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Receptor-type tyrosine-protein phosphatase H (R-PTP-H) (EC 3.1.3.48) (Stomach cancer-associated protein tyrosine phosphatase 1) (SAP-1) (Transmembrane-type protein-tyrosine phosphatase type H)

 PTPRH_HUMAN             Reviewed;        1115 AA.
Q9HD43; C9JCH2; Q15426; Q2NKN9; Q2NKP0;
26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
25-OCT-2017, entry version 138.
RecName: Full=Receptor-type tyrosine-protein phosphatase H;
Short=R-PTP-H;
EC=3.1.3.48;
AltName: Full=Stomach cancer-associated protein tyrosine phosphatase 1;
Short=SAP-1;
AltName: Full=Transmembrane-type protein-tyrosine phosphatase type H;
Flags: Precursor;
Name=PTPRH; Synonyms=SAP1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
VARIANT GLU-823.
PubMed=8294459;
Matozaki T., Suzuki T., Uchida T., Inazawa J., Ariyama T., Matsuda K.,
Horita K., Noguchi H., Mizuno H., Sakamoto C., Kasuga M.;
"Molecular cloning of a human transmembrane-type protein tyrosine
phosphatase and its expression in gastrointestinal cancers.";
J. Biol. Chem. 269:2075-2081(1994).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
PubMed=11435690;
Marneros A.G., Mehenni H., Reichenberger E., Antonarakis S.E.,
Krieg T., Olsen B.R.;
"Gene for the human transmembrane-type protein tyrosine phosphatase H
(PTPRH): genomic structure, fine-mapping and its exclusion as a
candidate for Peutz-Jeghers syndrome.";
Cytogenet. Cell Genet. 92:213-216(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND
VARIANTS TYR-348 AND GLU-823.
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).
[5]
FUNCTION, AND MUTAGENESIS OF ASP-986 AND CYS-1020.
PubMed=11278335; DOI=10.1074/jbc.M007208200;
Noguchi T., Tsuda M., Takeda H., Takada T., Inagaki K., Yamao T.,
Fukunaga K., Matozaki T., Kasuga M.;
"Inhibition of cell growth and spreading by stomach cancer-associated
protein-tyrosine phosphatase-1 (SAP-1) through dephosphorylation of
p130cas.";
J. Biol. Chem. 276:15216-15224(2001).
[6]
FUNCTION, AND MUTAGENESIS OF CYS-1020.
PubMed=12101188; DOI=10.1074/jbc.M206541200;
Takada T., Noguchi T., Inagaki K., Hosooka T., Fukunaga K., Yamao T.,
Ogawa W., Matozaki T., Kasuga M.;
"Induction of apoptosis by stomach cancer-associated protein-tyrosine
phosphatase-1.";
J. Biol. Chem. 277:34359-34366(2002).
[7]
FUNCTION, DOMAIN, TISSUE SPECIFICITY, AND INTERACTION WITH LCK.
PubMed=12837766; DOI=10.1074/jbc.M300648200;
Ito T., Okazawa H., Maruyama K., Tomizawa K., Motegi S., Ohnishi H.,
Kuwano H., Kosugi A., Matozaki T.;
"Interaction of SAP-1, a transmembrane-type protein-tyrosine
phosphatase, with the tyrosine kinase Lck. Roles in regulation of T
cell function.";
J. Biol. Chem. 278:34854-34863(2003).
[8]
SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
PubMed=12879010; DOI=10.1038/sj.onc.1206588;
Nagano H., Noguchi T., Inagaki K., Yoon S., Matozaki T., Itoh H.,
Kasuga M., Hayashi Y.;
"Downregulation of stomach cancer-associated protein tyrosine
phosphatase-1 (SAP-1) in advanced human hepatocellular carcinoma.";
Oncogene 22:4656-4663(2003).
[9]
FUNCTION, SUBUNIT, ENZYME REGULATION, AND DOMAIN.
PubMed=15850787; DOI=10.1016/j.bbrc.2005.03.196;
Waelchli S., Espanel X., Hooft van Huijsduijnen R.;
"Sap-1/PTPRH activity is regulated by reversible dimerization.";
Biochem. Biophys. Res. Commun. 331:497-502(2005).
-!- FUNCTION: Protein phosphatase that may contribute to contact
inhibition of cell growth and motility by mediating the
dephosphorylation of focal adhesion-associated substrates and thus
negatively regulating integrin-promoted signaling processes.
Induces apoptotic cell death by at least two distinct mechanisms:
inhibition of cell survival signaling mediated by PI 3-kinase,
Akt, and ILK and activation of a caspase-dependent proapoptotic
pathway. Inhibits the basal activity of LCK and its activation in
response to TCR stimulation and TCR-induced activation of MAP
kinase and surface expression of CD69. Inhibits TCR-induced
tyrosine phosphorylation of LAT and ZAP70. Inhibits both basal
activity of DOK1 and its CD2-induced tyrosine phosphorylation.
Induces dephosphorylation of BCAR1, focal adhesion kinase and SRC.
Reduces migratory activity of activity of Jurkat cells. Reduces
tyrosine phosphorylation of CEACAM20 and thereby contributes to
suppress the intestinal immune response CEACAM20 (By similarity).
{ECO:0000250|UniProtKB:E9Q0N2, ECO:0000269|PubMed:11278335,
ECO:0000269|PubMed:12101188, ECO:0000269|PubMed:12837766,
ECO:0000269|PubMed:15850787}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- ENZYME REGULATION: Regulated by reversible dimerization.
Dimerization reduces its catalytic activity.
{ECO:0000269|PubMed:15850787}.
-!- SUBUNIT: Homodimer; disulfide-linked (Probable). Interacts with
LCK (PubMed:12837766). Interacts (phosphorylated form) with GRB2
(via SH2 domain) (By similarity). Interacts (phosphorylated form)
with FYN (via SH2 domain) (By similarity). Interacts (via
extracellular domain) with CEACAM20 (via extracellular domain);
the interaction dephosphorylates CEACAM20 (By similarity).
{ECO:0000250|UniProtKB:E9Q0N2, ECO:0000269|PubMed:12837766,
ECO:0000305|PubMed:15850787}.
-!- INTERACTION:
P49366:DHPS; NbExp=3; IntAct=EBI-1267176, EBI-741925;
P10912:GHR; NbExp=4; IntAct=EBI-1267176, EBI-286316;
P60410:KRTAP10-8; NbExp=3; IntAct=EBI-1267176, EBI-10171774;
-!- SUBCELLULAR LOCATION: Cell projection, microvillus membrane
{ECO:0000250|UniProtKB:E9Q0N2}; Single-pass type I membrane
protein {ECO:0000305}. Apical cell membrane
{ECO:0000250|UniProtKB:E9Q0N2}; Single-pass type I membrane
protein {ECO:0000305}. Cytoplasm {ECO:0000269|PubMed:12879010}.
Note=Colocalizes with CEACAM20 at the apical brush border of
intestinal cells. {ECO:0000250|UniProtKB:E9Q0N2}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9HD43-1; Sequence=Displayed;
Name=2;
IsoId=Q9HD43-2; Sequence=VSP_031318;
Name=3;
IsoId=Q9HD43-3; Sequence=VSP_054222;
-!- TISSUE SPECIFICITY: Expressed at high levels in the brain, spleen
and liver and at lower levels in the heart and stomach. Expressed
in pancreatic and colorectal cancer cells, but not in normal
pancreas or colon. Expression in hepatocellular carcinoma is
related to the differentiation status of the tumor and expression
is inversely related to tumor aggressiveness.
{ECO:0000269|PubMed:12837766, ECO:0000269|PubMed:12879010,
ECO:0000269|PubMed:8294459}.
-!- INDUCTION: Induced at the early stage of hepatocellular carcinoma
and is suppressed at later stages. {ECO:0000269|PubMed:12879010}.
-!- DOMAIN: The extracellular domain mediates homodimerization. One or
more cysteines in the extracellular domain is essential for the
formation of dimers probably by forming a disulfide bond.
-!- DOMAIN: The cytoplasmic domain mediates the interaction with LCK.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 3 subfamily. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA03645.2; Type=Frameshift; Positions=213, 244, 264, 287, 291; Evidence={ECO:0000305};
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EMBL; D15049; BAA03645.2; ALT_FRAME; mRNA.
EMBL; AF275150; AAF91411.1; -; Genomic_DNA.
EMBL; AF275131; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275132; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275133; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275134; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275135; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275136; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275137; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275138; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275139; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275140; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275141; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275142; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275143; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275144; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275145; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275146; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275147; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275148; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AF275149; AAF91411.1; JOINED; Genomic_DNA.
EMBL; AC010327; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC111715; AAI11716.1; -; mRNA.
EMBL; BC111716; AAI11717.1; -; mRNA.
CCDS; CCDS33110.1; -. [Q9HD43-1]
CCDS; CCDS54321.1; -. [Q9HD43-3]
PIR; A49724; A49724.
UniGene; Hs.179770; -.
ProteinModelPortal; Q9HD43; -.
SMR; Q9HD43; -.
IntAct; Q9HD43; 12.
MINT; MINT-1349530; -.
STRING; 9606.ENSP00000365528; -.
DEPOD; Q9HD43; -.
iPTMnet; Q9HD43; -.
PhosphoSitePlus; Q9HD43; -.
BioMuta; PTPRH; -.
DMDM; 296452983; -.
MaxQB; Q9HD43; -.
PaxDb; Q9HD43; -.
PeptideAtlas; Q9HD43; -.
PRIDE; Q9HD43; -.
Ensembl; ENST00000263434; ENSP00000263434; ENSG00000080031.
Ensembl; ENST00000376350; ENSP00000365528; ENSG00000080031.
UCSC; uc002qjq.4; human. [Q9HD43-1]
DisGeNET; 5794; -.
EuPathDB; HostDB:ENSG00000080031.9; -.
GeneCards; PTPRH; -.
HGNC; HGNC:9672; PTPRH.
HPA; HPA042300; -.
MIM; 602510; gene.
neXtProt; NX_Q9HD43; -.
PharmGKB; PA34017; -.
eggNOG; KOG0791; Eukaryota.
eggNOG; COG5599; LUCA.
HOGENOM; HOG000170539; -.
HOVERGEN; HBG108307; -.
InParanoid; Q9HD43; -.
OrthoDB; EOG091G08FR; -.
PhylomeDB; Q9HD43; -.
TreeFam; TF351926; -.
BRENDA; 3.1.3.48; 2681.
SIGNOR; Q9HD43; -.
PRO; PR:Q9HD43; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000080031; -.
CleanEx; HS_PTPRH; -.
Genevisible; Q9HD43; HS.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
GO; GO:0006470; P:protein dephosphorylation; TAS:ProtInc.
CDD; cd00063; FN3; 7.
Gene3D; 1.20.5.100; -; 1.
Gene3D; 2.60.40.10; -; 7.
Gene3D; 3.90.190.10; -; 1.
InterPro; IPR021157; Cyt_c1_TM_anchor_C.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR028855; R-PTP-H.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
PANTHER; PTHR19134:SF297; PTHR19134:SF297; 5.
Pfam; PF00041; fn3; 6.
Pfam; PF00102; Y_phosphatase; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 7.
SMART; SM00194; PTPc; 1.
SMART; SM00404; PTPc_motif; 1.
SUPFAM; SSF49265; SSF49265; 4.
SUPFAM; SSF52799; SSF52799; 1.
PROSITE; PS50853; FN3; 7.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 1.
1: Evidence at protein level;
Alternative splicing; Apoptosis; Cell membrane; Cell projection;
Complete proteome; Cytoplasm; Disulfide bond; Glycoprotein; Hydrolase;
Membrane; Phosphoprotein; Polymorphism; Protein phosphatase;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 27 {ECO:0000255}.
CHAIN 28 1115 Receptor-type tyrosine-protein
phosphatase H.
/FTId=PRO_0000318950.
TOPO_DOM 28 754 Extracellular. {ECO:0000255}.
TRANSMEM 755 775 Helical. {ECO:0000255}.
TOPO_DOM 776 1115 Cytoplasmic. {ECO:0000255}.
DOMAIN 32 121 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 122 209 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 210 299 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 300 387 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 388 477 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 478 563 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 564 666 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 665 749 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 820 1079 Tyrosine-protein phosphatase.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
ACT_SITE 1020 1020 Phosphocysteine intermediate.
{ECO:0000255|PROSITE-ProRule:PRU00160,
ECO:0000255|PROSITE-ProRule:PRU10044}.
MOD_RES 1094 1094 Phosphotyrosine.
{ECO:0000250|UniProtKB:E9Q0N2}.
MOD_RES 1102 1102 Phosphotyrosine.
{ECO:0000250|UniProtKB:E9Q0N2}.
CARBOHYD 35 35 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 256 256 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 285 285 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 350 350 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 434 434 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 556 556 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 642 642 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 84 261 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_031318.
VAR_SEQ 126 303 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_054222.
VARIANT 232 232 D -> N (in dbSNP:rs55870162).
/FTId=VAR_061762.
VARIANT 243 243 V -> I (in dbSNP:rs45535035).
/FTId=VAR_061763.
VARIANT 348 348 H -> Y (in dbSNP:rs2288515).
{ECO:0000269|PubMed:15489334}.
/FTId=VAR_038918.
VARIANT 543 543 L -> F (in dbSNP:rs16986309).
/FTId=VAR_038919.
VARIANT 781 781 K -> N (in dbSNP:rs2288523).
/FTId=VAR_038920.
VARIANT 823 823 K -> E (in dbSNP:rs890870).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:8294459}.
/FTId=VAR_038921.
VARIANT 831 831 G -> D (in dbSNP:rs36092369).
/FTId=VAR_061764.
VARIANT 1076 1076 I -> V (in dbSNP:rs2288419).
/FTId=VAR_038922.
MUTAGEN 986 986 D->A: Loss of activity. Acts as a
dominant negative mutant.
{ECO:0000269|PubMed:11278335}.
MUTAGEN 1020 1020 C->S: Loss of activity. No induction of
apoptosis. {ECO:0000269|PubMed:11278335,
ECO:0000269|PubMed:12101188}.
CONFLICT 294 294 A -> T (in Ref. 1; BAA03645).
{ECO:0000305}.
CONFLICT 422 422 E -> G (in Ref. 1; BAA03645).
{ECO:0000305}.
CONFLICT 951 951 G -> D (in Ref. 4; AAI11716).
{ECO:0000305}.
CONFLICT 1109 1109 Q -> K (in Ref. 4; AAI11716).
{ECO:0000305}.
SEQUENCE 1115 AA; 122352 MW; A7A1AB24CFCD3846 CRC64;
MAGAGGGLGV WGNLVLLGLC SWTGARAPAP NPGRNLTVET QTTSSISLSW EVPDGLDSQN
SNYWVQCTGD GGTTETRNTT ATNVTVDGLG PGSLYTCSVW VEKDGVNSSV GTVTTATAPN
PVRNLRVEAQ TNSSIALTWE VPDGPDPQNS TYGVEYTGDG GRAGTRSTAH TNITVDGLEP
GCLYAFSMWV GKNGINSSRE TRNATTAHNP VRNLRVEAQT TSSISLSWEV PDGTDPQNST
YCVQCTGDGG RTETRNTTDT RVTVDGLGPG SLYTCSVWVE KDGVNSSVEI VTSATAPNPV
RNLTVEAQTN SSIALTWEVP DGPDPQNSTY GVEYTGDGGR AGTRSTAHTN ITVDRLEPGC
LYVFSVWVGK NGINSSRETR NATTAPNPVR NLHMETQTNS SIALCWEVPD GPYPQDYTYW
VEYTGDGGGT ETRNTTNTSV TAERLEPGTL YTFSVWAEKN GARGSRQNVS ISTVPNAVTS
LSKQDWTNST IALRWTAPQG PGQSSYSYWV SWVREGMTDP RTQSTSGTDI TLKELEAGSL
YHLTVWAERN EVRGYNSTLT AATAPNEVTD LQNETQTKNS VMLWWKAPGD PHSQLYVYWV
QWASKGHPRR GQDPQANWVN QTSRTNETWY KVEALEPGTL YNFTVWAERN DVASSTQSLC
ASTYPDTVTI TSCVSTSAGY GVNLIWSCPQ GGYEAFELEV GGQRGSQDRS SCGEAVSVLG
LGPARSYPAT ITTIWDGMKV VSHSVVCHTE SAGVIAGAFV GILLFLILVG LLIFFLKRRN
KKKQQKPELR DLVFSSPGDI PAEDFADHVR KNERDSNCGF ADKYQQLSLV GHSQSQMVAS
ASENNAKNRY RNVLPYDWSR VPLKPIHEEP GSDYINASFM PGLWSPQEFI ATQGPLPQTV
GDFWRLVWEQ QSHTLVMLTN CMEAGRVKCE HYWPLDSQPC THGHLRVTLV GEEVMENWTV
RELLLLQVEE QKTLSVRQFH YQAWPDHGVP SSPDTLLAFW RMLRQWLDQT MEGGPPIVHC
SAGVGRTGTL IALDVLLRQL QSEGLLGPFS FVRKMRESRP LMVQTEAQYV FLHQCILRFL
QQSAQAPAEK EVPYEDVENL IYENVAAIQA HKLEV


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EIAAB33048 Mouse,Mus musculus,Neural-specific protein-tyrosine phosphatase,Ptpn5,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
PP-SHP1-020 SHP-1, Tyrosine-protein phosphatase non-receptor type 6, EC 3.1.3.48, Protein-tyrosine phosphatase 1C, PTP-1C, Hematopoietic cell protein-tyrosine phosphatase, SH-PTP1, Protein-tyrosine phosphatase SH 20
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.001 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.005 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.01 mg
10-782-55086 Tyrosine-protein phosphatase non-receptor type 6 - EC 3.1.3.48; Protein-tyrosine phosphatase 1C; PTP-1C; Hematopoietic cell protein-tyrosine phosphatase; SH-PTP1; Protein-tyrosine phosphatase SHP-1 N_ 0.02 mg
EIAAB33107 PC12-PTP1,Protein-tyrosine phosphatase PCPTP1,Ptp,Ptprr,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase R,R-PTP-R,Tyrosine phosphatase CBPTP
EIAAB33054 Hematopoietic protein-tyrosine phosphatase,HEPTP,Homo sapiens,Human,Protein-tyrosine phosphatase LC-PTP,PTPN7,Tyrosine-protein phosphatase non-receptor type 7
EIAAB33056 Hematopoietic protein-tyrosine phosphatase,HEPTP,Lcptp,Protein-tyrosine phosphatase LC-PTP,Ptpn7,Rat,Rattus norvegicus,Tyrosine-protein phosphatase non-receptor type 7
EIAAB33119 Embryonic stem cell protein-tyrosine phosphatase,ES cell phosphatase,Esp,Osteotesticular protein-tyrosine phosphatase,OST-PTP,Ptprv,Rat,Rattus norvegicus,Receptor-type tyrosine-protein phosphatase V,R
EIAAB33021 Protein-tyrosine phosphatase 1D,Protein-tyrosine phosphatase SYP,PTP-1D,Ptpn11,Rat,Rattus norvegicus,Shp2,SHP-2,SH-PTP2,Tyrosine-protein phosphatase non-receptor type 11
15-288-21551 Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.1 mg
15-288-21497A Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.05 mg
10-782-55091 Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.001 mg
10-782-55091 Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.005 mg
15-288-21497A Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.1 mg
10-782-55091 Tyrosine-protein phosphatase non-receptor type 13 - EC 3.1.3.48; Protein-tyrosine phosphatase 1E; PTP-E1; hPTPE1; PTP-BAS; Protein-tyrosine phosphatase PTPL1; Fas-associated protein-tyrosine phosphata 0.02 mg


 

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