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Receptor-type tyrosine-protein phosphatase S (R-PTP-S) (EC 3.1.3.48) (Leukocyte common antigen-related protein-tyrosine phosphatase 2) (LAR-PTP2) (Receptor-type tyrosine-protein phosphatase sigma) (R-PTP-sigma)

 PTPRS_RAT               Reviewed;        1907 AA.
Q64605; Q07808; Q3KRE9; Q64621; Q64675;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
24-JUL-2007, sequence version 2.
22-NOV-2017, entry version 127.
RecName: Full=Receptor-type tyrosine-protein phosphatase S;
Short=R-PTP-S;
EC=3.1.3.48 {ECO:0000269|PubMed:8068021};
AltName: Full=Leukocyte common antigen-related protein-tyrosine phosphatase 2;
Short=LAR-PTP2 {ECO:0000303|PubMed:8068021};
AltName: Full=Receptor-type tyrosine-protein phosphatase sigma;
Short=R-PTP-sigma;
Flags: Precursor;
Name=Ptprs;
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), CATALYTIC ACTIVITY, FUNCTION,
AND TISSUE SPECIFICITY.
STRAIN=Sprague-Dawley; TISSUE=Liver;
PubMed=8068021; DOI=10.1042/bj3020039;
Zhang W.-R., Hashimoto N., Ahmad F., Ding W., Goldstein B.J.;
"Molecular cloning and expression of a unique receptor-like protein-
tyrosine-phosphatase in the leucocyte-common-antigen-related phosphate
family.";
Biochem. J. 302:39-47(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Prostate;
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).
[3]
INTERACTION WITH NTRK1 AND NTRK3.
PubMed=17967490; DOI=10.1016/j.bbamcr.2007.06.008;
Faux C., Hawadle M., Nixon J., Wallace A., Lee S., Murray S.,
Stoker A.;
"PTPsigma binds and dephosphorylates neurotrophin receptors and can
suppress NGF-dependent neurite outgrowth from sensory neurons.";
Biochim. Biophys. Acta 1773:1689-1700(2007).
[4]
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22519304; DOI=10.1111/j.1471-4159.2012.07762.x;
Horn K.E., Xu B., Gobert D., Hamam B.N., Thompson K.M., Wu C.L.,
Bouchard J.F., Uetani N., Racine R.J., Tremblay M.L., Ruthazer E.S.,
Chapman C.A., Kennedy T.E.;
"Receptor protein tyrosine phosphatase sigma regulates synapse
structure, function and plasticity.";
J. Neurochem. 122:147-161(2012).
[5]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1328-1614.
PubMed=18058037; DOI=10.1007/s10969-007-9036-1;
Almo S.C., Bonanno J.B., Sauder J.M., Emtage S., Dilorenzo T.P.,
Malashkevich V., Wasserman S.R., Swaminathan S., Eswaramoorthy S.,
Agarwal R., Kumaran D., Madegowda M., Ragumani S., Patskovsky Y.,
Alvarado J., Ramagopal U.A., Faber-Barata J., Chance M.R., Sali A.,
Fiser A., Zhang Z.Y., Lawrence D.S., Burley S.K.;
"Structural genomics of protein phosphatases.";
J. Struct. Funct. Genomics 8:121-140(2007).
-!- FUNCTION: Cell surface receptor that binds to glycosaminoglycans,
including chondroitin sulfate proteoglycans and heparan sulfate
proteoglycans. Binding to chondroitin sulfate and heparan sulfate
proteoglycans has opposite effects on PTPRS oligomerization and
regulation of neurite outgrowth. Contributes to the inhibition of
neurite and axonal outgrowth by chondroitin sulfate proteoglycans,
also after nerve transection. Plays a role in stimulating neurite
outgrowth in response to the heparan sulfate proteoglycan GPC2.
Required for normal brain development, especially for normal
development of the pituitary gland and the olfactory bulb (By
similarity). Functions as tyrosine phosphatase (PubMed:8068021).
Mediates dephosphorylation of NTRK1, NTRK2 and NTRK3 (By
similarity). Plays a role in down-regulation of signaling cascades
that lead to the activation of Akt and MAP kinases. Down-regulates
TLR9-mediated activation of NF-kappa-B, as well as production of
TNF, interferon alpha and interferon beta (By similarity).
{ECO:0000250|UniProtKB:B0V2N1, ECO:0000250|UniProtKB:F1NWE3,
ECO:0000269|PubMed:8068021}.
-!- CATALYTIC ACTIVITY: Protein tyrosine phosphate + H(2)O = protein
tyrosine + phosphate. {ECO:0000255|PROSITE-ProRule:PRU10044,
ECO:0000269|PubMed:8068021}.
-!- SUBUNIT: Binding to large heparan sulfate proteoglycan structures
promotes oligomerization. Binding to chondroitin sulfate
proteoglycan does not lead to oligomerization (By similarity).
Interacts (via Ig-like domains) with NTRK1 and NTRK3, but does not
form detectable complexes with NTRK2 (PubMed:17967490). Interacts
with PPFIA1, PPFIA2 and PPFIA3 (By similarity).
{ECO:0000250|UniProtKB:B0V2N1, ECO:0000250|UniProtKB:Q13332,
ECO:0000269|PubMed:17967490}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22519304};
Single-pass type I membrane protein
{ECO:0000250|UniProtKB:B0V2N1}. Cell projection, axon
{ECO:0000250|UniProtKB:B0V2N1}. Perikaryon
{ECO:0000250|UniProtKB:B0V2N1}. Cytoplasmic vesicle, secretory
vesicle, synaptic vesicle membrane {ECO:0000269|PubMed:22519304}.
Cell junction, synapse, synaptosome {ECO:0000269|PubMed:22519304}.
Cell junction, synapse, postsynaptic cell membrane, postsynaptic
density {ECO:0000269|PubMed:22519304}. Note=Is rapidly
internalized when dendritic cells are stimulated with the TLR9
ligand cytidine-phosphate-guanosine (CpG). Detected in a punctate
pattern along neurites and axon growth cones.
{ECO:0000250|UniProtKB:B0V2N1}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q64605-1; Sequence=Displayed;
Name=2;
IsoId=Q64605-2; Sequence=VSP_026932;
-!- TISSUE SPECIFICITY: Detected in brain neocortex (at protein level)
(PubMed:22519304). Detected in heart, testis and liver
(PubMed:8068021). Detected at lower levels in skeletal muscle,
brain, spleen and kidney (PubMed:8068021).
{ECO:0000269|PubMed:22519304, ECO:0000269|PubMed:8068021}.
-!- PTM: A cleavage occurs, separating the extracellular domain from
the transmembrane segment. This process called 'ectodomain
shedding' is thought to be involved in receptor desensitization,
signal transduction and/or membrane localization (By similarity).
{ECO:0000250}.
-!- SIMILARITY: Belongs to the protein-tyrosine phosphatase family.
Receptor class 2A subfamily. {ECO:0000305}.
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EMBL; L11587; AAC37656.1; -; mRNA.
EMBL; BC105753; AAI05754.1; -; mRNA.
PIR; I58148; I58148.
PIR; S46217; S46217.
RefSeq; NP_062013.1; NM_019140.2.
UniGene; Rn.91202; -.
PDB; 2NV5; X-ray; 2.00 A; A/B/C=1328-1614.
PDBsum; 2NV5; -.
ProteinModelPortal; Q64605; -.
SMR; Q64605; -.
STRING; 10116.ENSRNOP00000065227; -.
iPTMnet; Q64605; -.
PhosphoSitePlus; Q64605; -.
PaxDb; Q64605; -.
PRIDE; Q64605; -.
GeneID; 25529; -.
KEGG; rno:25529; -.
CTD; 5802; -.
RGD; 3452; Ptprs.
eggNOG; KOG4228; Eukaryota.
eggNOG; COG5599; LUCA.
HOVERGEN; HBG053758; -.
InParanoid; Q64605; -.
KO; K06778; -.
PhylomeDB; Q64605; -.
EvolutionaryTrace; Q64605; -.
PRO; PR:Q64605; -.
Proteomes; UP000002494; Unplaced.
GO; GO:0030424; C:axon; ISS:UniProtKB.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0070062; C:extracellular exosome; ISO:RGD.
GO; GO:0099061; C:integral component of postsynaptic density membrane; IDA:UniProtKB.
GO; GO:0030285; C:integral component of synaptic vesicle membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IEA:UniProtKB-SubCell.
GO; GO:0005886; C:plasma membrane; ISO:RGD.
GO; GO:0035374; F:chondroitin sulfate binding; ISS:UniProtKB.
GO; GO:0043395; F:heparan sulfate proteoglycan binding; ISS:UniProtKB.
GO; GO:0008201; F:heparin binding; ISS:UniProtKB.
GO; GO:0004721; F:phosphoprotein phosphatase activity; ISO:RGD.
GO; GO:0004725; F:protein tyrosine phosphatase activity; IDA:RGD.
GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
GO; GO:0021549; P:cerebellum development; ISO:RGD.
GO; GO:0021987; P:cerebral cortex development; ISO:RGD.
GO; GO:0022038; P:corpus callosum development; ISO:RGD.
GO; GO:0090557; P:establishment of endothelial intestinal barrier; ISO:RGD.
GO; GO:0021766; P:hippocampus development; ISO:RGD.
GO; GO:0030517; P:negative regulation of axon extension; ISS:UniProtKB.
GO; GO:0048681; P:negative regulation of axon regeneration; ISS:UniProtKB.
GO; GO:0048671; P:negative regulation of collateral sprouting; ISS:UniProtKB.
GO; GO:0061000; P:negative regulation of dendritic spine development; ISS:UniProtKB.
GO; GO:0032687; P:negative regulation of interferon-alpha production; ISO:RGD.
GO; GO:0032688; P:negative regulation of interferon-beta production; ISO:RGD.
GO; GO:0010977; P:negative regulation of neuron projection development; ISS:UniProtKB.
GO; GO:0034164; P:negative regulation of toll-like receptor 9 signaling pathway; ISO:RGD.
GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; ISO:RGD.
GO; GO:0006470; P:protein dephosphorylation; ISO:RGD.
GO; GO:0021510; P:spinal cord development; ISO:RGD.
CDD; cd00063; FN3; 8.
Gene3D; 2.60.40.10; -; 11.
Gene3D; 3.90.190.10; -; 2.
InterPro; IPR003961; FN3_dom.
InterPro; IPR036116; FN3_sf.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR013098; Ig_I-set.
InterPro; IPR003599; Ig_sub.
InterPro; IPR003598; Ig_sub2.
InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
InterPro; IPR000242; PTPase_domain.
InterPro; IPR016130; Tyr_Pase_AS.
InterPro; IPR003595; Tyr_Pase_cat.
InterPro; IPR000387; TYR_PHOSPHATASE_dom.
Pfam; PF00041; fn3; 6.
Pfam; PF07679; I-set; 3.
Pfam; PF00102; Y_phosphatase; 2.
PRINTS; PR00700; PRTYPHPHTASE.
SMART; SM00060; FN3; 8.
SMART; SM00409; IG; 3.
SMART; SM00408; IGc2; 3.
SMART; SM00194; PTPc; 2.
SMART; SM00404; PTPc_motif; 2.
SUPFAM; SSF48726; SSF48726; 3.
SUPFAM; SSF49265; SSF49265; 5.
SUPFAM; SSF52799; SSF52799; 2.
PROSITE; PS50853; FN3; 8.
PROSITE; PS50835; IG_LIKE; 3.
PROSITE; PS00383; TYR_PHOSPHATASE_1; 2.
PROSITE; PS50056; TYR_PHOSPHATASE_2; 2.
PROSITE; PS50055; TYR_PHOSPHATASE_PTP; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell adhesion; Cell junction;
Cell membrane; Cell projection; Complete proteome;
Cytoplasmic vesicle; Disulfide bond; Glycoprotein; Heparin-binding;
Hydrolase; Immunoglobulin domain; Membrane;
Postsynaptic cell membrane; Protein phosphatase; Receptor;
Reference proteome; Repeat; Signal; Synapse; Synaptosome;
Transmembrane; Transmembrane helix.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 1907 Receptor-type tyrosine-protein
phosphatase S.
/FTId=PRO_5000142153.
TOPO_DOM 30 1257 Extracellular. {ECO:0000255}.
TRANSMEM 1258 1278 Helical. {ECO:0000255}.
TOPO_DOM 1279 1907 Cytoplasmic. {ECO:0000255}.
DOMAIN 33 123 Ig-like C2-type 1.
DOMAIN 135 224 Ig-like C2-type 2.
DOMAIN 232 314 Ig-like C2-type 3.
DOMAIN 321 411 Fibronectin type-III 1.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 416 510 Fibronectin type-III 2.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 514 603 Fibronectin type-III 3.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 608 705 Fibronectin type-III 4.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 710 809 Fibronectin type-III 5.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 810 906 Fibronectin type-III 6.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 907 1008 Fibronectin type-III 7.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1011 1095 Fibronectin type-III 8.
{ECO:0000255|PROSITE-ProRule:PRU00316}.
DOMAIN 1352 1607 Tyrosine-protein phosphatase 1.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
DOMAIN 1639 1898 Tyrosine-protein phosphatase 2.
{ECO:0000255|PROSITE-ProRule:PRU00160}.
REGION 68 72 Important for binding to
glycosaminoglycan chains.
{ECO:0000250|UniProtKB:B0V2N1}.
REGION 1548 1554 Substrate binding. {ECO:0000250}.
ACT_SITE 1548 1548 Phosphocysteine intermediate.
{ECO:0000250}.
ACT_SITE 1839 1839 Phosphocysteine intermediate.
{ECO:0000250}.
BINDING 1516 1516 Substrate. {ECO:0000250}.
BINDING 1592 1592 Substrate. {ECO:0000250}.
SITE 1172 1173 Cleavage. {ECO:0000250}.
CARBOHYD 250 250 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 295 295 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 720 720 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 916 916 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 54 107 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 156 207 {ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 253 298 {ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 624 668 VSWRPPPPETHNGALVGYSVRYRPLGSEDPDPKEVNNIPPT
TTQI -> I (in isoform 2).
{ECO:0000303|PubMed:8068021}.
/FTId=VSP_026932.
CONFLICT 597 597 R -> C (in Ref. 1; AAC37656).
{ECO:0000305}.
CONFLICT 753 753 A -> T (in Ref. 1; AAC37656).
{ECO:0000305}.
CONFLICT 913 913 A -> P (in Ref. 1; AAC37656).
{ECO:0000305}.
CONFLICT 934 934 R -> G (in Ref. 1; AAC37656).
{ECO:0000305}.
CONFLICT 950 950 A -> T (in Ref. 1; AAC37656).
{ECO:0000305}.
HELIX 1334 1336 {ECO:0000244|PDB:2NV5}.
HELIX 1337 1358 {ECO:0000244|PDB:2NV5}.
HELIX 1369 1371 {ECO:0000244|PDB:2NV5}.
TURN 1373 1375 {ECO:0000244|PDB:2NV5}.
HELIX 1376 1378 {ECO:0000244|PDB:2NV5}.
HELIX 1388 1390 {ECO:0000244|PDB:2NV5}.
STRAND 1391 1393 {ECO:0000244|PDB:2NV5}.
TURN 1401 1404 {ECO:0000244|PDB:2NV5}.
STRAND 1405 1413 {ECO:0000244|PDB:2NV5}.
STRAND 1416 1423 {ECO:0000244|PDB:2NV5}.
HELIX 1428 1430 {ECO:0000244|PDB:2NV5}.
HELIX 1431 1440 {ECO:0000244|PDB:2NV5}.
STRAND 1445 1448 {ECO:0000244|PDB:2NV5}.
STRAND 1452 1454 {ECO:0000244|PDB:2NV5}.
STRAND 1457 1460 {ECO:0000244|PDB:2NV5}.
STRAND 1466 1472 {ECO:0000244|PDB:2NV5}.
STRAND 1475 1484 {ECO:0000244|PDB:2NV5}.
STRAND 1486 1497 {ECO:0000244|PDB:2NV5}.
STRAND 1504 1511 {ECO:0000244|PDB:2NV5}.
STRAND 1516 1519 {ECO:0000244|PDB:2NV5}.
HELIX 1524 1536 {ECO:0000244|PDB:2NV5}.
STRAND 1544 1553 {ECO:0000244|PDB:2NV5}.
HELIX 1554 1571 {ECO:0000244|PDB:2NV5}.
STRAND 1572 1574 {ECO:0000244|PDB:2NV5}.
HELIX 1576 1584 {ECO:0000244|PDB:2NV5}.
HELIX 1594 1608 {ECO:0000244|PDB:2NV5}.
SEQUENCE 1907 AA; 211931 MW; 5CD377A88377CDA4 CRC64;
MAPTWRPSVV SVVGPVGLFL VLLARGCLAE EPPRFIREPK DQIGVSGGVA SFVCQATGDP
KPRVTWNKKG KKVNSQRFET IDFDESSGAV LRIQPLRTPR DENVYECVAQ NSVGEITVHA
KLTVLREDQL PPGFPNIDMG PQLKVVERTR TATMLCAASG NPDPEITWFK DFLPVDPSAS
NGRIKQLRSG ALQIESSEET DQGKYECVAT NSAGVRYSSP ANLYVRVRRV APRFSILPMS
HEIMPGGNVN ITCVAVGSPM PYVKWMQGAE DLTPEDDMPV GRNVLELTDV KDSANYTCVA
MSSLGVIEAV AQITVKSLPK APGTPVVTEN TATSITVTWD SGNPDPVSYY VIEYKSKSQD
GPYQIKEDIT TTRYSIGGLS PNSEYEIWVS AVNSIGQGPP SESVVTRTGE QAPASAPRNV
QARMLSATTM IVQWEEPVEP NGLIRGYRVY YTMEPEHPVG NWQKHNVDDS LLTTVGSLLE
DETYTVRVLA FTSVGDGPLS DPIQVKTQQG VPGQPMNLRA EAKSETSIGL SWSAPRQESV
IKYELLFREG DRGREVGRTF DPTTAFVVED LKPNTEYAFR LAARSPQGLG AFTAVVRQRT
LQAKPSAPPQ DVKCTSLRST AILVSWRPPP PETHNGALVG YSVRYRPLGS EDPDPKEVNN
IPPTTTQILL EALEKWTEYR VTAVAYTEVG PGPESSPVVV RTDEDVPSAP PRKVEAEALN
ATAIRVLWRS PTPGRQHGQI RGYQVHYVRM EGAEARGPPR IKDIMLADAQ EMVITNLQPE
TAYSITVAAY TMKGDGARSK PKVVVTKGAV LGRPTLSVQQ TPEGSLLARW EPPADAAEDP
VLGYRLQFGR EDAAPATLEL AAWERRFAAP AHKGATYVFR LAARGRAGLG EEASAALSIP
EDAPRGFPQI LGAAGNVSAG SVILRWLPPV PAERNGAIIK YTVSVREAGA PGPATETELA
AAAQPGAETA LTLQGLRPET AYELRVRAHT RRGPGPFSPP LRYRLARDPV SPKNFKVKMI
MKTSVLLSWE FPDNYNSPTP YKIQYNGLTL DVDGRTTKKL ITHLKPHTFY NFVLTNRGSS
LGGLQQTVTA RTAFNMLSGK PSVAPKPDND GSIVVYLPDG QSPVTVQNYF IVMVPLRKSR
GGQFPILLGS PEDMDLEELI QDLSRLQRRS LRHSRQLEVP RPYIAARFSI LPAVFHPGNQ
KQYGGFDNRG LEPGHRYVLF VLAVLQKNEP TFAASPFSDP FQLDNPDPQP IVDGEEGLIW
VIGPVLAVVF IICIVIAILL YKNKPDSKRK DSEPRTKCLL NNADLAPHHP KDPVEMRRIN
FQTPGMLSHP PIPITDMAEH MERLKANDSL KLSQEYESID PGQQFTWEHS NLEANKPKNR
YANVIAYDHS RVILQPLEGI MGSDYINANY VDGYRRQNAY IATQGPLPET FGDFWRMVWE
QRSATVVMMT RLEEKSRVKC DQYWPNRGTE TYGFIQVTLL DTMELATFCV RTFSLHKNGS
SEKREVRHFQ FTAWPDHGVP EYPTPFLAFL RRVKTCNPPD AGPVVVHCSA GVGRTGCFIV
IDAMLERIRT EKTVDVYGHV TLMRSQRNYM VQTEDQYSFI HEALLEAVGC GNTEVPARSL
YTYIQKLAQV EPGEHVTGME LEFKRLASSK AHTSRFITAS LPCNKFKNRL VNILPYESSR
VCLQPIRGVE GSDYINASFI DGYRQQKAYI ATQGPLAETT EDFWRALWEN NSTIVVMLTK
LREMGREKCH QYWPAERSAR YQYFVVDPMA EYNMPQYILR EFKVTDARDG QSRTVRQFQF
TDWPEQGAPK SGEGFIDFIG QVHKTKEQFG QDGPISVHCS AGVGRTGVFI TLSIVLERMR
YEGVVDIFQT VKVLRTQRPA MVQTEDEYQF CFQAALEYLG SFDHYAT


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EIAAB33049 Neural-specific protein-tyrosine phosphatase,Ptpn5,Rat,Rattus norvegicus,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
EIAAB33048 Mouse,Mus musculus,Neural-specific protein-tyrosine phosphatase,Ptpn5,STEP,Striatum-enriched protein-tyrosine phosphatase,Tyrosine-protein phosphatase non-receptor type 5
10-782-55090 Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase 2C; PTP-2C; PTP-1D; SH-PTP3; SH-PTP2; SHP-2; Shp2 N_A 0.02 mg
10-782-55090 Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase 2C; PTP-2C; PTP-1D; SH-PTP3; SH-PTP2; SHP-2; Shp2 N_A 0.01 mg
10-782-55090 Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase 2C; PTP-2C; PTP-1D; SH-PTP3; SH-PTP2; SHP-2; Shp2 N_A 0.001 mg
10-782-55090 Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase 2C; PTP-2C; PTP-1D; SH-PTP3; SH-PTP2; SHP-2; Shp2 N_A 0.005 mg
15-288-21495A Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase SYP; SH-PTP2; SHP-2; Shp2 Polyclonal 0.1 mg
15-288-21495A Tyrosine-protein phosphatase non-receptor type 11 - EC 3.1.3.48; Protein-tyrosine phosphatase SYP; SH-PTP2; SHP-2; Shp2 Polyclonal 0.05 mg


 

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