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Heparanase (EC 3.2.1.166) (Endo-glucoronidase) (Heparanase-1) (Hpa1) [Cleaved into: Heparanase 8 kDa subunit; Heparanase 50 kDa subunit]

 HPSE_HUMAN              Reviewed;         543 AA.
Q9Y251; A9JIG7; C7F7I3; C7F7I4; E9PCA9; E9PGR1; Q53GE5; Q9UL39;
11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 2.
27-SEP-2017, entry version 153.
RecName: Full=Heparanase;
EC=3.2.1.166;
AltName: Full=Endo-glucoronidase;
AltName: Full=Heparanase-1;
Short=Hpa1;
Contains:
RecName: Full=Heparanase 8 kDa subunit;
Contains:
RecName: Full=Heparanase 50 kDa subunit;
Flags: Precursor;
Name=HPSE; Synonyms=HEP, HPA, HPA1, HPR1, HPSE1, HSE1;
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), VARIANT ARG-307, AND TISSUE
SPECIFICITY.
TISSUE=Placenta;
PubMed=10405343; DOI=10.1006/bbrc.1999.0962;
Kussie P.H., Hulmes J.D., Ludwig D.L., Patel S., Navarro E.C.,
Seddon A.P., Giorgio N.A., Bohlen P.;
"Cloning and functional expression of a human heparanase gene.";
Biochem. Biophys. Res. Commun. 261:183-187(1999).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES,
PROTEIN SEQUENCE OF 158-168; 326-337 AND 447-491, AND VARIANT ARG-307.
TISSUE=Embryonic fibroblast;
PubMed=10446189; DOI=10.1074/jbc.274.34.24153;
Toyoshima M., Nakajima M.;
"Human heparanase. Purification, characterization, cloning, and
expression.";
J. Biol. Chem. 274:24153-24160(1999).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), GLYCOSYLATION, PROTEOLYTIC
PROCESSING, AND VARIANT ARG-307.
PubMed=10395325; DOI=10.1038/10518;
Vlodavsky I., Friedmann Y., Elkin M., Aingorn H., Atzmon R.,
Ishai-Michaeli R., Bitan M., Pappo O., Peretz T., Michal I.,
Spector L., Pecker I.;
"Mammalian heparanase: gene cloning, expression and function in tumor
progression and metastasis.";
Nat. Med. 5:793-802(1999).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, PROTEIN
SEQUENCE OF 158-174; 263-272; 326-337; 433-436; 438-443; 466-468 AND
478-483, AND VARIANT ARG-307.
TISSUE=Placenta;
PubMed=10395326; DOI=10.1038/10525;
Hulett M.D., Freeman C., Hamdorf B.J., Baker R.T., Harris M.J.,
Parish C.R.;
"Cloning of mammalian heparanase, an important enzyme in tumor
invasion and metastasis.";
Nat. Med. 5:803-809(1999).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES,
TISSUE SPECIFICITY, AND VARIANT ARG-307.
TISSUE=Placenta;
PubMed=10764835; DOI=10.1093/glycob/10.5.467;
Dempsey L.A., Plummer T.B., Coombes S.L., Platt J.L.;
"Heparanase expression in invasive trophoblasts and acute vascular
damage.";
Glycobiology 10:467-475(2000).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND SUBCELLULAR LOCATION.
PubMed=11547900; DOI=10.1023/A:1011375624902;
Zcharia E., Metzger S., Chajek-Shaul T., Friedmann Y., Pappo O.,
Aviv A., Elkin M., Pecker I., Peretz T., Vlodavsky I.;
"Molecular properties and involvement of heparanase in cancer
progression and mammary gland morphogenesis.";
J. Mammary Gland Biol. Neoplasia 6:311-322(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 36-41 AND
158-163, SUBUNIT, GLYCOSYLATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
TISSUE=Placenta;
PubMed=12713442; DOI=10.1042/BJ20030318;
McKenzie E., Young K., Hircock M., Bennett J., Bhaman M., Felix R.,
Turner P., Stamps A., McMillan D., Saville G., Ng S., Mason S.,
Snell D., Schofield D., Gong H., Townsend R., Gallagher J., Page M.,
Parekh R., Stubberfield C.;
"Biochemical characterization of the active heterodimer form of human
heparanase (Hpa1) protein expressed in insect cells.";
Biochem. J. 373:423-435(2003).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), ALTERNATIVE SPLICING, AND
VARIANT ARG-307.
TISSUE=Kidney;
PubMed=17208203; DOI=10.1016/j.bbrc.2006.12.189;
Nasser N.J., Avivi A., Shushy M., Vlodavsky I., Nevo E.;
"Cloning, expression, and characterization of an alternatively spliced
variant of human heparanase.";
Biochem. Biophys. Res. Commun. 354:33-38(2007).
[9]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ARG-307.
Pinhal M.A., Semedo P.;
"Cloned heparanase from MCF-7 cells.";
Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4), AND VARIANT ARG-307.
Jin S., Yu L., Gong F.;
"Two new transcript variants of Homo sapiens heparanase (HPSE).";
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-307.
TISSUE=Small intestine;
Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
Tanaka A., Yokoyama S.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
ARG-307.
TISSUE=Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[14]
MUTAGENESIS OF GLU-225; GLU-343 AND ASP-367.
PubMed=11123890; DOI=10.1021/bi002080p;
Hulett M.D., Hornby J.R., Ohms S.J., Zuegg J., Freeman C.,
Gready J.E., Parish C.R.;
"Identification of active-site residues of the pro-metastatic
endoglycosidase heparanase.";
Biochemistry 39:15659-15667(2000).
[15]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND INTERACTION WITH
SDC1.
PubMed=12441129; DOI=10.1006/excr.2002.5651;
Goldshmidt O., Nadav L., Aingorn H., Irit C., Feinstein N., Ilan N.,
Zamir E., Geiger B., Vlodavsky I., Katz B.Z.;
"Human heparanase is localized within lysosomes in a stable form.";
Exp. Cell Res. 281:50-62(2002).
[16]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=12213822; DOI=10.1074/jbc.M206510200;
Okada Y., Yamada S., Toyoshima M., Dong J., Nakajima M., Sugahara K.;
"Structural recognition by recombinant human heparanase that plays
critical roles in tumor metastasis. Hierarchical sulfate groups with
different effects and the essential target disulfated trisaccharide
sequence.";
J. Biol. Chem. 277:42488-42495(2002).
[17]
PROTEOLYTIC PROCESSING, ENZYME ACTIVITY, AND SUBCELLULAR LOCATION.
PubMed=11973358;
Nadav L., Eldor A., Yacoby-Zeevi O., Zamir E., Pecker I., Ilan N.,
Geiger B., Vlodavsky I., Katz B.Z.;
"Activation, processing and trafficking of extracellular heparanase by
primary human fibroblasts.";
J. Cell Sci. 115:2179-2187(2002).
[18]
HETERODIMERIZATION, AND ENZYME ACTIVITY.
PubMed=12927802; DOI=10.1016/S0006-291X(03)01478-5;
Levy-Adam F., Miao H.Q., Heinrikson R.L., Vlodavsky I., Ilan N.;
"Heterodimer formation is essential for heparanase enzymatic
activity.";
Biochem. Biophys. Res. Commun. 308:885-891(2003).
[19]
FUNCTION, AND MUTAGENESIS OF GLU-225.
PubMed=12773484; DOI=10.1096/fj.02-0773com;
Goldshmidt O., Zcharia E., Cohen M., Aingorn H., Cohen I., Nadav L.,
Katz B.Z., Geiger B., Vlodavsky I.;
"Heparanase mediates cell adhesion independent of its enzymatic
activity.";
FASEB J. 17:1015-1025(2003).
[20]
GLYCOSYLATION AT ASN-162; ASN-178; ASN-200; ASN-217; ASN-238 AND
ASN-459, AND MUTAGENESIS OF ASN-162; ASN-178; ASN-200; ASN-217;
ASN-238 AND ASN-459.
PubMed=14573609; DOI=10.1074/jbc.M300541200;
Simizu S., Ishida K., Wierzba M.K., Osada H.;
"Secretion of heparanase protein is regulated by glycosylation in
human tumor cell lines.";
J. Biol. Chem. 279:2697-2703(2004).
[21]
FUNCTION.
PubMed=15044433; DOI=10.1074/jbc.M400554200;
Gingis-Velitski S., Zetser A., Flugelman M.Y., Vlodavsky I., Ilan N.;
"Heparanase induces endothelial cell migration via protein kinase
B/Akt activation.";
J. Biol. Chem. 279:23536-23541(2004).
[22]
SUBCELLULAR LOCATION.
PubMed=15292202; DOI=10.1074/jbc.M402131200;
Gingis-Velitski S., Zetser A., Kaplan V., Ben-Zaken O., Cohen E.,
Levy-Adam F., Bashenko Y., Flugelman M.Y., Vlodavsky I., Ilan N.;
"Heparanase uptake is mediated by cell membrane heparan sulfate
proteoglycans.";
J. Biol. Chem. 279:44084-44092(2004).
[23]
PROTEOLYTIC PROCESSING, AND SUBCELLULAR LOCATION.
PubMed=15126626; DOI=10.1242/jcs.01068;
Zetser A., Levy-Adam F., Kaplan V., Gingis-Velitski S., Bashenko Y.,
Schubert S., Flugelman M.Y., Vlodavsky I., Ilan N.;
"Processing and activation of latent heparanase occurs in lysosomes.";
J. Cell Sci. 117:2249-2258(2004).
[24]
BIOPHYSICOCHEMICAL PROPERTIES, PROTEOLYTIC PROCESSING, AND SUBCELLULAR
LOCATION.
PubMed=15848168; DOI=10.1016/j.febslet.2005.03.030;
Cohen E., Atzmon R., Vlodavsky I., Ilan N.;
"Heparanase processing by lysosomal/endosomal protein preparation.";
FEBS Lett. 579:2334-2338(2005).
[25]
SUBCELLULAR LOCATION, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
TYR-156.
PubMed=15659389; DOI=10.1074/jbc.M413370200;
Abboud-Jarrous G., Rangini-Guetta Z., Aingorn H., Atzmon R.,
Elgavish S., Peretz T., Vlodavsky I.;
"Site-directed mutagenesis, proteolytic cleavage, and activation of
human proheparanase.";
J. Biol. Chem. 280:13568-13575(2005).
[26]
HEPARIN/HS-BINDING DOMAINS, AND MUTAGENESIS OF LYS-158 AND LYS-161.
PubMed=15760902; DOI=10.1074/jbc.M414546200;
Levy-Adam F., Abboud-Jarrous G., Guerrini M., Beccati D.,
Vlodavsky I., Ilan N.;
"Identification and characterization of heparin/heparan sulfate
binding domains of the endoglycosidase heparanase.";
J. Biol. Chem. 280:20457-20466(2005).
[27]
FUNCTION.
PubMed=16452201; DOI=10.1158/0008-5472.CAN-05-1811;
Zetser A., Bashenko Y., Edovitsky E., Levy-Adam F., Vlodavsky I.,
Ilan N.;
"Heparanase induces vascular endothelial growth factor expression:
correlation with p38 phosphorylation levels and Src activation.";
Cancer Res. 66:1455-1463(2006).
[28]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217.
TISSUE=Platelet;
PubMed=16263699; DOI=10.1074/mcp.M500324-MCP200;
Lewandrowski U., Moebius J., Walter U., Sickmann A.;
"Elucidation of N-glycosylation sites on human platelet proteins: a
glycoproteomic approach.";
Mol. Cell. Proteomics 5:226-233(2006).
[29]
TISSUE SPECIFICITY, AND FUNCTION.
PubMed=18557927; DOI=10.1111/j.1600-0625.2008.00739.x;
Malgouries S., Donovan M., Thibaut S., Bernard B.A.;
"Heparanase 1: a key participant of inner root sheath differentiation
program and hair follicle homeostasis.";
Exp. Dermatol. 17:1017-1023(2008).
[30]
FUNCTION.
PubMed=18798279; DOI=10.1002/ijc.23898;
Cohen-Kaplan V., Naroditsky I., Zetser A., Ilan N., Vlodavsky I.,
Doweck I.;
"Heparanase induces VEGF C and facilitates tumor lymphangiogenesis.";
Int. J. Cancer 123:2566-2573(2008).
[31]
FUNCTION OF THE C-TERMINAL DOMAIN, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF VAL-414; LYS-417; PRO-525; PHE-527; SER-528; TYR-529;
PHE-531; VAL-533; ILE-534; ARG-535; ASN-536; ALA-537; LYS-538;
VAL-539; ALA-540; ALA-541 AND CYS-542.
PubMed=19244131; DOI=10.1158/0008-5472.CAN-08-1837;
Fux L., Feibish N., Cohen-Kaplan V., Gingis-Velitski S., Feld S.,
Geffen C., Vlodavsky I., Ilan N.;
"Structure-function approach identifies a COOH-terminal domain that
mediates heparanase signaling.";
Cancer Res. 69:1758-1767(2009).
[32]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-217 AND ASN-238.
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).
[33]
FUNCTION.
PubMed=20097882; DOI=10.1182/blood-2009-07-234757;
Purushothaman A., Uyama T., Kobayashi F., Yamada S., Sugahara K.,
Rapraeger A.C., Sanderson R.D.;
"Heparanase-enhanced shedding of syndecan-1 by myeloma cells promotes
endothelial invasion and angiogenesis.";
Blood 115:2449-2457(2010).
[34]
INTERACTION WITH TF, AND ENZYME ACTIVITY.
PubMed=20634491; DOI=10.3324/haematol.2010.023713;
Nadir Y., Brenner B., Fux L., Shafat I., Attias J., Vlodavsky I.;
"Heparanase enhances the generation of activated factor X in the
presence of tissue factor and activated factor VII.";
Haematologica 95:1927-1934(2010).
[35]
INTERACTION WITH HRG, ENZYME ACTIVITY, AND FUNCTION.
PubMed=20561914; DOI=10.1016/j.biocel.2010.05.008;
Poon I.K., Yee D.Y., Jones A.L., Wood R.J., Davis D.S., Freeman C.,
Parish C.R., Hulett M.D.;
"Histidine-rich glycoprotein binds heparanase and regulates its
enzymatic activity and cell surface interactions.";
Int. J. Biochem. Cell Biol. 42:1507-1516(2010).
[36]
CATALYTIC ACTIVITY, AND FUNCTION.
PubMed=20181948; DOI=10.1074/jbc.M110.104166;
Peterson S.B., Liu J.;
"Unraveling the specificity of heparanase utilizing synthetic
substrates.";
J. Biol. Chem. 285:14504-14513(2010).
[37]
INTERACTION WITH HPSE2.
PubMed=20576607; DOI=10.1074/jbc.M110.116384;
Levy-Adam F., Feld S., Cohen-Kaplan V., Shteingauz A., Gross M.,
Arvatz G., Naroditsky I., Ilan N., Doweck I., Vlodavsky I.;
"Heparanase 2 interacts with heparan sulfate with high affinity and
inhibits heparanase activity.";
J. Biol. Chem. 285:28010-28019(2010).
[38]
FUNCTION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=20309870; DOI=10.1002/jor.21138;
Smith P.N., Freeman C., Yu D., Chen M., Gatenby P.A., Parish C.R.,
Li R.W.;
"Heparanase in primary human osteoblasts.";
J. Orthop. Res. 28:1315-1322(2010).
[39]
FUNCTION.
PubMed=21131364; DOI=10.1074/jbc.M110.183277;
Ramani V.C., Yang Y., Ren Y., Nan L., Sanderson R.D.;
"Heparanase plays a dual role in driving hepatocyte growth factor
(HGF) signaling by enhancing HGF expression and activity.";
J. Biol. Chem. 286:6490-6499(2011).
[40]
VARIANT SER-260.
PubMed=15334672; DOI=10.3748/wjg.v10.i19.2795;
Chen X.P., Liu Y.B., Rui J., Peng S.Y., Peng C.H., Zhou Z.Y.,
Shi L.H., Shen H.W., Xu B.;
"Heparanase mRNA expression and point mutation in hepatocellular
carcinoma.";
World J. Gastroenterol. 10:2795-2799(2004).
-!- FUNCTION: Endoglycosidase that cleaves heparan sulfate
proteoglycans (HSPGs) into heparan sulfate side chains and core
proteoglycans. Participates in extracellular matrix (ECM)
degradation and remodeling. Selectively cleaves the linkage
between a glucuronic acid unit and an N-sulfo glucosamine unit
carrying either a 3-O-sulfo or a 6-O-sulfo group. Can also cleave
the linkage between a glucuronic acid unit and an N-sulfo
glucosamine unit carrying a 2-O-sulfo group, but not linkages
between a glucuronic acid unit and a 2-O-sulfated iduronic acid
moiety. It is essentially inactive at neutral pH but becomes
active under acidic conditions such as during tumor invasion and
in inflammatory processes. Facilitates cell migration associated
with metastasis, wound healing and inflammation. Enhances shedding
of syndecans, and increases endothelial invasion and angiogenesis
in myelomas. Acts as procoagulant by increasing the generation of
activation factor X in the presence of tissue factor and
activation factor VII. Increases cell adhesion to the
extracellular matrix (ECM), independent of its enzymatic activity.
Induces AKT1/PKB phosphorylation via lipid rafts increasing cell
mobility and invasion. Heparin increases this AKT1/PKB activation.
Regulates osteogenesis. Enhances angiogenesis through up-
regulation of SRC-mediated activation of VEGF. Implicated in hair
follicle inner root sheath differentiation and hair homeostasis.
{ECO:0000269|PubMed:12213822, ECO:0000269|PubMed:12773484,
ECO:0000269|PubMed:15044433, ECO:0000269|PubMed:16452201,
ECO:0000269|PubMed:18557927, ECO:0000269|PubMed:18798279,
ECO:0000269|PubMed:19244131, ECO:0000269|PubMed:20097882,
ECO:0000269|PubMed:20181948, ECO:0000269|PubMed:20309870,
ECO:0000269|PubMed:20561914, ECO:0000269|PubMed:21131364}.
-!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glycosidic
bonds of heparan sulfate chains in heparan sulfate proteoglycan.
{ECO:0000269|PubMed:11973358, ECO:0000269|PubMed:12213822,
ECO:0000269|PubMed:12927802, ECO:0000269|PubMed:20181948,
ECO:0000269|PubMed:20561914, ECO:0000269|PubMed:20634491}.
-!- ENZYME REGULATION: Inhibited by EDTA, laminarin sulfate and, to a
lower extent, by heparin and sulfamin and activated by calcium and
magnesium. {ECO:0000250}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is 4-6. {ECO:0000269|PubMed:10446189,
ECO:0000269|PubMed:10764835, ECO:0000269|PubMed:12713442,
ECO:0000269|PubMed:15848168};
-!- SUBUNIT: Heterodimer; heterodimer formation between the 8 kDa and
the 50 kDa subunits is required for enzyme activity. Interacts
with TF; the interaction, inhibited by heparin, enhances the
generation of activated factor X and activates coagulation.
Interacts with HRG; the interaction is enhanced at acidic pH,
partially inhibits binding of HPSE to cell surface receptors and
modulates its enzymatic activity. Interacts with SDC1; the
interaction enhances the shedding of SDC1. Interacts with HPSE2.
{ECO:0000269|PubMed:12441129, ECO:0000269|PubMed:12713442,
ECO:0000269|PubMed:20561914, ECO:0000269|PubMed:20576607,
ECO:0000269|PubMed:20634491}.
-!- SUBCELLULAR LOCATION: Lysosome membrane; Peripheral membrane
protein. Secreted. Nucleus. Note=Proheparanase is secreted via
vesicles of the Golgi. Interacts with cell membrane heparan
sulfate proteoglycans (HSPGs). Endocytosed and accumulates in
endosomes. Transferred to lysosomes where it is proteolytically
cleaved to produce the active enzyme. Under certain stimuli,
transferred to the cell surface. Associates with lipid rafts.
Colocalizes with SDC1 in endosomal/lysosomal vesicles. Accumulates
in perinuclear lysosomal vesicles. Heparin retains proheparanase
in the extracellular medium (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q9Y251-1; Sequence=Displayed;
Name=2; Synonyms=55 kDa, splice 5;
IsoId=Q9Y251-2; Sequence=VSP_044537;
Note=Escapes proteolytic cleavage, devoid of HS degradation
activity.;
Name=3; Synonyms=ex9-10del;
IsoId=Q9Y251-3; Sequence=VSP_044664;
Name=4; Synonyms=ex10del;
IsoId=Q9Y251-4; Sequence=VSP_053730, VSP_053731;
-!- TISSUE SPECIFICITY: Highly expressed in placenta and spleen and
weakly expressed in lymph node, thymus, peripheral blood
leukocytes, bone marrow, endothelial cells, fetal liver and tumor
tissues. Also expressed in hair follicles, specifically in both
Henle's and Huxley's layers of inner the root sheath (IRS) at
anagen phase. {ECO:0000269|PubMed:10395326,
ECO:0000269|PubMed:10405343, ECO:0000269|PubMed:10764835,
ECO:0000269|PubMed:18557927, ECO:0000269|PubMed:20309870}.
-!- PTM: Proteolytically processed. The cleavage of the 65 kDa form
leads to the generation of a linker peptide, and 8 kDa and 50 kDa
products. The active form, the 8/50 kDa heterodimer, is resistant
to degradation. Complete removal of the linker peptide appears to
be a prerequisite to the complete activation of the enzyme.
{ECO:0000269|PubMed:10395325, ECO:0000269|PubMed:11973358,
ECO:0000269|PubMed:12441129, ECO:0000269|PubMed:15126626,
ECO:0000269|PubMed:15659389, ECO:0000269|PubMed:15848168}.
-!- PTM: N-glycosylated. Glycosylation of the 50 kDa subunit appears
to be essential for its solubility. {ECO:0000269|PubMed:10395325,
ECO:0000269|PubMed:12713442, ECO:0000269|PubMed:14573609,
ECO:0000269|PubMed:16263699, ECO:0000269|PubMed:19159218}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 79 family.
{ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF152376; AAD45669.1; -; mRNA.
EMBL; AF155510; AAD54941.1; -; mRNA.
EMBL; AF144325; AAD41342.1; -; mRNA.
EMBL; AF165154; AAD45379.1; -; mRNA.
EMBL; AF084467; AAD54516.1; -; mRNA.
EMBL; AM419200; CAL91960.1; -; mRNA.
EMBL; AY948074; AAX47106.1; -; mRNA.
EMBL; GQ337901; ACT98237.1; -; mRNA.
EMBL; GQ337902; ACT98238.1; -; mRNA.
EMBL; AK222986; BAD96706.1; -; mRNA.
EMBL; AC114781; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC051321; AAH51321.1; -; mRNA.
CCDS; CCDS3602.1; -. [Q9Y251-1]
CCDS; CCDS54774.1; -. [Q9Y251-3]
CCDS; CCDS56337.1; -. [Q9Y251-2]
RefSeq; NP_001092010.1; NM_001098540.2. [Q9Y251-1]
RefSeq; NP_001159970.1; NM_001166498.2. [Q9Y251-3]
RefSeq; NP_001186759.1; NM_001199830.1. [Q9Y251-2]
RefSeq; NP_006656.2; NM_006665.5. [Q9Y251-1]
UniGene; Hs.44227; -.
PDB; 5E8M; X-ray; 1.75 A; A=158-543, B=36-109.
PDB; 5E97; X-ray; 1.63 A; A=158-543, B=36-109.
PDB; 5E98; X-ray; 1.63 A; A=158-543, B=36-109.
PDB; 5E9B; X-ray; 1.88 A; A=158-543, B=36-109.
PDB; 5E9C; X-ray; 1.73 A; A=158-543, B=36-109.
PDB; 5L9Y; X-ray; 1.88 A; A=158-543, B=36-109.
PDB; 5L9Z; X-ray; 1.57 A; A=158-543, B=36-109.
PDB; 5LA4; X-ray; 1.90 A; A=36-543.
PDB; 5LA7; X-ray; 1.94 A; A=36-543.
PDBsum; 5E8M; -.
PDBsum; 5E97; -.
PDBsum; 5E98; -.
PDBsum; 5E9B; -.
PDBsum; 5E9C; -.
PDBsum; 5L9Y; -.
PDBsum; 5L9Z; -.
PDBsum; 5LA4; -.
PDBsum; 5LA7; -.
ProteinModelPortal; Q9Y251; -.
SMR; Q9Y251; -.
BioGrid; 116066; 14.
IntAct; Q9Y251; 7.
STRING; 9606.ENSP00000308107; -.
BindingDB; Q9Y251; -.
ChEMBL; CHEMBL3921; -.
DrugBank; DB06779; Dalteparin.
DrugBank; DB01109; Heparin.
CAZy; GH79; Glycoside Hydrolase Family 79.
iPTMnet; Q9Y251; -.
PhosphoSitePlus; Q9Y251; -.
BioMuta; HPSE; -.
DMDM; 296434532; -.
EPD; Q9Y251; -.
PaxDb; Q9Y251; -.
PeptideAtlas; Q9Y251; -.
PRIDE; Q9Y251; -.
TopDownProteomics; Q9Y251-1; -. [Q9Y251-1]
DNASU; 10855; -.
Ensembl; ENST00000311412; ENSP00000308107; ENSG00000173083. [Q9Y251-1]
Ensembl; ENST00000405413; ENSP00000384262; ENSG00000173083. [Q9Y251-1]
Ensembl; ENST00000509906; ENSP00000421038; ENSG00000173083. [Q9Y251-4]
Ensembl; ENST00000512196; ENSP00000423265; ENSG00000173083. [Q9Y251-3]
Ensembl; ENST00000513463; ENSP00000421365; ENSG00000173083. [Q9Y251-2]
GeneID; 10855; -.
KEGG; hsa:10855; -.
UCSC; uc003hoi.4; human. [Q9Y251-1]
CTD; 10855; -.
DisGeNET; 10855; -.
EuPathDB; HostDB:ENSG00000173083.14; -.
GeneCards; HPSE; -.
HGNC; HGNC:5164; HPSE.
HPA; HPA055344; -.
MIM; 604724; gene.
neXtProt; NX_Q9Y251; -.
OpenTargets; ENSG00000173083; -.
PharmGKB; PA29435; -.
eggNOG; ENOG410IHNV; Eukaryota.
eggNOG; ENOG410YDJW; LUCA.
GeneTree; ENSGT00390000004874; -.
HOGENOM; HOG000007256; -.
HOVERGEN; HBG081606; -.
InParanoid; Q9Y251; -.
KO; K07964; -.
OMA; SVTWHHY; -.
OrthoDB; EOG091G05QD; -.
PhylomeDB; Q9Y251; -.
TreeFam; TF328999; -.
BioCyc; MetaCyc:ENSG00000173083-MONOMER; -.
BRENDA; 3.2.1.166; 2681.
Reactome; R-HSA-2024096; HS-GAG degradation.
Reactome; R-HSA-6798695; Neutrophil degranulation.
GeneWiki; Heparanase; -.
GenomeRNAi; 10855; -.
PRO; PR:Q9Y251; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000173083; -.
CleanEx; HS_HPSE; -.
ExpressionAtlas; Q9Y251; baseline and differential.
Genevisible; Q9Y251; HS.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0043202; C:lysosomal lumen; TAS:Reactome.
GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
GO; GO:0005764; C:lysosome; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005578; C:proteinaceous extracellular matrix; IBA:GO_Central.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:0004566; F:beta-glucuronidase activity; TAS:ProtInc.
GO; GO:0030305; F:heparanase activity; IDA:UniProtKB.
GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB.
GO; GO:0045545; F:syndecan binding; IDA:UniProtKB.
GO; GO:0060055; P:angiogenesis involved in wound healing; IBA:GO_Central.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0006027; P:glycosaminoglycan catabolic process; TAS:Reactome.
GO; GO:0030200; P:heparan sulfate proteoglycan catabolic process; IDA:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0030194; P:positive regulation of blood coagulation; IDA:UniProtKB.
GO; GO:0051798; P:positive regulation of hair follicle development; IEA:Ensembl.
GO; GO:0033690; P:positive regulation of osteoblast proliferation; IDA:UniProtKB.
GO; GO:0051897; P:positive regulation of protein kinase B signaling; IDA:UniProtKB.
GO; GO:0010575; P:positive regulation of vascular endothelial growth factor production; IDA:UniProtKB.
GO; GO:0006029; P:proteoglycan metabolic process; TAS:ProtInc.
GO; GO:0051797; P:regulation of hair follicle development; IDA:UniProtKB.
GO; GO:0061042; P:vascular wound healing; IEA:Ensembl.
InterPro; IPR005199; Glyco_hydro_79.
InterPro; IPR017853; Glycoside_hydrolase_SF.
PANTHER; PTHR14363; PTHR14363; 1.
Pfam; PF03662; Glyco_hydro_79n; 1.
SUPFAM; SSF51445; SSF51445; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell adhesion;
Complete proteome; Direct protein sequencing; Glycoprotein; Hydrolase;
Lysosome; Magnesium; Membrane; Nucleus; Polymorphism;
Reference proteome; Secreted; Signal.
SIGNAL 1 35 {ECO:0000269|PubMed:12713442}.
CHAIN 36 109 Heparanase 8 kDa subunit.
/FTId=PRO_0000042260.
PROPEP 110 157 Linker peptide.
{ECO:0000269|PubMed:10395326,
ECO:0000269|PubMed:10446189,
ECO:0000269|PubMed:12713442}.
/FTId=PRO_0000042261.
CHAIN 158 543 Heparanase 50 kDa subunit.
/FTId=PRO_0000042262.
REGION 158 162 Heparin/HS-binding.
REGION 270 280 Heparin/HS-binding.
REGION 527 543 Required for transferring proheparanase
to the Golgi apparatus, secretion and
subsequent enzyme activity and for
enhancement of PKB/AKT1 phosphorylation.
ACT_SITE 225 225 Proton donor. {ECO:0000255}.
ACT_SITE 343 343 Nucleophile. {ECO:0000255}.
CARBOHYD 162 162 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609}.
CARBOHYD 178 178 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609}.
CARBOHYD 200 200 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609}.
CARBOHYD 217 217 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609,
ECO:0000269|PubMed:16263699,
ECO:0000269|PubMed:19159218}.
CARBOHYD 238 238 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609,
ECO:0000269|PubMed:19159218}.
CARBOHYD 459 459 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:14573609}.
VAR_SEQ 167 225 RSSVDVLYTFANCSGLDLIFGLNALLRTADLQWNSSNAQLL
LDYCSSKGYNISWELGNE -> K (in isoform 2).
{ECO:0000303|PubMed:17208203}.
/FTId=VSP_044537.
VAR_SEQ 329 402 Missing (in isoform 3).
{ECO:0000303|Ref.10}.
/FTId=VSP_044664.
VAR_SEQ 365 380 WLDKLGLSARMGIEVV -> IIGYLFCSRNWWAPRC (in
isoform 4). {ECO:0000303|Ref.10}.
/FTId=VSP_053730.
VAR_SEQ 381 543 Missing (in isoform 4).
{ECO:0000303|Ref.10}.
/FTId=VSP_053731.
VARIANT 260 260 N -> S (in some hepatocellular
carcinoma).
{ECO:0000269|PubMed:15334672}.
/FTId=VAR_023600.
VARIANT 307 307 K -> R (in dbSNP:rs11099592).
{ECO:0000269|PubMed:10395325,
ECO:0000269|PubMed:10395326,
ECO:0000269|PubMed:10405343,
ECO:0000269|PubMed:10446189,
ECO:0000269|PubMed:10764835,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17208203,
ECO:0000269|Ref.10, ECO:0000269|Ref.11,
ECO:0000269|Ref.9}.
/FTId=VAR_068907.
MUTAGEN 156 156 Y->A,E: Alteration of the correct
processing of heparanase which results in
the cleavage at an upstream site in the
linker peptide and no activation of
proheparanase.
{ECO:0000269|PubMed:15659389}.
MUTAGEN 156 156 Y->V: Normal processing.
{ECO:0000269|PubMed:15659389}.
MUTAGEN 158 158 K->A: No association with GS-modified
heparin; when associated with K-158.
{ECO:0000269|PubMed:15760902}.
MUTAGEN 161 161 K->A: Two-fold increase in the level of
secretion upon addition of GS-modified
heparin. No association with GS-modified
heparin; when associated with K-161.
{ECO:0000269|PubMed:15760902}.
MUTAGEN 162 162 N->Q: Faster electrophoretic migration
typical of a size reduction and important
decrease of secretion. Larger size
reduction; when associated with Q-178; Q-
200; Q-217; Q-238 and Q-459.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 178 178 N->Q: Faster electrophoretic migration
typical of a size reduction and important
decrease of secretion. Larger size
reduction; when associated with Q-162; Q-
200; Q-217; Q-238 and Q-459.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 200 200 N->Q: Faster electrophoretic migration
typical of a size reduction and partial
decrease in secretion. Larger size
reduction; when associated with Q-162; Q-
178; Q-217; Q-238 and Q-459.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 217 217 N->Q: Faster electrophoretic migration
typical of a size reduction and partial
decrease in secretion. Larger size
reduction; when associated with Q-162; Q-
178; Q-200; Q-238 and Q-459.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 225 225 E->A: Loss of heparanase activity. No
effect on HPSE-mediated cell adhesion.
{ECO:0000269|PubMed:11123890,
ECO:0000269|PubMed:12773484}.
MUTAGEN 238 238 N->Q: Faster electrophoretic migration
typical of a size reduction. Larger size
reduction and important decrease of
secretion; when associated with Q-162; Q-
178; Q-200; Q-217 and Q-459.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 343 343 E->A: Loss of heparanase activity.
{ECO:0000269|PubMed:11123890}.
MUTAGEN 367 367 D->A: Strong decrease in heparanase
activity. {ECO:0000269|PubMed:11123890}.
MUTAGEN 378 378 E->A: No reduction in heparanase
activity.
MUTAGEN 396 396 E->A: No reduction in heparanase
activity.
MUTAGEN 414 414 V->K: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 417 417 K->E: No effect on processing nor
secretion. No enzyme activity detected.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 459 459 N->Q: Faster electrophoretic migration
typical of a size reduction. Larger size
reduction and important decrease of
secretion; when associated with Q-162; Q-
178; Q-200; Q-217 and Q-238.
{ECO:0000269|PubMed:14573609}.
MUTAGEN 525 525 P->G: No effect on processing nor
secretion. No enzyme activity detected.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 527 527 F->R: No effect on processing nor
secretion. No enzyme activity detected.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 528 528 S->K: No effect on processing nor
secretion. No enzyme activity detected.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 529 529 Y->A: No effect on processing nor
secretion. No enzyme activity detected.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 531 531 F->R: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 533 533 V->R: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 534 534 I->D: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 535 535 R->A: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 536 536 N->A: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 537 537 A->K: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 538 538 K->A: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 539 539 V->A: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 540 540 A->K: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 541 541 A->K: No effect on processing, secretion
nor enzyme activity.
{ECO:0000269|PubMed:19244131}.
MUTAGEN 542 542 C->A: Abolishes processing, secretion and
enzyme activity.
{ECO:0000269|PubMed:19244131}.
CONFLICT 13 13 L -> LL (in Ref. 5; AAD54516).
{ECO:0000305}.
CONFLICT 36 36 Q -> QQ (in Ref. 5; AAD54516).
{ECO:0000305}.
CONFLICT 291 291 D -> G (in Ref. 11; BAD96706).
{ECO:0000305}.
STRAND 38 44 {ECO:0000244|PDB:5E97}.
STRAND 49 51 {ECO:0000244|PDB:5E97}.
STRAND 57 62 {ECO:0000244|PDB:5E97}.
HELIX 63 67 {ECO:0000244|PDB:5E97}.
HELIX 71 76 {ECO:0000244|PDB:5E97}.
HELIX 78 86 {ECO:0000244|PDB:5E97}.
STRAND 89 96 {ECO:0000244|PDB:5E97}.
HELIX 97 101 {ECO:0000244|PDB:5E97}.
STRAND 102 104 {ECO:0000244|PDB:5E97}.
STRAND 163 165 {ECO:0000244|PDB:5E97}.
HELIX 167 180 {ECO:0000244|PDB:5E97}.
STRAND 182 188 {ECO:0000244|PDB:5E97}.
HELIX 202 213 {ECO:0000244|PDB:5E97}.
STRAND 219 222 {ECO:0000244|PDB:5E97}.
HELIX 226 228 {ECO:0000244|PDB:5E97}.
HELIX 229 233 {ECO:0000244|PDB:5E97}.
HELIX 239 254 {ECO:0000244|PDB:5E97}.
STRAND 256 258 {ECO:0000244|PDB:5E97}.
STRAND 263 268 {ECO:0000244|PDB:5E97}.
HELIX 273 286 {ECO:0000244|PDB:5E97}.
HELIX 287 289 {ECO:0000244|PDB:5E97}.
STRAND 291 301 {ECO:0000244|PDB:5E97}.
TURN 302 304 {ECO:0000244|PDB:5E97}.
HELIX 307 310 {ECO:0000244|PDB:5E97}.
HELIX 313 316 {ECO:0000244|PDB:5E97}.
HELIX 318 331 {ECO:0000244|PDB:5E97}.
STRAND 338 348 {ECO:0000244|PDB:5E97}.
TURN 353 357 {ECO:0000244|PDB:5E97}.
HELIX 359 361 {ECO:0000244|PDB:5E97}.
HELIX 362 375 {ECO:0000244|PDB:5E97}.
STRAND 379 383 {ECO:0000244|PDB:5E97}.
STRAND 385 390 {ECO:0000244|PDB:5E97}.
HELIX 402 413 {ECO:0000244|PDB:5E97}.
STRAND 414 418 {ECO:0000244|PDB:5E97}.
STRAND 420 423 {ECO:0000244|PDB:5E97}.
STRAND 429 438 {ECO:0000244|PDB:5E97}.
STRAND 450 456 {ECO:0000244|PDB:5E97}.
STRAND 458 460 {ECO:0000244|PDB:5E97}.
STRAND 462 465 {ECO:0000244|PDB:5E97}.
STRAND 475 482 {ECO:0000244|PDB:5E97}.
STRAND 484 486 {ECO:0000244|PDB:5E97}.
HELIX 487 489 {ECO:0000244|PDB:5E97}.
STRAND 493 495 {ECO:0000244|PDB:5E97}.
STRAND 522 524 {ECO:0000244|PDB:5E97}.
STRAND 528 534 {ECO:0000244|PDB:5E97}.
HELIX 540 542 {ECO:0000244|PDB:5E97}.
SEQUENCE 543 AA; 61149 MW; A990F5AFD639CA1A CRC64;
MLLRSKPALP PPLMLLLLGP LGPLSPGALP RPAQAQDVVD LDFFTQEPLH LVSPSFLSVT
IDANLATDPR FLILLGSPKL RTLARGLSPA YLRFGGTKTD FLIFDPKKES TFEERSYWQS
QVNQDICKYG SIPPDVEEKL RLEWPYQEQL LLREHYQKKF KNSTYSRSSV DVLYTFANCS
GLDLIFGLNA LLRTADLQWN SSNAQLLLDY CSSKGYNISW ELGNEPNSFL KKADIFINGS
QLGEDFIQLH KLLRKSTFKN AKLYGPDVGQ PRRKTAKMLK SFLKAGGEVI DSVTWHHYYL
NGRTATKEDF LNPDVLDIFI SSVQKVFQVV ESTRPGKKVW LGETSSAYGG GAPLLSDTFA
AGFMWLDKLG LSARMGIEVV MRQVFFGAGN YHLVDENFDP LPDYWLSLLF KKLVGTKVLM
ASVQGSKRRK LRVYLHCTNT DNPRYKEGDL TLYAINLHNV TKYLRLPYPF SNKQVDKYLL
RPLGPHGLLS KSVQLNGLTL KMVDDQTLPP LMEKPLRPGS SLGLPAFSYS FFVIRNAKVA
ACI


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