11867212}.
/FTId=VSP_020002.
VAR_SEQ 658 692 YRRYGEEYGNLTRPDITFTYFQPKPRQAWVWAAVR -> GG
VRAQLMHISWWSRPGLGERDLCARGRWPGGSSD (in
isoform 4). {ECO:0000303|Ref.5}.
/FTId=VSP_055538.
VAR_SEQ 693 1427 Missing (in isoform 4).
{ECO:0000303|Ref.5}.
/FTId=VSP_055539.
VAR_SEQ 1135 1190 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:11867212}.
/FTId=VSP_020003.
VARIANT 7 7 R -> W (does not affect protein
secretion; dbSNP:rs34024143).
{ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:16160007,
ECO:0000269|Ref.6}.
/FTId=VAR_027109.
VARIANT 79 79 I -> M (in TTP; dbSNP:rs281875297).
{ECO:0000269|PubMed:15009458}.
/FTId=VAR_067770.
VARIANT 88 88 V -> M (in TTP; reduces protein secretion
and proteolytic activity;
dbSNP:rs281875302).
{ECO:0000269|PubMed:16453338}.
/FTId=VAR_027110.
VARIANT 96 96 H -> D (in TTP; dbSNP:rs121908467).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027111.
VARIANT 102 102 R -> C (in TTP; dbSNP:rs121908469).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027112.
VARIANT 119 119 S -> F (in TTP; dbSNP:rs281875291).
{ECO:0000269|PubMed:18443791}.
/FTId=VAR_067771.
VARIANT 178 178 I -> T (in TTP; dbSNP:rs281875289).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067772.
VARIANT 193 193 R -> W (in TTP; low activity;
dbSNP:rs281875287).
{ECO:0000269|PubMed:14563640,
ECO:0000269|PubMed:19055667}.
/FTId=VAR_027113.
VARIANT 196 196 T -> I (in TTP; dbSNP:rs121908470).
{ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:14512317,
ECO:0000269|PubMed:16807643}.
/FTId=VAR_027114.
VARIANT 203 203 S -> P (in TTP; dbSNP:rs281875298).
{ECO:0000269|PubMed:15009458}.
/FTId=VAR_067773.
VARIANT 232 232 L -> Q (in TTP; dbSNP:rs281875292).
{ECO:0000269|PubMed:12393505}.
/FTId=VAR_067774.
VARIANT 234 234 H -> Q (in TTP; dbSNP:rs281875304).
{ECO:0000269|PubMed:16449289}.
/FTId=VAR_027115.
VARIANT 235 235 D -> H (in TTP; dbSNP:rs281875337).
{ECO:0000269|PubMed:12753286}.
/FTId=VAR_067775.
VARIANT 250 250 A -> V (in TTP; mild effect on protein
secretion; strong reduction of
proteolytic activity; dbSNP:rs121908478).
{ECO:0000269|PubMed:15126318}.
/FTId=VAR_027116.
VARIANT 263 263 S -> C (in TTP; dbSNP:rs281875293).
{ECO:0000269|PubMed:12393505,
ECO:0000269|PubMed:16807643}.
/FTId=VAR_067776.
VARIANT 268 268 R -> P (in TTP; affects protein
secretion; dbSNP:rs121908477).
{ECO:0000269|PubMed:12181489,
ECO:0000269|PubMed:15009458}.
/FTId=VAR_027117.
VARIANT 304 304 Y -> C (in TTP; dbSNP:rs281875285).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067777.
VARIANT 311 311 C -> Y (in TTP; dbSNP:rs281875336).
{ECO:0000269|PubMed:12753286}.
/FTId=VAR_067778.
VARIANT 339 339 T -> R (in dbSNP:rs149517360).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067779.
VARIANT 347 347 C -> S (in TTP; dbSNP:rs281875294).
{ECO:0000269|PubMed:16807643}.
/FTId=VAR_067780.
VARIANT 349 349 R -> C (in TTP; dbSNP:rs281875288).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067781.
VARIANT 353 353 P -> L (in TTP; dbSNP:rs281875338).
{ECO:0000269|PubMed:12393505,
ECO:0000269|PubMed:12753286,
ECO:0000269|PubMed:16807643}.
/FTId=VAR_067782.
VARIANT 390 390 W -> C (in TTP; dbSNP:rs281875306).
{ECO:0000269|PubMed:15327386}.
/FTId=VAR_027118.
VARIANT 398 398 R -> H (in TTP; dbSNP:rs121908471).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027119.
VARIANT 448 448 Q -> E (does not affect protein
secretion; normal proteolytic activity;
dbSNP:rs2301612).
{ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:12181489,
ECO:0000269|PubMed:12975309,
ECO:0000269|PubMed:14512317,
ECO:0000269|PubMed:14563640,
ECO:0000269|PubMed:16160007,
ECO:0000269|PubMed:17003922,
ECO:0000269|PubMed:19055667,
ECO:0000269|Ref.6}.
/FTId=VAR_027120.
VARIANT 456 456 Q -> H (in dbSNP:rs36220239).
{ECO:0000269|Ref.6}.
/FTId=VAR_027162.
VARIANT 457 457 P -> L (in dbSNP:rs36220240).
{ECO:0000269|PubMed:12753286,
ECO:0000269|Ref.6}.
/FTId=VAR_027163.
VARIANT 475 475 P -> S (in dbSNP:rs11575933).
{ECO:0000269|PubMed:12181489}.
/FTId=VAR_027121.
VARIANT 507 507 R -> Q (in TTP; dbSNP:rs281875296).
{ECO:0000269|PubMed:15009458,
ECO:0000269|PubMed:16807643}.
/FTId=VAR_067783.
VARIANT 508 508 C -> Y (in TTP; impairs protein
secretion; dbSNP:rs281875305).
{ECO:0000269|PubMed:12181489}.
/FTId=VAR_027122.
VARIANT 525 525 G -> D (in TTP; dbSNP:rs281875286).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067784.
VARIANT 528 528 R -> G (in TTP; dbSNP:rs121908473).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027123.
VARIANT 596 596 A -> V (in TTP; dbSNP:rs281875299).
{ECO:0000269|PubMed:15009458}.
/FTId=VAR_067785.
VARIANT 606 606 A -> P (in TTP; dbSNP:rs281875290).
{ECO:0000269|PubMed:19055667}.
/FTId=VAR_067786.
VARIANT 618 618 P -> A (in dbSNP:rs28647808).
{ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:16160007,
ECO:0000269|PubMed:19055667,
ECO:0000269|Ref.6}.
/FTId=VAR_027124.
VARIANT 625 625 R -> H (in dbSNP:rs36090624).
{ECO:0000269|PubMed:11586351,
ECO:0000269|Ref.6}.
/FTId=VAR_027125.
VARIANT 658 658 Y -> C (in TTP; dbSNP:rs281875335).
{ECO:0000269|PubMed:22075512}.
/FTId=VAR_067787.
VARIANT 671 671 P -> L (in TTP; dbSNP:rs281875295).
{ECO:0000269|PubMed:16807643}.
/FTId=VAR_067788.
VARIANT 673 673 I -> F (in TTP; impairs protein
secretion; dbSNP:rs281875307).
{ECO:0000269|PubMed:14563640}.
/FTId=VAR_027126.
VARIANT 692 692 R -> C (in TTP; dbSNP:rs121908475).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027127.
VARIANT 732 732 A -> V (in dbSNP:rs41314453).
{ECO:0000269|PubMed:11586351,
ECO:0000269|PubMed:12614216,
ECO:0000269|PubMed:16160007}.
/FTId=VAR_027128.
VARIANT 740 740 E -> K (in dbSNP:rs36221451).
{ECO:0000269|Ref.6}.
/FTId=VAR_027164.
VARIANT 758 758 C -> R (in TTP; dbSNP:rs281875300).
{ECO:0000269|PubMed:15009458}.
/FTId=VAR_067789.
VARIANT 900 900 A -> V (in dbSNP:rs685523).
{ECO:0000269|PubMed:11557746,
ECO:0000269|PubMed:11586351,
ECO:0000269|Ref.6}.
/FTId=VAR_027129.
VARIANT 903 903 S -> L (in dbSNP:rs78977446).
{ECO:0000269|PubMed:16449289,
ECO:0000269|PubMed:16468327}.
/FTId=VAR_027130.
VARIANT 908 908 C -> S (in TTP; dbSNP:rs281875301).
{ECO:0000269|PubMed:15009458}.
/FTId=VAR_067790.
VARIANT 908 908 C -> Y (in TTP; impairs protein
secretion; dbSNP:rs281875301).
{ECO:0000269|PubMed:14563640}.
/FTId=VAR_027131.
VARIANT 951 951 C -> G (in TTP; dbSNP:rs121908468).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027132.
VARIANT 977 979 CAR -> W (in TTP).
{ECO:0000269|PubMed:19116307}.
/FTId=VAR_067791.
VARIANT 982 982 G -> R (in dbSNP:rs36222275).
{ECO:0000269|Ref.6}.
/FTId=VAR_027165.
VARIANT 1024 1024 C -> G (in TTP; dbSNP:rs121908472).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027133.
VARIANT 1033 1033 A -> T (in dbSNP:rs28503257).
{ECO:0000269|PubMed:11586351,
ECO:0000269|Ref.6}.
/FTId=VAR_027134.
VARIANT 1060 1060 R -> W (in TTP; affects protein
secretion; the mutant protein has reduced
protease activity; dbSNP:rs142572218).
{ECO:0000269|PubMed:16796708,
ECO:0000269|PubMed:16807643,
ECO:0000269|PubMed:17003922}.
/FTId=VAR_067792.
VARIANT 1095 1095 R -> W (in a patient with thrombotic
thrombocytopenic purpura;
dbSNP:rs782383410).
{ECO:0000269|PubMed:16468327}.
/FTId=VAR_027135.
VARIANT 1123 1123 R -> C (in TTP; impairs protein
secretion; the mutant protein has reduced
protease activity; dbSNP:rs281875340).
{ECO:0000269|PubMed:14563640,
ECO:0000269|PubMed:17003922}.
/FTId=VAR_027136.
VARIANT 1213 1213 C -> Y (in TTP; dbSNP:rs121908474).
{ECO:0000269|PubMed:11586351}.
/FTId=VAR_027137.
VARIANT 1219 1219 R -> W (in TTP; affects protein
secretion; the mutant protein has reduced
protease activity; dbSNP:rs281875339).
{ECO:0000269|PubMed:17003922}.
/FTId=VAR_067793.
VARIANT 1226 1226 T -> I (in dbSNP:rs36222894).
{ECO:0000269|Ref.6}.
/FTId=VAR_027166.
VARIANT 1239 1239 G -> V (in TTP; impairs protein
secretion; dbSNP:rs281875303).
{ECO:0000269|PubMed:16453338}.
/FTId=VAR_027138.
VARIANT 1314 1314 S -> L (found in a patient with hemolytic
uremic syndrome; dbSNP:rs142060916).
{ECO:0000269|PubMed:21488199}.
/FTId=VAR_067794.
VARIANT 1336 1336 R -> W (in TTP; impairs protein secretion
and proteolytic activity;
dbSNP:rs281875308).
{ECO:0000269|PubMed:12614216,
ECO:0000269|PubMed:16160007}.
/FTId=VAR_027139.
MUTAGEN 71 71 R->K: Abolishes pro-domain removal but no
loss of proteolytic activity; when
associated with D-73.
{ECO:0000269|PubMed:12975358}.
MUTAGEN 73 73 R->D: Abolishes pro-domain removal but no
loss of proteolytic activity; when
associated with K-71.
{ECO:0000269|PubMed:12975358}.
MUTAGEN 83 83 E->A: No change in calcium dependence for
proteolysis.
{ECO:0000269|PubMed:19047683}.
MUTAGEN 173 173 D->A: No change in calcium dependence for
proteolysis.
{ECO:0000269|PubMed:19047683}.
MUTAGEN 184 184 E->A: Dramatically reduced affinity for
calcium. {ECO:0000269|PubMed:19047683}.
MUTAGEN 187 187 D->A: Dramatically reduced affinity for
calcium. {ECO:0000269|PubMed:19047683}.
MUTAGEN 212 212 E->A: Dramatically reduced affinity for
calcium. {ECO:0000269|PubMed:19047683}.
MUTAGEN 399 399 S->A: No effect on cleavage of VWF and
little change in secretion of ADAMTS13.
Abolishes secretion of ADAMTS13; when
associated with A-698.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 698 698 S->A: No effect on cleavage of VWF and
greatly reduced secretion of ADAMTS13.
Abolishes secretion of ADAMTS13; when
associated with A-399.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 757 757 S->A: No effect on cleavage of VWF and
little change in secretion of ADAMTS13.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 907 907 S->A: No effect on cleavage of VWF and
greatly reduced secretion of ADAMTS13.
Abolishes most of the secretion of
ADAMTS13; when associated with A-965.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 965 965 S->A: No effect on cleavage of VWF and
little change in secretion of ADAMTS13.
Abolishes most of the secretion of
ADAMTS13; when associated with A-907.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 1027 1027 S->A: No effect on cleavage of VWF and
little change in secretion of ADAMTS13.
Abolishes most of the secretion of
ADAMTS13; when associated with A-1087.
{ECO:0000269|PubMed:17395589}.
MUTAGEN 1087 1087 S->A: No effect on cleavage of VWF and
little change in secretion of ADAMTS13.
Abolishes most of the secretion of
ADAMTS13; when associated with A-1027.
{ECO:0000269|PubMed:17395589}.
CONFLICT 101 101 E -> R (in Ref. 1; AA sequence).
{ECO:0000305}.
HELIX 301 303 {ECO:0000244|PDB:3GHM}.
HELIX 307 314 {ECO:0000244|PDB:3GHM}.
HELIX 331 334 {ECO:0000244|PDB:3GHN}.
STRAND 337 340 {ECO:0000244|PDB:3GHM}.
STRAND 348 351 {ECO:0000244|PDB:3VN4}.
STRAND 359 361 {ECO:0000244|PDB:3GHM}.
STRAND 364 367 {ECO:0000244|PDB:3GHM}.
STRAND 370 373 {ECO:0000244|PDB:3GHM}.
HELIX 374 377 {ECO:0000244|PDB:3GHM}.
STRAND 399 401 {ECO:0000244|PDB:3GHM}.
STRAND 403 406 {ECO:0000244|PDB:3GHM}.
STRAND 417 419 {ECO:0000244|PDB:3GHM}.
STRAND 430 433 {ECO:0000244|PDB:3GHM}.
HELIX 442 451 {ECO:0000244|PDB:3GHM}.
TURN 452 455 {ECO:0000244|PDB:3GHM}.
STRAND 470 472 {ECO:0000244|PDB:3GHM}.
TURN 474 476 {ECO:0000244|PDB:3GHM}.
HELIX 479 483 {ECO:0000244|PDB:3GHM}.
STRAND 486 489 {ECO:0000244|PDB:3GHM}.
STRAND 495 497 {ECO:0000244|PDB:3GHM}.
STRAND 519 523 {ECO:0000244|PDB:3GHM}.
STRAND 526 530 {ECO:0000244|PDB:3GHM}.
STRAND 534 536 {ECO:0000244|PDB:3GHM}.
STRAND 554 562 {ECO:0000244|PDB:3GHM}.
STRAND 569 576 {ECO:0000244|PDB:3GHM}.
STRAND 581 588 {ECO:0000244|PDB:3GHM}.
STRAND 592 599 {ECO:0000244|PDB:3GHM}.
STRAND 602 605 {ECO:0000244|PDB:3GHM}.
STRAND 608 610 {ECO:0000244|PDB:3GHM}.
STRAND 614 618 {ECO:0000244|PDB:3GHM}.
STRAND 623 632 {ECO:0000244|PDB:3GHM}.
STRAND 634 636 {ECO:0000244|PDB:3GHM}.
STRAND 638 647 {ECO:0000244|PDB:3GHM}.
STRAND 653 661 {ECO:0000244|PDB:3GHM}.
HELIX 663 665 {ECO:0000244|PDB:3GHM}.
HELIX 667 669 {ECO:0000244|PDB:3GHN}.
STRAND 673 680 {ECO:0000244|PDB:3GHM}.
SEQUENCE 1427 AA; 153604 MW; A2103AFABC1A4445 CRC64;
MHQRHPRARC PPLCVAGILA CGFLLGCWGP SHFQQSCLQA LEPQAVSSYL SPGAPLKGRP
PSPGFQRQRQ RQRRAAGGIL HLELLVAVGP DVFQAHQEDT ERYVLTNLNI GAELLRDPSL
GAQFRVHLVK MVILTEPEGA PNITANLTSS LLSVCGWSQT INPEDDTDPG HADLVLYITR
FDLELPDGNR QVRGVTQLGG ACSPTWSCLI TEDTGFDLGV TIAHEIGHSF GLEHDGAPGS
GCGPSGHVMA SDGAAPRAGL AWSPCSRRQL LSLLSAGRAR CVWDPPRPQP GSAGHPPDAQ
PGLYYSANEQ CRVAFGPKAV ACTFAREHLD MCQALSCHTD PLDQSSCSRL LVPLLDGTEC
GVEKWCSKGR CRSLVELTPI AAVHGRWSSW GPRSPCSRSC GGGVVTRRRQ CNNPRPAFGG
RACVGADLQA EMCNTQACEK TQLEFMSQQC ARTDGQPLRS SPGGASFYHW GAAVPHSQGD
ALCRHMCRAI GESFIMKRGD SFLDGTRCMP SGPREDGTLS LCVSGSCRTF GCDGRMDSQQ
VWDRCQVCGG DNSTCSPRKG SFTAGRAREY VTFLTVTPNL TSVYIANHRP LFTHLAVRIG
GRYVVAGKMS ISPNTTYPSL LEDGRVEYRV ALTEDRLPRL EEIRIWGPLQ EDADIQVYRR
YGEEYGNLTR PDITFTYFQP KPRQAWVWAA VRGPCSVSCG AGLRWVNYSC LDQARKELVE
TVQCQGSQQP PAWPEACVLE PCPPYWAVGD FGPCSASCGG GLRERPVRCV EAQGSLLKTL
PPARCRAGAQ QPAVALETCN PQPCPARWEV SEPSSCTSAG GAGLALENET CVPGADGLEA
PVTEGPGSVD EKLPAPEPCV GMSCPPGWGH LDATSAGEKA PSPWGSIRTG AQAAHVWTPA
AGSCSVSCGR GLMELRFLCM DSALRVPVQE ELCGLASKPG SRREVCQAVP CPARWQYKLA
ACSVSCGRGV VRRILYCARA HGEDDGEEIL LDTQCQGLPR PEPQEACSLE PCPPRWKVMS
LGPCSASCGL GTARRSVACV QLDQGQDVEV DEAACAALVR PEASVPCLIA DCTYRWHVGT
WMECSVSCGD GIQRRRDTCL GPQAQAPVPA DFCQHLPKPV TVRGCWAGPC VGQGTPSLVP
HEEAAAPGRT TATPAGASLE WSQARGLLFS PAPQPRRLLP GPQENSVQSS ACGRQHLEPT
GTIDMRGPGQ ADCAVAIGRP LGEVVTLRVL ESSLNCSAGD MLLLWGRLTW RKMCRKLLDM
TFSSKTNTLV VRQRCGRPGG GVLLRYGSQL APETFYRECD MQLFGPWGEI VSPSLSPATS
NAGGCRLFIN VAPHARIAIH ALATNMGAGT EGANASYILI RDTHSLRTTA FHGQQVLYWE
SESSQAEMEF SEGFLKAQAS LRGQYWTLQS WVPEMQDPQS WKGKEGT


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