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Hyaluronan-binding protein 2 (EC 3.4.21.-) (Factor VII-activating protease) (Factor seven-activating protease) (FSAP) (Hepatocyte growth factor activator-like protein) (Plasma hyaluronan-binding protein) [Cleaved into: Hyaluronan-binding protein 2 50 kDa heavy chain; Hyaluronan-binding protein 2 50 kDa heavy chain alternate form; Hyaluronan-binding protein 2 27 kDa light chain; Hyaluronan-binding protein 2 27 kDa light chain alternate form]

 HABP2_HUMAN             Reviewed;         560 AA.
Q14520; A8K467; B7Z8U5; F5H5M6; O00663;
30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
28-MAR-2018, entry version 163.
RecName: Full=Hyaluronan-binding protein 2;
EC=3.4.21.-;
AltName: Full=Factor VII-activating protease;
AltName: Full=Factor seven-activating protease;
Short=FSAP;
AltName: Full=Hepatocyte growth factor activator-like protein;
AltName: Full=Plasma hyaluronan-binding protein;
Contains:
RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain;
Contains:
RecName: Full=Hyaluronan-binding protein 2 50 kDa heavy chain alternate form;
Contains:
RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain;
Contains:
RecName: Full=Hyaluronan-binding protein 2 27 kDa light chain alternate form;
Flags: Precursor;
Name=HABP2; Synonyms=HGFAL, PHBP;
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 24-42;
140-169; 174-183; 206-235; 255-260; 314-334; 417-429; 433-459; 500-517
AND 546-551, FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Plasma;
PubMed=8827452; DOI=10.1093/oxfordjournals.jbchem.a021362;
Choi-Miura N.-H., Tobe T., Sumiya J., Nakano Y., Sano Y., Mazda T.,
Tomita M.;
"Purification and characterization of a novel hyaluronan-binding
protein (PHBP) from human plasma: it has three EGF, a kringle and a
serine protease domain, similar to hepatocyte growth factor
activator.";
J. Biochem. 119:1157-1165(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Kitamura N.;
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS ILE-90 AND GLN-393, AND
VARIANT NMTC5 GLU-534.
SeattleSNPs variation discovery resource;
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Liver, and Trachea;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J.,
Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D.,
Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L.,
Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S.,
Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L.,
Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J.,
Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M.,
Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S.,
Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M.,
Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A.,
Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T.,
Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I.,
Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T.,
Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W.,
Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H.,
Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L.,
Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K.,
Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T.,
Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
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).
[8]
FUNCTION.
PubMed=10754382;
Roemisch J., Vermoehlen S., Feussner A., Stoehr H.-A.;
"The FVII activating protease cleaves single-chain plasminogen
activators.";
Haemostasis 29:292-299(1999).
[9]
FUNCTION.
PubMed=11217080; DOI=10.1248/bpb.24.140;
Choi-Miura N.H., Yoda M., Saito K., Takahashi K., Tomita M.;
"Identification of the substrates for plasma hyaluronan binding
protein.";
Biol. Pharm. Bull. 24:140-143(2001).
[10]
VARIANT GLN-393, AND VARIANT NMTC5 GLU-534.
PubMed=12578864; DOI=10.1161/01.CIR.0000055189.18831.B1;
Willeit J., Kiechl S., Weimer T., Mair A., Santer P., Wiedermann C.J.,
Roemisch J.;
"Marburg I polymorphism of factor VII-activating protease: a prominent
risk predictor of carotid stenosis.";
Circulation 107:667-670(2003).
[11]
FUNCTION, INVOLVEMENT IN NMTC5, VARIANT NMTC5 GLU-534, AND
CHARACTERIZATION OF VARIANT NMTC5 GLU-534.
PubMed=26222560; DOI=10.1056/NEJMoa1502449;
Gara S.K., Jia L., Merino M.J., Agarwal S.K., Zhang L., Cam M.,
Patel D., Kebebew E.;
"Germline HABP2 mutation causing familial nonmedullary thyroid
cancer.";
N. Engl. J. Med. 373:448-455(2015).
-!- FUNCTION: Cleaves the alpha-chain at multiple sites and the beta-
chain between 'Lys-53' and 'Lys-54' but not the gamma-chain of
fibrinogen and therefore does not initiate the formation of the
fibrin clot and does not cause the fibrinolysis directly. It does
not cleave (activate) prothrombin and plasminogen but converts the
inactive single chain urinary plasminogen activator (pro-
urokinase) to the active two chain form. Activates coagulation
factor VII (PubMed:8827452, PubMed:10754382, PubMed:11217080). May
function as a tumor suppressor negatively regulating cell
proliferation and cell migration (PubMed:26222560).
{ECO:0000269|PubMed:10754382, ECO:0000269|PubMed:11217080,
ECO:0000269|PubMed:26222560, ECO:0000269|PubMed:8827452}.
-!- SUBUNIT: Heterodimer; disulfide-linked. Heterodimer of a 50 kDa
heavy and a 27 kDa light chain linked by a disulfide bond (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:8827452}.
Note=Secreted as an inactive single-chain precursor and is then
activated to a heterodimeric form.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q14520-1; Sequence=Displayed;
Name=2;
IsoId=Q14520-2; Sequence=VSP_044583;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Ubiquitously expressed.
{ECO:0000269|PubMed:8827452}.
-!- PTM: Proteolytic cleavage at Gly-23 or Met-27 can give rise to the
50 kDa heavy chain and cleavage at Arg-313 or Lys-319 can give
rise to the 27 kDa light chain. The heavy chain can undergo
further proteolytic cleavage at Lys-169 or Arg-170 to give rise to
2 inactive 26 kDa fragments and the light chain can undergo
further proteolytic cleavage at Arg-480 to give rise to inactive
17 kDa and 8 kDa fragments (By similarity). {ECO:0000250}.
-!- DISEASE: Thyroid cancer, non-medullary, 5 (NMTC5) [MIM:616535]: A
form of non-medullary thyroid cancer (NMTC), a cancer
characterized by tumors originating from the thyroid follicular
cells. NMTCs represent approximately 95% of all cases of thyroid
cancer and are classified into papillary, follicular, Hurthle
cell, and anaplastic neoplasms. {ECO:0000269|PubMed:12578864,
ECO:0000269|PubMed:26222560}. Note=Disease susceptibility is
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the peptidase S1 family.
{ECO:0000255|PROSITE-ProRule:PRU00274}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/habp2/";
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EMBL; S83182; AAB46909.1; -; mRNA.
EMBL; D49742; BAA08576.1; -; mRNA.
EMBL; AY534754; AAS16352.1; -; Genomic_DNA.
EMBL; AK290832; BAF83521.1; -; mRNA.
EMBL; AK303948; BAH14081.1; -; mRNA.
EMBL; AL390197; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471066; EAW49505.1; -; Genomic_DNA.
EMBL; BC031412; AAH31412.1; -; mRNA.
CCDS; CCDS53579.1; -. [Q14520-2]
CCDS; CCDS7577.1; -. [Q14520-1]
PIR; JC4795; JC4795.
RefSeq; NP_001171131.1; NM_001177660.2. [Q14520-2]
RefSeq; NP_004123.1; NM_004132.4. [Q14520-1]
UniGene; Hs.422542; -.
ProteinModelPortal; Q14520; -.
SMR; Q14520; -.
IntAct; Q14520; 1.
MINT; Q14520; -.
STRING; 9606.ENSP00000277903; -.
DrugBank; DB08818; Hyaluronic acid.
MEROPS; S01.033; -.
iPTMnet; Q14520; -.
PhosphoSitePlus; Q14520; -.
BioMuta; HABP2; -.
DMDM; 73919921; -.
EPD; Q14520; -.
MaxQB; Q14520; -.
PaxDb; Q14520; -.
PeptideAtlas; Q14520; -.
PRIDE; Q14520; -.
DNASU; 3026; -.
Ensembl; ENST00000351270; ENSP00000277903; ENSG00000148702. [Q14520-1]
Ensembl; ENST00000542051; ENSP00000443283; ENSG00000148702. [Q14520-2]
GeneID; 3026; -.
KEGG; hsa:3026; -.
UCSC; uc001lai.5; human. [Q14520-1]
CTD; 3026; -.
DisGeNET; 3026; -.
EuPathDB; HostDB:ENSG00000148702.14; -.
GeneCards; HABP2; -.
HGNC; HGNC:4798; HABP2.
HPA; HPA019518; -.
MalaCards; HABP2; -.
MIM; 603924; gene.
MIM; 616535; phenotype.
neXtProt; NX_Q14520; -.
OpenTargets; ENSG00000148702; -.
PharmGKB; PA29172; -.
eggNOG; KOG1217; Eukaryota.
eggNOG; KOG3627; Eukaryota.
eggNOG; COG5640; LUCA.
GeneTree; ENSGT00760000119133; -.
HOGENOM; HOG000237314; -.
HOVERGEN; HBG106385; -.
InParanoid; Q14520; -.
KO; K08648; -.
OMA; RDEIPHN; -.
OrthoDB; EOG091G0AH5; -.
PhylomeDB; Q14520; -.
TreeFam; TF329901; -.
BRENDA; 3.4.21.B1; 2681.
SABIO-RK; Q14520; -.
ChiTaRS; HABP2; human.
GeneWiki; HABP2; -.
GenomeRNAi; 3026; -.
PRO; PR:Q14520; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000148702; -.
CleanEx; HS_HABP2; -.
Genevisible; Q14520; HS.
GO; GO:0005576; C:extracellular region; NAS:UniProtKB.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005539; F:glycosaminoglycan binding; TAS:ProtInc.
GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
CDD; cd00190; Tryp_SPc; 1.
Gene3D; 2.40.20.10; -; 1.
InterPro; IPR001881; EGF-like_Ca-bd_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR000001; Kringle.
InterPro; IPR013806; Kringle-like.
InterPro; IPR018056; Kringle_CS.
InterPro; IPR038178; Kringle_sf.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR001314; Peptidase_S1A.
InterPro; IPR001254; Trypsin_dom.
InterPro; IPR018114; TRYPSIN_HIS.
InterPro; IPR033116; TRYPSIN_SER.
Pfam; PF00008; EGF; 2.
Pfam; PF00051; Kringle; 1.
Pfam; PF00089; Trypsin; 1.
PRINTS; PR00722; CHYMOTRYPSIN.
SMART; SM00181; EGF; 3.
SMART; SM00179; EGF_CA; 2.
SMART; SM00130; KR; 1.
SMART; SM00020; Tryp_SPc; 1.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF57440; SSF57440; 1.
PROSITE; PS00022; EGF_1; 3.
PROSITE; PS01186; EGF_2; 2.
PROSITE; PS50026; EGF_3; 3.
PROSITE; PS00021; KRINGLE_1; 1.
PROSITE; PS50070; KRINGLE_2; 1.
PROSITE; PS50240; TRYPSIN_DOM; 1.
PROSITE; PS00134; TRYPSIN_HIS; 1.
PROSITE; PS00135; TRYPSIN_SER; 1.
1: Evidence at protein level;
Alternative splicing; Cleavage on pair of basic residues;
Complete proteome; Direct protein sequencing; Disulfide bond;
EGF-like domain; Glycoprotein; Hydrolase; Kringle; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Serine protease;
Signal.
SIGNAL 1 23 {ECO:0000269|PubMed:8827452}.
CHAIN 24 313 Hyaluronan-binding protein 2 50 kDa heavy
chain.
/FTId=PRO_0000027899.
CHAIN 27 313 Hyaluronan-binding protein 2 50 kDa heavy
chain alternate form. {ECO:0000250}.
/FTId=PRO_0000027900.
CHAIN 314 560 Hyaluronan-binding protein 2 27 kDa light
chain.
/FTId=PRO_0000027901.
CHAIN 320 560 Hyaluronan-binding protein 2 27 kDa light
chain alternate form. {ECO:0000250}.
/FTId=PRO_0000027902.
DOMAIN 73 109 EGF-like 1. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 111 148 EGF-like 2. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 150 188 EGF-like 3. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
DOMAIN 193 276 Kringle. {ECO:0000255|PROSITE-
ProRule:PRU00121}.
DOMAIN 314 555 Peptidase S1. {ECO:0000255|PROSITE-
ProRule:PRU00274}.
ACT_SITE 362 362 Charge relay system. {ECO:0000250}.
ACT_SITE 411 411 Charge relay system. {ECO:0000250}.
ACT_SITE 509 509 Charge relay system. {ECO:0000250}.
SITE 169 170 Cleavage. {ECO:0000250}.
SITE 170 171 Cleavage. {ECO:0000250}.
SITE 480 481 Cleavage. {ECO:0000250}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 207 207 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 77 88 {ECO:0000250}.
DISULFID 82 97 {ECO:0000250}.
DISULFID 99 108 {ECO:0000250}.
DISULFID 115 125 {ECO:0000250}.
DISULFID 120 136 {ECO:0000250}.
DISULFID 138 147 {ECO:0000250}.
DISULFID 154 165 {ECO:0000250}.
DISULFID 159 176 {ECO:0000250}.
DISULFID 178 187 {ECO:0000250}.
DISULFID 194 276 {ECO:0000250}.
DISULFID 215 257 {ECO:0000250}.
DISULFID 246 271 {ECO:0000250}.
DISULFID 301 435 Interchain (between heavy and light
chains). {ECO:0000255|PROSITE-
ProRule:PRU00076, ECO:0000255|PROSITE-
ProRule:PRU00121, ECO:0000255|PROSITE-
ProRule:PRU00274}.
DISULFID 347 363 {ECO:0000250}.
DISULFID 447 515 {ECO:0000250}.
DISULFID 477 493 {ECO:0000250}.
DISULFID 505 533 {ECO:0000250}.
VAR_SEQ 1 26 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044583.
VARIANT 90 90 V -> I (in dbSNP:rs11575750).
{ECO:0000269|Ref.3}.
/FTId=VAR_023399.
VARIANT 393 393 E -> Q (polymorphism; Marburg II;
dbSNP:rs11575688).
{ECO:0000269|PubMed:12578864,
ECO:0000269|Ref.3}.
/FTId=VAR_023400.
VARIANT 534 534 G -> E (in NMTC5; associated with disease
susceptibility; Marburg I polymorphism;
could be a prominent risk predictor of
carotid stenosis; impairs the pro-
urokinase activating potency; increased
cell migration and increased cell
proliferation; dominant negative effect;
dbSNP:rs7080536).
{ECO:0000269|PubMed:12578864,
ECO:0000269|PubMed:26222560,
ECO:0000269|Ref.3}.
/FTId=VAR_023401.
CONFLICT 157 157 N -> S (in Ref. 4; BAH14081).
{ECO:0000305}.
SEQUENCE 560 AA; 62672 MW; 5C1907230784ACD4 CRC64;
MFARMSDLHV LLLMALVGKT ACGFSLMSLL ESLDPDWTPD QYDYSYEDYN QEENTSSTLT
HAENPDWYYT EDQADPCQPN PCEHGGDCLV HGSTFTCSCL APFSGNKCQK VQNTCKDNPC
GRGQCLITQS PPYYRCVCKH PYTGPSCSQV VPVCRPNPCQ NGATCSRHKR RSKFTCACPD
QFKGKFCEIG SDDCYVGDGY SYRGKMNRTV NQHACLYWNS HLLLQENYNM FMEDAETHGI
GEHNFCRNPD ADEKPWCFIK VTNDKVKWEY CDVSACSAQD VAYPEESPTE PSTKLPGFDS
CGKTEIAERK IKRIYGGFKS TAGKHPWQAS LQSSLPLTIS MPQGHFCGGA LIHPCWVLTA
AHCTDIKTRH LKVVLGDQDL KKEEFHEQSF RVEKIFKYSH YNERDEIPHN DIALLKLKPV
DGHCALESKY VKTVCLPDGS FPSGSECHIS GWGVTETGKG SRQLLDAKVK LIANTLCNSR
QLYDHMIDDS MICAGNLQKP GQDTCQGDSG GPLTCEKDGT YYVYGIVSWG LECGKRPGVY
TQVTKFLNWI KATIKSESGF


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E02H0035 Rat Hyaluronan Binding Protein 1 ELISA , HABP1 96 Tests/kit
E11H0035 Bovine Hyaluronan Binding Protein 1 ELISA 96T/kit
E07H0035 Porcine Hyaluronan Binding Protein 1 ELISA 96T/kit
E10167h Human Hyaluronan Binding Protein 4 ELISA Kit 96T
E03H0035 Mouse Hyaluronan Binding Protein 1 ELISA 96T/kit
E12H0035 Chicken Hyaluronan Binding Protein 1 ELISA 96T/kit


 

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