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Receptor-type tyrosine-protein phosphatase C (EC 3.1.3.48) (Leukocyte common antigen) (L-CA) (T200) (CD antigen CD45)

 PTPRC_HUMAN             Reviewed;        1304 AA.
P08575; A8K7W6; Q16614; Q9H0Y6;
01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
19-JUL-2003, sequence version 2.
25-OCT-2017, entry version 205.
RecName: Full=Receptor-type tyrosine-protein phosphatase C;
EC=3.1.3.48;
AltName: Full=Leukocyte common antigen;
Short=L-CA;
AltName: Full=T200;
AltName: CD_antigen=CD45;
Flags: Precursor;
Name=PTPRC; Synonyms=CD45;
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), AND ALTERNATIVE SPLICING.
TISSUE=Lymphocyte;
PubMed=2824653; DOI=10.1084/jem.166.5.1548;
Streuli M., Hall L.R., Saga Y., Schlossman S.F., Saito H.;
"Differential usage of three exons generates at least five different
mRNAs encoding human leukocyte common antigens.";
J. Exp. Med. 166:1548-1566(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND ALTERNATIVE SPLICING.
PubMed=2956090;
Ralph S.J., Thomas M.L., Morton C.C., Trowbridge I.S.;
"Structural variants of human T200 glycoprotein (leukocyte-common
antigen).";
EMBO J. 6:1251-1257(1987).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Synovium;
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).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 146-192.
PubMed=2531281; DOI=10.1128/MCB.9.10.4550;
Tsai A.Y.M., Streuli M., Saito H.;
"Integrity of the exon 6 sequence is essential for tissue-specific
alternative splicing of human leukocyte common antigen pre-mRNA.";
Mol. Cell. Biol. 9:4550-4555(1989).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-1304.
TISSUE=Placenta;
PubMed=2971730;
Hall L.R., Streuli M., Schlossman S.F., Saito H.;
"Complete exon-intron organization of the human leukocyte common
antigen (CD45) gene.";
J. Immunol. 141:2781-2787(1988).
[6]
FUNCTION.
PubMed=2845400; DOI=10.1073/pnas.85.19.7182;
Charbonneau H., Tonks N.K., Walsh K.A., Fischer E.H.;
"The leukocyte common antigen (CD45): a putative receptor-linked
protein tyrosine phosphatase.";
Proc. Natl. Acad. Sci. U.S.A. 85:7182-7186(1988).
[7]
MUTAGENESIS.
PubMed=1695146;
Streuli M., Krueger N.X., Thai T., Tang M., Saito H.;
"Distinct functional roles of the two intracellular phosphatase like
domains of the receptor-linked protein tyrosine phosphatases LCA and
LAR.";
EMBO J. 9:2399-2407(1990).
[8]
INTERACTION WITH SKAP1, MUTAGENESIS OF CYS-851, AND FUNCTION.
PubMed=11909961; DOI=10.1128/MCB.22.8.2673-2686.2002;
Wu L., Fu J., Shen S.-H.;
"SKAP55 coupled with CD45 positively regulates T-cell receptor-
mediated gene transcription.";
Mol. Cell. Biol. 22:2673-2686(2002).
[9]
INTERACTION WITH DPP4, AND SUBCELLULAR LOCATION.
PubMed=12676959; DOI=10.1074/jbc.M212978200;
Salgado F.J., Lojo J., Alonso-Lebrero J.L., Lluis C., Franco R.,
Cordero O.J., Nogueira M.;
"A role for interleukin-12 in the regulation of T cell plasma membrane
compartmentation.";
J. Biol. Chem. 278:24849-24857(2003).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=T-cell;
PubMed=19367720; DOI=10.1021/pr800500r;
Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
"Phosphorylation analysis of primary human T lymphocytes using
sequential IMAC and titanium oxide enrichment.";
J. Proteome Res. 7:5167-5176(2008).
[11]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232 AND ASN-335.
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).
[12]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-232; ASN-240; ASN-276;
ASN-284; ASN-335; ASN-419; ASN-488 AND ASN-497.
TISSUE=Leukemic T-cell;
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973 AND SER-1297, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[15]
INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL11.
PubMed=22174689; DOI=10.1371/journal.ppat.1002432;
Gabaev I., Steinbrueck L., Pokoyski C., Pich A., Stanton R.J.,
Schwinzer R., Schulz T.F., Jacobs R., Messerle M., Kay-Fedorov P.C.;
"The human cytomegalovirus UL11 protein interacts with the receptor
tyrosine phosphatase CD45, resulting in functional paralysis of T
cells.";
PLoS Pathog. 7:E1002432-E1002432(2011).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-973 AND SER-992, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[17]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[18]
X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS) OF 622-1231 ALONE AND IN COMPLEX
WITH PHOSPHOPEPTIDE.
PubMed=15684325; DOI=10.1084/jem.20041890;
Nam H.J., Poy F., Saito H., Frederick C.A.;
"Structural basis for the function and regulation of the receptor
protein tyrosine phosphatase CD45.";
J. Exp. Med. 201:441-452(2005).
[19]
INVOLVEMENT IN SUSCEPTIBILITY TO MS.
PubMed=11101853; DOI=10.1038/82659;
Jacobsen M., Schweer D., Ziegler A., Gaber R., Schock S.,
Schwinzer R., Wonigeit K., Lindert R.-B., Kantarci O.,
Schaefer-Klein J., Schipper H.I., Oertel W.H., Heidenreich F.,
Weinshenker B.G., Sommer N., Hemmer B.;
"A point mutation in PTPRC is associated with the development of
multiple sclerosis.";
Nat. Genet. 26:495-499(2000).
[20]
VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL, AND CHARACTERIZATION
OF VARIANT T(-)B(+)NK(+) SCID 362-GLU-TYR-363 DEL.
PubMed=11145714; DOI=10.4049/jimmunol.166.2.1308;
Tchilian E.Z., Wallace D.L., Wells R.S., Flower D.R., Morgan G.,
Beverley P.C.L.;
"A deletion in the gene encoding the CD45 antigen in a patient with
SCID.";
J. Immunol. 166:1308-1313(2001).
[21]
VARIANTS [LARGE SCALE ANALYSIS] ALA-228 AND ARG-863.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Protein tyrosine-protein phosphatase required for T-cell
activation through the antigen receptor. Acts as a positive
regulator of T-cell coactivation upon binding to DPP4. The first
PTPase domain has enzymatic activity, while the second one seems
to affect the substrate specificity of the first one. Upon T-cell
activation, recruits and dephosphorylates SKAP1 and FYN.
Dephosphorylates LYN, and thereby modulates LYN activity (By
similarity). {ECO:0000250, ECO:0000269|PubMed:11909961,
ECO:0000269|PubMed:2845400}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044}.
-!- SUBUNIT: Binds GANAB and PRKCSH (By similarity). Interacts with
SKAP1. Interacts with DPP4; the interaction is enhanced in a
interleukin-12-dependent manner in activated lymphocytes.
Interacts with human cytomegalovirus protein UL11. {ECO:0000250,
ECO:0000269|PubMed:11909961, ECO:0000269|PubMed:12676959,
ECO:0000269|PubMed:15684325, ECO:0000269|PubMed:22174689}.
-!- INTERACTION:
P41240:CSK; NbExp=3; IntAct=EBI-1341, EBI-1380630;
P35222:CTNNB1; NbExp=2; IntAct=EBI-1341, EBI-491549;
P04626:ERBB2; NbExp=2; IntAct=EBI-1341, EBI-641062;
P20701:ITGAL; NbExp=2; IntAct=EBI-1341, EBI-961214;
P06239:LCK; NbExp=7; IntAct=EBI-1341, EBI-1348;
P06240:Lck (xeno); NbExp=2; IntAct=EBI-1341, EBI-1401;
P09382:LGALS1; NbExp=2; IntAct=EBI-1341, EBI-1048875;
Q02763:TEK; NbExp=3; IntAct=EBI-1341, EBI-2257090;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:12676959};
Single-pass type I membrane protein {ECO:0000269|PubMed:12676959}.
Membrane raft {ECO:0000269|PubMed:12676959}. Note=Colocalized with
DPP4 in membrane rafts.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=At least 8 isoforms are produced.;
Name=1;
IsoId=P08575-1; Sequence=Displayed;
Name=2;
IsoId=P08575-2; Sequence=VSP_007780;
-!- DOMAIN: The first PTPase domain interacts with SKAP1.
-!- PTM: Heavily N- and O-glycosylated. {ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
-!- DISEASE: Severe combined immunodeficiency autosomal recessive T-
cell-negative/B-cell-positive/NK-cell-positive (T(-)B(+)NK(+)
SCID) [MIM:608971]: A form of severe combined immunodeficiency
(SCID), a genetically and clinically heterogeneous group of rare
congenital disorders characterized by impairment of both humoral
and cell-mediated immunity, leukopenia, and low or absent antibody
levels. Patients present in infancy recurrent, persistent
infections by opportunistic organisms. The common characteristic
of all types of SCID is absence of T-cell-mediated cellular
immunity due to a defect in T-cell development.
{ECO:0000269|PubMed:11145714}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- DISEASE: Multiple sclerosis (MS) [MIM:126200]: A multifactorial,
inflammatory, demyelinating disease of the central nervous system.
Sclerotic lesions are characterized by perivascular infiltration
of monocytes and lymphocytes and appear as indurated areas in
pathologic specimens (sclerosis in plaques). The pathological
mechanism is regarded as an autoimmune attack of the myelin
sheath, mediated by both cellular and humoral immunity. Clinical
manifestations include visual loss, extra-ocular movement
disorders, paresthesias, loss of sensation, weakness, dysarthria,
spasticity, ataxia and bladder dysfunction. Genetic and
environmental factors influence susceptibility to the disease.
{ECO:0000269|PubMed:11101853}. Note=Disease susceptibility may be
associated with variations affecting the gene represented in this
entry.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 1/6 subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=PTPRCbase; Note=PTPRC mutation db;
URL="http://structure.bmc.lu.se/idbase/PTPRCbase/";
-!- WEB RESOURCE: Name=Wikipedia; Note=CD45 entry;
URL="https://en.wikipedia.org/wiki/CD45";
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EMBL; Y00638; CAA68669.1; -; mRNA.
EMBL; Y00062; CAA68269.1; -; mRNA.
EMBL; AK292131; BAF84820.1; -; mRNA.
EMBL; M23492; AAD15273.2; -; Genomic_DNA.
EMBL; M23496; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23466; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23467; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23468; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23469; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23470; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23471; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23472; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23473; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23474; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23475; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23476; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23477; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23478; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23479; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23480; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23481; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23482; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23483; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23484; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23485; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23486; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23487; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23488; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23489; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23490; AAD15273.2; JOINED; Genomic_DNA.
EMBL; M23491; AAD15273.2; JOINED; Genomic_DNA.
PIR; A46546; A46546.
RefSeq; NP_002829.3; NM_002838.4.
RefSeq; NP_563578.2; NM_080921.3.
UniGene; Hs.654514; -.
PDB; 1YGR; X-ray; 2.90 A; A/B=622-1231.
PDB; 1YGU; X-ray; 2.90 A; A/B=622-1231.
PDB; 5FMV; X-ray; 2.90 A; A/B=223-571.
PDB; 5FN6; X-ray; 3.30 A; A=223-479.
PDB; 5FN7; X-ray; 2.30 A; A/B=223-392.
PDBsum; 1YGR; -.
PDBsum; 1YGU; -.
PDBsum; 5FMV; -.
PDBsum; 5FN6; -.
PDBsum; 5FN7; -.
ProteinModelPortal; P08575; -.
SMR; P08575; -.
BioGrid; 111752; 24.
DIP; DIP-224N; -.
IntAct; P08575; 40.
MINT; MINT-1130341; -.
STRING; 9606.ENSP00000356346; -.
BindingDB; P08575; -.
ChEMBL; CHEMBL3243; -.
DEPOD; P08575; -.
iPTMnet; P08575; -.
PhosphoSitePlus; P08575; -.
SwissPalm; P08575; -.
UniCarbKB; P08575; -.
BioMuta; PTPRC; -.
DMDM; 33112650; -.
EPD; P08575; -.
MaxQB; P08575; -.
PaxDb; P08575; -.
PeptideAtlas; P08575; -.
PRIDE; P08575; -.
Ensembl; ENST00000367376; ENSP00000356346; ENSG00000081237.
Ensembl; ENST00000573477; ENSP00000461074; ENSG00000262418.
Ensembl; ENST00000573679; ENSP00000458322; ENSG00000262418.
Ensembl; ENST00000594404; ENSP00000471843; ENSG00000081237.
GeneID; 5788; -.
KEGG; hsa:5788; -.
UCSC; uc061fse.1; human. [P08575-1]
CTD; 5788; -.
DisGeNET; 5788; -.
GeneCards; PTPRC; -.
HGNC; HGNC:9666; PTPRC.
HPA; HPA000440; -.
MalaCards; PTPRC; -.
MIM; 126200; phenotype.
MIM; 151460; gene.
MIM; 608971; phenotype.
neXtProt; NX_P08575; -.
Orphanet; 169157; T-B+ severe combined immunodeficiency due to CD45 deficiency.
PharmGKB; PA34011; -.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
HOGENOM; HOG000049064; -.
HOVERGEN; HBG000066; -.
InParanoid; P08575; -.
KO; K06478; -.
OrthoDB; EOG091G015A; -.
PhylomeDB; P08575; -.
TreeFam; TF351829; -.
Reactome; R-HSA-202427; Phosphorylation of CD3 and TCR zeta chains.
Reactome; R-HSA-416700; Other semaphorin interactions.
Reactome; R-HSA-6798695; Neutrophil degranulation.
SignaLink; P08575; -.
SIGNOR; P08575; -.
ChiTaRS; PTPRC; human.
EvolutionaryTrace; P08575; -.
GeneWiki; PTPRC; -.
GenomeRNAi; 5788; -.
PRO; PR:P08575; -.
Proteomes; UP000005640; Chromosome 1.
CleanEx; HS_PTPRC; -.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005925; C:focal adhesion; ISS:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0030667; C:secretory granule membrane; TAS:Reactome.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:UniProtKB.
GO; GO:0005001; F:transmembrane receptor protein tyrosine phosphatase activity; TAS:ProtInc.
GO; GO:0042100; P:B cell proliferation; ISS:UniProtKB.
GO; GO:0050853; P:B cell receptor signaling pathway; ISS:UniProtKB.
GO; GO:0048539; P:bone marrow development; IMP:UniProtKB.
GO; GO:0044770; P:cell cycle phase transition; IMP:UniProtKB.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; ISS:UniProtKB.
GO; GO:0016311; P:dephosphorylation; ISS:UniProtKB.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IMP:UniProtKB.
GO; GO:0002378; P:immunoglobulin biosynthetic process; IMP:UniProtKB.
GO; GO:0006933; P:negative regulation of cell adhesion involved in substrate-bound cell migration; IMP:UniProtKB.
GO; GO:0001960; P:negative regulation of cytokine-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0006469; P:negative regulation of protein kinase activity; IDA:UniProtKB.
GO; GO:0001915; P:negative regulation of T cell mediated cytotoxicity; ISS:UniProtKB.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0050857; P:positive regulation of antigen receptor-mediated signaling pathway; ISS:UniProtKB.
GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:UniProtKB.
GO; GO:2000473; P:positive regulation of hematopoietic stem cell migration; IMP:UniProtKB.
GO; GO:0045860; P:positive regulation of protein kinase activity; NAS:UniProtKB.
GO; GO:2000648; P:positive regulation of stem cell proliferation; IMP:UniProtKB.
GO; GO:0042102; P:positive regulation of T cell proliferation; ISS:UniProtKB.
GO; GO:0006470; P:protein dephosphorylation; ISS:UniProtKB.
GO; GO:0051726; P:regulation of cell cycle; ISS:UniProtKB.
GO; GO:0051209; P:release of sequestered calcium ion into cytosol; ISS:UniProtKB.
GO; GO:0048864; P:stem cell development; IMP:UniProtKB.
GO; GO:0030217; P:T cell differentiation; ISS:UniProtKB.
GO; GO:0050852; P:T cell receptor signaling pathway; IDA:UniProtKB.
CDD; cd00063; FN3; 2.
Gene3D; 2.60.40.10; -; 2.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR024739; PTP_recept_N.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016335; Ptprc.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF12567; CD45; 1.
Pfam; PF00041; fn3; 2.
Pfam; PF12453; PTP_N; 1.
Pfam; PF00102; Y_phosphatase; 2.
PIRSF; PIRSF002004; Leukocyte_common_antigen; 1.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 2.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF49265; SSF49265; 1.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 2.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 1.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Complete proteome;
Disease mutation; Glycoprotein; Hydrolase; Membrane; Phosphoprotein;
Polymorphism; Protein phosphatase; Reference proteome; Repeat; SCID;
Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 23
CHAIN 24 1304 Receptor-type tyrosine-protein
phosphatase C.
/FTId=PRO_0000025470.
TOPO_DOM 24 575 Extracellular. {ECO:0000255}.
TRANSMEM 576 597 Helical. {ECO:0000255}.
TOPO_DOM 598 1304 Cytoplasmic. {ECO:0000255}.
DOMAIN 389 481 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 482 574 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 651 910 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 942 1226 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 851 857 Substrate binding. {ECO:0000250}.
ACT_SITE 851 851 Phosphocysteine intermediate.
ACT_SITE 1167 1167 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 819 819 Substrate. {ECO:0000250}.
BINDING 895 895 Substrate. {ECO:0000250}.
MOD_RES 681 681 Phosphotyrosine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 973 973 Phosphoserine.
{ECO:0000244|PubMed:19367720,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
MOD_RES 992 992 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 995 995 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 999 999 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1002 1002 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1003 1003 Phosphoserine.
{ECO:0000250|UniProtKB:P06800}.
MOD_RES 1007 1007 Phosphoserine.
{ECO:0000250|UniProtKB:P04157}.
MOD_RES 1297 1297 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
CARBOHYD 78 78 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 90 90 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 95 95 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 184 184 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 190 190 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 197 197 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 232 232 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 240 240 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 260 260 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 270 270 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 276 276 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 284 284 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 335 335 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19159218,
ECO:0000269|PubMed:19349973}.
CARBOHYD 378 378 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 419 419 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 468 468 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 488 488 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973}.
CARBOHYD 497 497 N-linked (GlcNAc...) asparagine;
atypical. {ECO:0000269|PubMed:19349973}.
CARBOHYD 529 529 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 32 192 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:2956090}.
/FTId=VSP_007780.
VARIANT 191 191 T -> A (in dbSNP:rs4915154).
/FTId=VAR_036860.
VARIANT 228 228 E -> A (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035653.
VARIANT 294 294 I -> L (in dbSNP:rs2230606).
/FTId=VAR_051763.
VARIANT 362 363 Missing (in T(-)B(+)NK(+) SCID;
associated with lack of surface
expression).
{ECO:0000269|PubMed:11145714}.
/FTId=VAR_021205.
VARIANT 421 421 T -> I (in dbSNP:rs6696162).
/FTId=VAR_051764.
VARIANT 568 568 H -> Q (in dbSNP:rs12136658).
/FTId=VAR_051765.
VARIANT 863 863 G -> R (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035654.
VARIANT 1283 1283 S -> R (in dbSNP:rs2298872).
/FTId=VAR_020303.
MUTAGEN 851 851 C->S: Loss of activity. Abolishes
interaction with SKAP1.
{ECO:0000269|PubMed:11909961}.
CONFLICT 650 650 L -> P (in Ref. 1; CAA68669).
{ECO:0000305}.
CONFLICT 1207 1207 P -> L (in Ref. 1; CAA68669).
{ECO:0000305}.
HELIX 226 229 {ECO:0000244|PDB:5FN7}.
TURN 230 232 {ECO:0000244|PDB:5FN7}.
STRAND 235 240 {ECO:0000244|PDB:5FN7}.
TURN 241 244 {ECO:0000244|PDB:5FN7}.
STRAND 245 250 {ECO:0000244|PDB:5FN7}.
STRAND 257 261 {ECO:0000244|PDB:5FN7}.
HELIX 264 266 {ECO:0000244|PDB:5FN7}.
STRAND 267 271 {ECO:0000244|PDB:5FN7}.
STRAND 276 282 {ECO:0000244|PDB:5FN7}.
STRAND 286 289 {ECO:0000244|PDB:5FN7}.
STRAND 291 296 {ECO:0000244|PDB:5FN7}.
HELIX 301 303 {ECO:0000244|PDB:5FN7}.
STRAND 304 308 {ECO:0000244|PDB:5FN7}.
HELIX 312 314 {ECO:0000244|PDB:5FN7}.
TURN 315 317 {ECO:0000244|PDB:5FN7}.
STRAND 319 325 {ECO:0000244|PDB:5FN7}.
HELIX 333 335 {ECO:0000244|PDB:5FN7}.
STRAND 336 342 {ECO:0000244|PDB:5FN7}.
STRAND 345 354 {ECO:0000244|PDB:5FN7}.
STRAND 362 371 {ECO:0000244|PDB:5FN7}.
STRAND 374 386 {ECO:0000244|PDB:5FN7}.
STRAND 394 399 {ECO:0000244|PDB:5FMV}.
STRAND 401 404 {ECO:0000244|PDB:5FMV}.
STRAND 406 411 {ECO:0000244|PDB:5FMV}.
STRAND 418 425 {ECO:0000244|PDB:5FMV}.
STRAND 427 436 {ECO:0000244|PDB:5FMV}.
STRAND 441 444 {ECO:0000244|PDB:5FMV}.
STRAND 452 468 {ECO:0000244|PDB:5FMV}.
STRAND 472 477 {ECO:0000244|PDB:5FMV}.
STRAND 487 497 {ECO:0000244|PDB:5FMV}.
STRAND 499 504 {ECO:0000244|PDB:5FMV}.
STRAND 516 539 {ECO:0000244|PDB:5FMV}.
STRAND 547 555 {ECO:0000244|PDB:5FMV}.
STRAND 564 569 {ECO:0000244|PDB:5FMV}.
TURN 633 635 {ECO:0000244|PDB:1YGR}.
HELIX 636 656 {ECO:0000244|PDB:1YGR}.
STRAND 663 665 {ECO:0000244|PDB:1YGR}.
TURN 668 670 {ECO:0000244|PDB:1YGR}.
HELIX 673 678 {ECO:0000244|PDB:1YGR}.
TURN 688 690 {ECO:0000244|PDB:1YGR}.
STRAND 691 693 {ECO:0000244|PDB:1YGR}.
STRAND 698 700 {ECO:0000244|PDB:1YGR}.
TURN 701 704 {ECO:0000244|PDB:1YGR}.
STRAND 705 711 {ECO:0000244|PDB:1YGR}.
STRAND 714 716 {ECO:0000244|PDB:1YGR}.
STRAND 720 723 {ECO:0000244|PDB:1YGR}.
TURN 728 730 {ECO:0000244|PDB:1YGR}.
HELIX 731 740 {ECO:0000244|PDB:1YGR}.
STRAND 745 748 {ECO:0000244|PDB:1YGR}.
STRAND 752 754 {ECO:0000244|PDB:1YGR}.
STRAND 757 759 {ECO:0000244|PDB:1YGR}.
TURN 767 769 {ECO:0000244|PDB:1YGR}.
STRAND 771 774 {ECO:0000244|PDB:1YGR}.
STRAND 777 786 {ECO:0000244|PDB:1YGR}.
STRAND 788 802 {ECO:0000244|PDB:1YGR}.
STRAND 807 814 {ECO:0000244|PDB:1YGR}.
HELIX 826 836 {ECO:0000244|PDB:1YGR}.
STRAND 847 850 {ECO:0000244|PDB:1YGR}.
STRAND 852 855 {ECO:0000244|PDB:1YGR}.
HELIX 856 869 {ECO:0000244|PDB:1YGR}.
HELIX 871 874 {ECO:0000244|PDB:1YGR}.
STRAND 875 877 {ECO:0000244|PDB:1YGR}.
HELIX 879 887 {ECO:0000244|PDB:1YGR}.
HELIX 897 913 {ECO:0000244|PDB:1YGR}.
HELIX 920 922 {ECO:0000244|PDB:1YGR}.
HELIX 923 930 {ECO:0000244|PDB:1YGR}.
HELIX 941 948 {ECO:0000244|PDB:1YGR}.
HELIX 960 962 {ECO:0000244|PDB:1YGR}.
HELIX 966 968 {ECO:0000244|PDB:1YGR}.
TURN 979 981 {ECO:0000244|PDB:1YGR}.
STRAND 1018 1022 {ECO:0000244|PDB:1YGR}.
STRAND 1029 1034 {ECO:0000244|PDB:1YGR}.
TURN 1038 1040 {ECO:0000244|PDB:1YGR}.
HELIX 1041 1050 {ECO:0000244|PDB:1YGR}.
STRAND 1055 1058 {ECO:0000244|PDB:1YGR}.
STRAND 1062 1064 {ECO:0000244|PDB:1YGR}.
STRAND 1067 1070 {ECO:0000244|PDB:1YGR}.
STRAND 1088 1093 {ECO:0000244|PDB:1YGR}.
STRAND 1095 1105 {ECO:0000244|PDB:1YGR}.
STRAND 1113 1120 {ECO:0000244|PDB:1YGR}.
STRAND 1125 1127 {ECO:0000244|PDB:1YGR}.
HELIX 1132 1143 {ECO:0000244|PDB:1YGR}.
STRAND 1163 1171 {ECO:0000244|PDB:1YGR}.
HELIX 1174 1189 {ECO:0000244|PDB:1YGR}.
STRAND 1190 1192 {ECO:0000244|PDB:1YGR}.
HELIX 1195 1205 {ECO:0000244|PDB:1YGR}.
TURN 1207 1210 {ECO:0000244|PDB:1YGR}.
HELIX 1213 1225 {ECO:0000244|PDB:1YGR}.
SEQUENCE 1304 AA; 147254 MW; A08FC22D6069BAF7 CRC64;
MYLWLKLLAF GFAFLDTEVF VTGQSPTPSP TGLTTAKMPS VPLSSDPLPT HTTAFSPAST
FERENDFSET TTSLSPDNTS TQVSPDSLDN ASAFNTTGVS SVQTPHLPTH ADSQTPSAGT
DTQTFSGSAA NAKLNPTPGS NAISDVPGER STASTFPTDP VSPLTTTLSL AHHSSAALPA
RTSNTTITAN TSDAYLNASE TTTLSPSGSA VISTTTIATT PSKPTCDEKY ANITVDYLYN
KETKLFTAKL NVNENVECGN NTCTNNEVHN LTECKNASVS ISHNSCTAPD KTLILDVPPG
VEKFQLHDCT QVEKADTTIC LKWKNIETFT CDTQNITYRF QCGNMIFDNK EIKLENLEPE
HEYKCDSEIL YNNHKFTNAS KIIKTDFGSP GEPQIIFCRS EAAHQGVITW NPPQRSFHNF
TLCYIKETEK DCLNLDKNLI KYDLQNLKPY TKYVLSLHAY IIAKVQRNGS AAMCHFTTKS
APPSQVWNMT VSMTSDNSMH VKCRPPRDRN GPHERYHLEV EAGNTLVRNE SHKNCDFRVK
DLQYSTDYTF KAYFHNGDYP GEPFILHHST SYNSKALIAF LAFLIIVTSI ALLVVLYKIY
DLHKKRSCNL DEQQELVERD DEKQLMNVEP IHADILLETY KRKIADEGRL FLAEFQSIPR
VFSKFPIKEA RKPFNQNKNR YVDILPYDYN RVELSEINGD AGSNYINASY IDGFKEPRKY
IAAQGPRDET VDDFWRMIWE QKATVIVMVT RCEEGNRNKC AEYWPSMEEG TRAFGDVVVK
INQHKRCPDY IIQKLNIVNK KEKATGREVT HIQFTSWPDH GVPEDPHLLL KLRRRVNAFS
NFFSGPIVVH CSAGVGRTGT YIGIDAMLEG LEAENKVDVY GYVVKLRRQR CLMVQVEAQY
ILIHQALVEY NQFGETEVNL SELHPYLHNM KKRDPPSEPS PLEAEFQRLP SYRSWRTQHI
GNQEENKSKN RNSNVIPYDY NRVPLKHELE MSKESEHDSD ESSDDDSDSE EPSKYINASF
IMSYWKPEVM IAAQGPLKET IGDFWQMIFQ RKVKVIVMLT ELKHGDQEIC AQYWGEGKQT
YGDIEVDLKD TDKSSTYTLR VFELRHSKRK DSRTVYQYQY TNWSVEQLPA EPKELISMIQ
VVKQKLPQKN SSEGNKHHKS TPLLIHCRDG SQQTGIFCAL LNLLESAETE EVVDIFQVVK
ALRKARPGMV STFEQYQFLY DVIASTYPAQ NGQVKKNNHQ EDKIEFDNEV DKVKQDANCV
NPLGAPEKLP EAKEQAEGSE PTSGTEGPEH SVNGPASPAL NQGS


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