Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Transmembrane prolyl 4-hydroxylase (P4H-TM) (EC 1.14.11.-) (Hypoxia-inducible factor prolyl hydroxylase 4) (HIF-PH4) (HIF-prolyl hydroxylase 4) (HPH-4)

 P4HTM_HUMAN             Reviewed;         502 AA.
Q9NXG6; Q6PAG6; Q8TCJ9; Q8WV55; Q96F22; Q9BW77;
16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
16-JUN-2003, sequence version 2.
27-SEP-2017, entry version 155.
RecName: Full=Transmembrane prolyl 4-hydroxylase;
Short=P4H-TM;
EC=1.14.11.-;
AltName: Full=Hypoxia-inducible factor prolyl hydroxylase 4;
Short=HIF-PH4;
Short=HIF-prolyl hydroxylase 4;
Short=HPH-4;
Name=P4HTM; Synonyms=PH4;
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), SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=12163023; DOI=10.1016/S0006-291X(02)00862-8;
Oehme F., Ellinghaus P., Kolkhof P., Smith T.J., Ramakrishnan S.,
Huetter J., Schramm M., Flamme I.;
"Overexpression of PH-4, a novel putative proline 4-hydroxylase,
modulates activity of hypoxia-inducible transcription factors.";
Biochem. Biophys. Res. Commun. 296:343-349(2002).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 166-502 (ISOFORM 1).
TISSUE=Duodenum, Hippocampus, and Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 84-502 (ISOFORM 2).
TISSUE=Colon mucosa;
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]
FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
INDUCTION, TOPOLOGY, AND GLYCOSYLATION.
PubMed=17726031; DOI=10.1074/jbc.M704988200;
Koivunen P., Tiainen P., Hyvaerinen J., Williams K.E., Sormunen R.,
Klaus S.J., Kivirikko K.I., Myllyharju J.;
"An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is
induced by hypoxia and acts on hypoxia-inducible factor alpha.";
J. Biol. Chem. 282:30544-30552(2007).
-!- FUNCTION: Catalyzes the post-translational formation of 4-
hydroxyproline in hypoxia-inducible factor (HIF) alpha proteins.
Hydroxylates HIF1A at 'Pro-402' and 'Pro-564'. May function as a
cellular oxygen sensor and, under normoxic conditions, may target
HIF through the hydroxylation for proteasomal degradation via the
von Hippel-Lindau ubiquitination complex.
{ECO:0000269|PubMed:17726031}.
-!- CATALYTIC ACTIVITY: An HIF alpha chain L-proline + 2-oxoglutarate
+ O(2) = An HIF alpha chain trans-4-hydroxy-L-proline + succinate
+ CO(2).
-!- COFACTOR:
Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00805};
Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|PROSITE-
ProRule:PRU00805};
-!- COFACTOR:
Name=L-ascorbate; Xref=ChEBI:CHEBI:38290; Evidence={ECO:0000250};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17726031}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:12163023, ECO:0000269|PubMed:17726031};
Single-pass type II membrane protein {ECO:0000269|PubMed:12163023,
ECO:0000269|PubMed:17726031}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9NXG6-1; Sequence=Displayed;
Name=2; Synonyms=b;
IsoId=Q9NXG6-2; Sequence=VSP_007574;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q9NXG6-3; Sequence=VSP_007573;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Widely expressed with highest levels in adult
pancreas, heart, skeletal muscle, brain, placenta, kidney and
adrenal gland. Expressed at lower levels in epiphyseal cartilage
and in fibroblasts. {ECO:0000269|PubMed:12163023,
ECO:0000269|PubMed:17726031}.
-!- INDUCTION: By hypoxia in many cultured cell lines.
{ECO:0000269|PubMed:17726031}.
-!- PTM: Glycosylated. {ECO:0000269|PubMed:17726031}.
-!- SEQUENCE CAUTION:
Sequence=AAH60321.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
Sequence=BAA91045.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=CAD28518.2; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AY198406; AAO43431.1; -; mRNA.
EMBL; AL713728; CAD28518.2; ALT_SEQ; mRNA.
EMBL; BC000580; AAH00580.1; -; mRNA.
EMBL; BC011710; AAH11710.3; -; mRNA.
EMBL; BC047566; AAH47566.1; -; mRNA.
EMBL; BC060321; AAH60321.1; ALT_SEQ; mRNA.
EMBL; AK000269; BAA91045.1; ALT_INIT; mRNA.
CCDS; CCDS2781.2; -. [Q9NXG6-3]
CCDS; CCDS43089.1; -. [Q9NXG6-1]
RefSeq; NP_808807.2; NM_177938.2. [Q9NXG6-3]
RefSeq; NP_808808.1; NM_177939.2. [Q9NXG6-1]
UniGene; Hs.654944; -.
ProteinModelPortal; Q9NXG6; -.
SMR; Q9NXG6; -.
BioGrid; 120100; 6.
IntAct; Q9NXG6; 1.
STRING; 9606.ENSP00000341422; -.
BindingDB; Q9NXG6; -.
ChEMBL; CHEMBL3047; -.
DrugBank; DB00126; Vitamin C.
iPTMnet; Q9NXG6; -.
PhosphoSitePlus; Q9NXG6; -.
BioMuta; P4HTM; -.
DMDM; 32129516; -.
MaxQB; Q9NXG6; -.
PaxDb; Q9NXG6; -.
PeptideAtlas; Q9NXG6; -.
PRIDE; Q9NXG6; -.
Ensembl; ENST00000343546; ENSP00000341422; ENSG00000178467. [Q9NXG6-3]
Ensembl; ENST00000383729; ENSP00000373235; ENSG00000178467. [Q9NXG6-1]
GeneID; 54681; -.
KEGG; hsa:54681; -.
UCSC; uc003cvg.4; human. [Q9NXG6-1]
CTD; 54681; -.
DisGeNET; 54681; -.
EuPathDB; HostDB:ENSG00000178467.17; -.
GeneCards; P4HTM; -.
HGNC; HGNC:28858; P4HTM.
HPA; HPA007199; -.
MIM; 614584; gene.
neXtProt; NX_Q9NXG6; -.
OpenTargets; ENSG00000178467; -.
PharmGKB; PA164724295; -.
eggNOG; KOG1591; Eukaryota.
eggNOG; ENOG410XS5J; LUCA.
GeneTree; ENSGT00390000014570; -.
HOGENOM; HOG000115323; -.
InParanoid; Q9NXG6; -.
KO; K06711; -.
OMA; DSQPEWA; -.
OrthoDB; EOG091G04NW; -.
PhylomeDB; Q9NXG6; -.
TreeFam; TF332923; -.
ChiTaRS; P4HTM; human.
GenomeRNAi; 54681; -.
PRO; PR:Q9NXG6; -.
Proteomes; UP000005640; Chromosome 3.
Bgee; ENSG00000178467; -.
ExpressionAtlas; Q9NXG6; baseline and differential.
Genevisible; Q9NXG6; HS.
GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005506; F:iron ion binding; IEA:InterPro.
GO; GO:0031418; F:L-ascorbic acid binding; IEA:UniProtKB-KW.
GO; GO:0016706; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors; IDA:MGI.
GO; GO:0045646; P:regulation of erythrocyte differentiation; IEA:Ensembl.
CDD; cd00051; EFh; 1.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR005123; Oxoglu/Fe-dep_dioxygenase.
InterPro; IPR006620; Pro_4_hyd_alph.
Pfam; PF13640; 2OG-FeII_Oxy_3; 1.
Pfam; PF13499; EF-hand_7; 1.
SMART; SM00702; P4Hc; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 2.
PROSITE; PS51471; FE2OG_OXY; 1.
1: Evidence at protein level;
Alternative splicing; Calcium; Complete proteome; Dioxygenase;
Endoplasmic reticulum; Glycoprotein; Iron; Membrane; Metal-binding;
Oxidoreductase; Reference proteome; Repeat; Signal-anchor;
Transmembrane; Transmembrane helix; Vitamin C.
CHAIN 1 502 Transmembrane prolyl 4-hydroxylase.
/FTId=PRO_0000206668.
TOPO_DOM 1 60 Cytoplasmic. {ECO:0000255}.
TRANSMEM 61 81 Helical; Signal-anchor for type II
membrane protein. {ECO:0000255}.
TOPO_DOM 82 502 Lumenal. {ECO:0000255}.
DOMAIN 185 220 EF-hand 1.
DOMAIN 224 259 EF-hand 2.
DOMAIN 310 460 Fe2OG dioxygenase. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
CA_BIND 198 210 1. {ECO:0000255}.
CA_BIND 237 249 2. {ECO:0000255}.
METAL 328 328 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 330 330 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
METAL 374 374 Iron. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
BINDING 451 451 2-oxoglutarate. {ECO:0000255|PROSITE-
ProRule:PRU00805}.
CARBOHYD 348 348 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 368 368 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 382 382 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 358 358 R -> RQVSPNWGLPSILRPGTPMTQAQPCTVGVPLGMGPG
DHWVIPVSPWEHPQLGTCSVPPLPYS (in isoform
3). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_007573.
VAR_SEQ 359 502 YMTVLFYLNNVTGGGETVFPVADNRTYDEMSLIQDDVDLRD
TRRHCDKGNLRVKPQQGTAVFWYNYLPDGQGWVGDVDDYSL
HGGCLVTRGTKWIANNWINVDPSRARQALFQQEMARLAREG
GTDSQPEWALDRAYRDARVEL -> QVSPNWGLPSILRPGT
PMTQAQPCTVGVPLGMGPGDHWVIPVSDALTSPHKLFTQWL
ERGGYWSS (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_007574.
CONFLICT 213 213 Q -> K (in Ref. 3; AAH47566).
{ECO:0000305}.
CONFLICT 240 240 G -> A (in Ref. 1; AAO43431).
{ECO:0000305}.
SEQUENCE 502 AA; 56661 MW; A2DAE4ACF4A2E18C CRC64;
MAAAAVTGQR PETAAAEEAS RPQWAPPDHC QAQAAAGLGD GEDAPVRPLC KPRGICSRAY
FLVLMVFVHL YLGNVLALLL FVHYSNGDES SDPGPQHRAQ GPGPEPTLGP LTRLEGIKVG
HERKVQLVTD RDHFIRTLSL KPLLFEIPGF LTDEECRLII HLAQMKGLQR SQILPTEEYE
EAMSTMQVSQ LDLFRLLDQN RDGHLQLREV LAQTRLGNGW WMTPESIQEM YAAIKADPDG
DGVLSLQEFS NMDLRDFHKY MRSHKAESSE LVRNSHHTWL YQGEGAHHIM RAIRQRVLRL
TRLSPEIVEL SEPLQVVRYG EGGHYHAHVD SGPVYPETIC SHTKLVANES VPFETSCRYM
TVLFYLNNVT GGGETVFPVA DNRTYDEMSL IQDDVDLRDT RRHCDKGNLR VKPQQGTAVF
WYNYLPDGQG WVGDVDDYSL HGGCLVTRGT KWIANNWINV DPSRARQALF QQEMARLARE
GGTDSQPEWA LDRAYRDARV EL


Related products :

Catalog number Product name Quantity
EIAAB29551 HIF-PH4,HIF-prolyl hydroxylase 4,Homo sapiens,HPH-4,Human,Hypoxia-inducible factor prolyl hydroxylase 4,P4HTM,P4H-TM,PH4,Transmembrane prolyl 4-hydroxylase
EIAAB29550 HIF-PH4,HIF-prolyl hydroxylase 4,HPH-4,Hypoxia-inducible factor prolyl hydroxylase 4,Mouse,Mus musculus,P4htm,P4H-TM,Ph4,Transmembrane prolyl 4-hydroxylase
EIAAB12620 Egl nine homolog 3,EGLN3,HIF-PH3,HIF-prolyl hydroxylase 3,Homo sapiens,HPH-1,HPH-3,Human,Hypoxia-inducible factor prolyl hydroxylase 3,PHD3,Prolyl hydroxylase domain-containing protein 3
18-003-42538 Egl nine homolog 2 - EC 1.14.11.-; Hypoxia-inducible factor prolyl hydroxylase 1; HIF-prolyl hydroxylase 1; HIF-PH1; HPH-3; Prolyl hydroxylase domain-containing protein 1; PHD1; Estrogen-induced tag 6 0.05 mg Aff Pur
EIAAB12617 Egl nine homolog 2,EGLN2,EIT6,Estrogen-induced tag 6,HIF-PH1,HIF-prolyl hydroxylase 1,Homo sapiens,HPH-1,HPH-3,Human,Hypoxia-inducible factor prolyl hydroxylase 1,PHD1,Prolyl hydroxylase domain-contai
18-003-42563 Egl nine homolog 1 - EC 1.14.11.-; Hypoxia-inducible factor prolyl hydroxylase 2; HIF-prolyl hydroxylase 2; HIF-PH2; HPH-2; Prolyl hydroxylase domain-containing protein 2; PHD2; SM-20 Polyclonal 0.1 mg Protein A
EIAAB12614 C1orf12,Egl nine homolog 1,EGLN1,HIF-PH2,HIF-prolyl hydroxylase 2,Homo sapiens,HPH-2,Human,Hypoxia-inducible factor prolyl hydroxylase 2,PHD2,PNAS-118,PNAS-137,Prolyl hydroxylase domain-containing pro
EIAAB12618 Egl nine homolog 2,Egln2,Falkor,HIF-PH1,HIF-prolyl hydroxylase 1,HPH-1,Hypoxia-inducible factor prolyl hydroxylase 1,Mouse,Mus musculus
EIAAB12619 Egl nine homolog 3, mitochondrial,Egln3,HIF-PH3,HIF-prolyl hydroxylase 3,HPH-3,Hypoxia-inducible factor prolyl hydroxylase 3,Rat,Rattus norvegicus,Sm20,SM-20
EIAAB12615 Egl nine homolog 1,Egln1,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Hypoxia-inducible factor prolyl hydroxylase 2,Rat,Rattus norvegicus
EIAAB12621 Egl nine homolog 3,Egln3,HIF-PH3,HIF-prolyl hydroxylase 3,HPH-3,Hypoxia-inducible factor prolyl hydroxylase 3,Mouse,Mus musculus,SM-20
EIAAB12616 Egl nine homolog 1,Egln1,HIF-PH2,HIF-prolyl hydroxylase 2,HPH-2,Hypoxia-inducible factor prolyl hydroxylase 2,Mouse,Mus musculus,SM-20
SCH-MCA2890P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications C, WB, C 0.1 mg
SCH-MCA2889P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications P, WB, C 0.1 mg
SCH-MCA2888P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format HRP, Isotypes IgG2a, Applications P*, WB, 0.1 mg
MCA2888P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format HRP, Isotypes IgG2a, Applications P*, WB, 0.1 mg
MCA2890P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications C, WB, C 0.1 mg
MCA2889P MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2 HRP, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format HRP, Isotypes IgG1, Applications P, WB, C 0.1 mg
MCA2889GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.1 mg
MCA2890 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications C, WB, 0.2 mg
MCA2888 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications P*, WB 0.2 mg
MCA2890GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 3, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 3, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications C, WB, 0.1 mg
MCA2889 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.2 mg
MCA2888GA MOUSE ANTI HUMAN PROLYL HYDROXYLASE 1, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 1, Target Species Human, Host Mouse, Format Purified, Isotypes IgG2a, Applications P*, WB 0.1 mg
SCH-MCA2889 MOUSE ANTI HUMAN PROLYL HYDROXYLASE 2, Product Type Monoclonal Antibody, Specificity PROLYL HYDROXYLASE 2, Target Species Human, Host Mouse, Format Purified, Isotypes IgG1, Applications P, WB, 0.2 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur