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Sodium channel protein type 10 subunit alpha (Peripheral nerve sodium channel 3) (PN3) (Sensory neuron sodium channel) (Sodium channel protein type X subunit alpha) (Voltage-gated sodium channel subunit alpha Nav1.8)

 SCNAA_RAT               Reviewed;        1956 AA.
Q62968; Q63554; Q6EWG6;
21-DEC-2004, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
18-JUL-2018, entry version 140.
RecName: Full=Sodium channel protein type 10 subunit alpha;
AltName: Full=Peripheral nerve sodium channel 3;
Short=PN3;
AltName: Full=Sensory neuron sodium channel;
AltName: Full=Sodium channel protein type X subunit alpha;
AltName: Full=Voltage-gated sodium channel subunit alpha Nav1.8;
Name=Scn10a; Synonyms=Sns;
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 1), TISSUE SPECIFICITY, AND
FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
TISSUE=Spinal ganglion;
PubMed=8538791; DOI=10.1038/379257a0;
Akopian A.N., Sivilotti L., Wood J.N.;
"A tetrodotoxin-resistant voltage-gated sodium channel expressed by
sensory neurons.";
Nature 379:257-262(1996).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
FUNCTION IN VOLTAGE-EVOKED DEPOLARIZATION.
STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
PubMed=8626372; DOI=10.1074/jbc.271.11.5953;
Sangameswaran L., Delgado S.G., Fish L.M., Koch B.D., Jakeman L.B.,
Stewart G.R., Sze P., Hunter J.C., Eglen R.M., Herman R.C.;
"Structure and function of a novel voltage-gated, tetrodotoxin-
resistant sodium channel specific to sensory neurons.";
J. Biol. Chem. 271:5953-5956(1996).
[3]
NUCLEOTIDE SEQUENCE (ISOFORM 1), AND INTERACTION WITH SCN1B; SCN2B AND
SCN3B.
STRAIN=Sprague-Dawley; TISSUE=Spinal ganglion;
PubMed=15178439; DOI=10.1016/j.bbrc.2004.05.026;
Vijayaragavan K., Powell A.J., Kinghorn I.J., Chahine M.;
"Role of auxiliary beta1-, beta2-, and beta3-subunits and their
interaction with Na(v)1.8 voltage-gated sodium channel.";
Biochem. Biophys. Res. Commun. 319:531-540(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 963-1097 (ISOFORMS 1 AND 2).
STRAIN=Wistar; TISSUE=Spinal ganglion, and Trigeminal ganglion;
PubMed=15047701; DOI=10.1074/jbc.M401281200;
Kerr N.C.H., Holmes F.E., Wynick D.;
"Novel isoforms of the sodium channels Nav1.8 and Nav1.5 are produced
by a conserved mechanism in mouse and rat.";
J. Biol. Chem. 279:24826-24833(2004).
[5]
INDUCTION.
PubMed=9450690; DOI=10.1016/S0169-328X(97)00239-8;
Oaklander A.L., Belzberg A.J.;
"Unilateral nerve injury down-regulates mRNA for Na+ channel SCN10A
bilaterally in rat dorsal root ganglia.";
Brain Res. Mol. Brain Res. 52:162-165(1997).
[6]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=11487631;
Benn S.C., Costigan M., Tate S., Fitzgerald M., Woolf C.J.;
"Developmental expression of the TTX-resistant voltage-gated sodium
channels Nav1.8 (SNS) and Nav1.9 (SNS2) in primary sensory neurons.";
J. Neurosci. 21:6077-6085(2001).
[7]
SUBCELLULAR LOCATION, AND INTERACTION WITH S100A10.
PubMed=12050667; DOI=10.1038/nature00781;
Okuse K., Malik-Hall M., Baker M.D., Poon W.-Y.L., Kong H., Chao M.V.,
Wood J.N.;
"Annexin II light chain regulates sensory neuron-specific sodium
channel expression.";
Nature 417:653-656(2002).
[8]
INTERACTION WITH FSTL1; PRX; DYNLT1 AND PDZD2, AND IDENTIFICATION IN
COMPLEXES WITH PRX; DYNLT1 AND PDZD2.
PubMed=12591166; DOI=10.1016/S0169-328X(02)00661-7;
Malik-Hall M., Poon W.-Y.L., Baker M.D., Wood J.N., Okuse K.;
"Sensory neuron proteins interact with the intracellular domains of
sodium channel NaV1.8.";
Brain Res. Mol. Brain Res. 110:298-304(2003).
[9]
FUNCTION IN PAIN.
PubMed=12514212;
Gold M.S., Weinreich D., Kim C.-S., Wang R., Treanor J., Porreca F.,
Lai J.;
"Redistribution of Na(V)1.8 in uninjured axons enables neuropathic
pain.";
J. Neurosci. 23:158-166(2003).
-!- FUNCTION: Tetrodotoxin-resistant channel that mediates the
voltage-dependent sodium ion permeability of excitable membranes.
Assuming opened or closed conformations in response to the voltage
difference across the membrane, the protein forms a sodium-
selective channel through which sodium ions may pass in accordance
with their electrochemical gradient. Plays a role in neuropathic
pain mechanisms. {ECO:0000269|PubMed:12514212,
ECO:0000269|PubMed:8538791, ECO:0000269|PubMed:8626372}.
-!- SUBUNIT: The channel consists of an ion conducting pore forming
alpha-subunit regulated by one or more associated auxiliary
subunits SCN1B, SCN2B and SCN3B; electrophysiological properties
may vary depending on the type of the associated beta subunits.
Found in a number of complexes with PRX, DYNLT1 and PDZD2.
Interacts with proteins such as FSTL1, PRX, DYNLT1, PDZD2, S100A10
and many others. Interacts with NEDD4 and NEDD4L.
{ECO:0000269|PubMed:12050667, ECO:0000269|PubMed:12591166,
ECO:0000269|PubMed:15178439}.
-!- INTERACTION:
Q9Z336:Dynlt1; NbExp=2; IntAct=EBI-1800320, EBI-920359;
Q63425:Prx; NbExp=2; IntAct=EBI-1800320, EBI-1800492;
P05943:S100a10; NbExp=4; IntAct=EBI-1800320, EBI-1800351;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:D0E0C2}; Multi-pass membrane protein
{ECO:0000250|UniProtKB:D0E0C2}. Note=It can be translocated to the
cell membrane through association with S100A10.
{ECO:0000269|PubMed:12050667}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q62968-1; Sequence=Displayed;
Name=2; Synonyms=Nav1.8c;
IsoId=Q62968-2; Sequence=VSP_012258;
-!- TISSUE SPECIFICITY: Expressed in dorsal root ganglia, trigeminal
ganglia, nodose ganglia and sciatic nerve.
{ECO:0000269|PubMed:11487631, ECO:0000269|PubMed:8538791,
ECO:0000269|PubMed:8626372}.
-!- DEVELOPMENTAL STAGE: Expressed in dorsal root ganglia at 15 dpc
onwards. {ECO:0000269|PubMed:11487631}.
-!- INDUCTION: Down-regulated after axotomy in dorsal root ganglia.
{ECO:0000269|PubMed:9450690}.
-!- DOMAIN: The sequence contains 4 internal repeats, each with 5
hydrophobic segments (S1, S2, S3, S5, S6) and one positively
charged segment (S4). Segments S4 are probably the voltage-sensors
and are characterized by a series of positively charged amino
acids at every third position. {ECO:0000305}.
-!- PTM: Ubiquitinated by NEDD4L; which promotes its endocytosis.
{ECO:0000250}.
-!- PTM: Phosphorylation at Ser-1452 by PKC in a highly conserved
cytoplasmic loop slows inactivation of the sodium channel and
reduces peak sodium currents. {ECO:0000250}.
-!- PTM: Lacks the cysteine which covalently binds the conotoxin
GVIIJ. This cysteine (position 815) is speculated in other sodium
channel subunits alpha to be implied in covalent binding with the
sodium channel subunit beta-2 or beta-4.
{ECO:0000250|UniProtKB:P15389}.
-!- SIMILARITY: Belongs to the sodium channel (TC 1.A.1.10) family.
Nav1.8/SCN10A subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; X92184; CAA63095.1; -; mRNA.
EMBL; U53833; AAC52619.1; -; Genomic_DNA.
EMBL; AJ623271; CAF25041.1; -; mRNA.
PIR; S68453; S68453.
RefSeq; NP_058943.1; NM_017247.1.
UniGene; Rn.10246; -.
ProteinModelPortal; Q62968; -.
CORUM; Q62968; -.
ELM; Q62968; -.
IntAct; Q62968; 23.
STRING; 10116.ENSRNOP00000047944; -.
BindingDB; Q62968; -.
ChEMBL; CHEMBL4017; -.
GuidetoPHARMACOLOGY; 585; -.
TCDB; 1.A.1.10.6; the voltage-gated ion channel (vic) superfamily.
iPTMnet; Q62968; -.
PhosphoSitePlus; Q62968; -.
PaxDb; Q62968; -.
PRIDE; Q62968; -.
Ensembl; ENSRNOT00000046864; ENSRNOP00000047944; ENSRNOG00000032473. [Q62968-1]
GeneID; 29571; -.
KEGG; rno:29571; -.
UCSC; RGD:3629; rat. [Q62968-1]
CTD; 6336; -.
RGD; 3629; Scn10a.
eggNOG; KOG2301; Eukaryota.
eggNOG; ENOG410XNP6; LUCA.
GeneTree; ENSGT00830000128242; -.
HOGENOM; HOG000231755; -.
HOVERGEN; HBG053100; -.
InParanoid; Q62968; -.
KO; K04842; -.
OMA; WNIFDCI; -.
OrthoDB; EOG091G00FK; -.
PhylomeDB; Q62968; -.
TreeFam; TF323985; -.
Reactome; R-RNO-5576892; Phase 0 - rapid depolarisation.
PRO; PR:Q62968; -.
Proteomes; UP000002494; Chromosome 8.
Bgee; ENSRNOG00000032473; -.
Genevisible; Q62968; RN.
GO; GO:0071439; C:clathrin complex; IDA:RGD.
GO; GO:0016021; C:integral component of membrane; IDA:RGD.
GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
GO; GO:0001518; C:voltage-gated sodium channel complex; IEA:Ensembl.
GO; GO:0044325; F:ion channel binding; IEA:Ensembl.
GO; GO:0005244; F:voltage-gated ion channel activity; IEA:UniProtKB-KW.
GO; GO:0005248; F:voltage-gated sodium channel activity; IDA:RGD.
GO; GO:0086016; P:AV node cell action potential; IEA:Ensembl.
GO; GO:0086043; P:bundle of His cell action potential; IEA:Ensembl.
GO; GO:0086010; P:membrane depolarization during action potential; IBA:GO_Central.
GO; GO:0019228; P:neuronal action potential; IBA:GO_Central.
GO; GO:0042475; P:odontogenesis of dentin-containing tooth; IEP:RGD.
GO; GO:0060371; P:regulation of atrial cardiac muscle cell membrane depolarization; IEA:Ensembl.
GO; GO:0055117; P:regulation of cardiac muscle contraction; IEA:Ensembl.
GO; GO:0002027; P:regulation of heart rate; IEA:Ensembl.
GO; GO:0034765; P:regulation of ion transmembrane transport; IEA:UniProtKB-KW.
GO; GO:0019233; P:sensory perception of pain; IMP:RGD.
GO; GO:0006814; P:sodium ion transport; IDA:RGD.
Gene3D; 1.20.120.350; -; 4.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR028809; Na_channel_a10su.
InterPro; IPR001696; Na_channel_asu.
InterPro; IPR010526; Na_trans_assoc.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR10037:SF208; PTHR10037:SF208; 1.
Pfam; PF00520; Ion_trans; 4.
Pfam; PF06512; Na_trans_assoc; 1.
PRINTS; PR00170; NACHANNEL.
1: Evidence at protein level;
Alternative splicing; Cell membrane; Complete proteome;
Disulfide bond; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Reference proteome; Repeat; Sodium; Sodium channel;
Sodium transport; Transmembrane; Transmembrane helix; Transport;
Ubl conjugation; Voltage-gated channel.
CHAIN 1 1956 Sodium channel protein type 10 subunit
alpha.
/FTId=PRO_0000048509.
TOPO_DOM 1 125 Cytoplasmic. {ECO:0000305}.
TRANSMEM 126 149 Helical; Name=S1 of repeat I.
{ECO:0000255}.
TOPO_DOM 150 154 Extracellular. {ECO:0000305}.
TRANSMEM 155 174 Helical; Name=S2 of repeat I.
{ECO:0000255}.
TOPO_DOM 175 187 Cytoplasmic. {ECO:0000305}.
TRANSMEM 188 206 Helical; Name=S3 of repeat I.
{ECO:0000255}.
TOPO_DOM 207 212 Extracellular. {ECO:0000305}.
TRANSMEM 213 232 Helical; Voltage-sensor; Name=S4 of
repeat I. {ECO:0000255}.
TOPO_DOM 233 248 Cytoplasmic. {ECO:0000305}.
TRANSMEM 249 272 Helical; Name=S5 of repeat I.
{ECO:0000255}.
TOPO_DOM 273 340 Extracellular. {ECO:0000305}.
INTRAMEM 341 365 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 366 372 Extracellular. {ECO:0000305}.
TRANSMEM 373 398 Helical; Name=S6 of repeat I.
{ECO:0000255}.
TOPO_DOM 399 658 Cytoplasmic. {ECO:0000305}.
TRANSMEM 659 683 Helical; Name=S1 of repeat II.
{ECO:0000255}.
TOPO_DOM 684 694 Extracellular. {ECO:0000305}.
TRANSMEM 695 718 Helical; Name=S2 of repeat II.
{ECO:0000255}.
TOPO_DOM 719 726 Cytoplasmic. {ECO:0000305}.
TRANSMEM 727 746 Helical; Name=S3 of repeat II.
{ECO:0000255}.
TOPO_DOM 747 752 Extracellular. {ECO:0000305}.
TRANSMEM 753 772 Helical; Voltage-sensor; Name=S4 of
repeat II. {ECO:0000255}.
TOPO_DOM 773 788 Cytoplasmic. {ECO:0000305}.
TRANSMEM 789 809 Helical; Name=S5 of repeat II.
{ECO:0000255}.
TOPO_DOM 810 833 Extracellular. {ECO:0000305}.
INTRAMEM 834 854 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 855 863 Extracellular. {ECO:0000305}.
TRANSMEM 864 889 Helical; Name=S6 of repeat II.
{ECO:0000255}.
TOPO_DOM 890 1148 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1149 1172 Helical; Name=S1 of repeat III.
{ECO:0000255}.
TOPO_DOM 1173 1185 Extracellular. {ECO:0000305}.
TRANSMEM 1186 1211 Helical; Name=S2 of repeat III.
{ECO:0000255}.
TOPO_DOM 1212 1217 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1218 1239 Helical; Name=S3 of repeat III.
{ECO:0000255}.
TOPO_DOM 1240 1243 Extracellular. {ECO:0000305}.
TRANSMEM 1244 1265 Helical; Voltage-sensor; Name=S4 of
repeat III. {ECO:0000255}.
TOPO_DOM 1266 1284 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1285 1312 Helical; Name=S5 of repeat III.
{ECO:0000255}.
TOPO_DOM 1313 1354 Extracellular. {ECO:0000305}.
INTRAMEM 1355 1376 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1377 1392 Extracellular. {ECO:0000305}.
TRANSMEM 1393 1419 Helical; Name=S6 of repeat III.
{ECO:0000255}.
TOPO_DOM 1420 1472 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1473 1496 Helical; Name=S1 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1497 1507 Extracellular. {ECO:0000305}.
TRANSMEM 1508 1531 Helical; Name=S2 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1532 1537 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1538 1561 Helical; Name=S3 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1562 1573 Extracellular. {ECO:0000305}.
TRANSMEM 1574 1595 Helical; Voltage-sensor; Name=S4 of
repeat IV. {ECO:0000255}.
TOPO_DOM 1596 1610 Cytoplasmic. {ECO:0000305}.
TRANSMEM 1611 1633 Helical; Name=S5 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1634 1647 Extracellular. {ECO:0000305}.
INTRAMEM 1648 1670 Pore-forming.
{ECO:0000250|UniProtKB:D0E0C2}.
TOPO_DOM 1671 1698 Extracellular. {ECO:0000305}.
TRANSMEM 1699 1723 Helical; Name=S6 of repeat IV.
{ECO:0000255}.
TOPO_DOM 1724 1956 Cytoplasmic. {ECO:0000305}.
REPEAT 116 404 I. {ECO:0000305}.
REPEAT 646 910 II. {ECO:0000305}.
REPEAT 1141 1450 III. {ECO:0000305}.
REPEAT 1459 1758 IV. {ECO:0000305}.
DOMAIN 1852 1881 IQ.
MOD_RES 440 440 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 443 443 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 466 466 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 478 478 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 611 611 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 614 614 Phosphoserine.
{ECO:0000250|UniProtKB:Q14524}.
MOD_RES 1452 1452 Phosphoserine; by PKC.
{ECO:0000250|UniProtKB:Q14524}.
CARBOHYD 279 279 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 288 288 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 311 311 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 334 334 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1323 1323 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1329 1329 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1337 1337 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 1687 1687 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 276 318 {ECO:0000250|UniProtKB:D0E0C2}.
DISULFID 856 865 {ECO:0000250|UniProtKB:D0E0C2}.
VAR_SEQ 1030 1030 Missing (in isoform 2).
{ECO:0000303|PubMed:15047701}.
/FTId=VSP_012258.
CONFLICT 59 59 A -> D (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 432 432 A -> E (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 520 520 T -> TP (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 587 587 D -> H (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 757 757 F -> L (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 938 938 R -> H (in Ref. 1; CAA63095).
{ECO:0000305}.
CONFLICT 1896 1896 V -> I (in Ref. 1; CAA63095).
{ECO:0000305}.
SEQUENCE 1956 AA; 219733 MW; 8FC58EDAD263AC67 CRC64;
MELPFASVGT TNFRRFTPES LAEIEKQIAA HRAAKKARTK HRGQEDKGEK PRPQLDLKAC
NQLPKFYGEL PAELVGEPLE DLDPFYSTHR TFMVLNKSRT ISRFSATWAL WLFSPFNLIR
RTAIKVSVHS WFSIFITITI LVNCVCMTRT DLPEKVEYVF TVIYTFEALI KILARGFCLN
EFTYLRDPWN WLDFSVITLA YVGAAIDLRG ISGLRTFRVL RALKTVSVIP GLKVIVGALI
HSVRKLADVT ILTVFCLSVF ALVGLQLFKG NLKNKCIRNG TDPHKADNLS SEMAEYIFIK
PGTTDPLLCG NGSDAGHCPG GYVCLKTPDN PDFNYTSFDS FAWAFLSLFR LMTQDSWERL
YQQTLRASGK MYMVFFVLVI FLGSFYLVNL ILAVVTMAYE EQSQATIAEI EAKEKKFQEA
LEVLQKEQEV LAALGIDTTS LQSHSGSPLA SKNANERRPR VKSRVSEGST DDNRSPQSDP
YNQRRMSFLG LSSGRRRASH GSVFHFRAPS QDISFPDGIT DDGVFHGDQE SRRGSILLGR
GAGQTGPLPR SPLPQSPNPG RRHGEEGQLG VPTGELTAGA PEGPALDTTG QKSFLSAGYL
NEPFRAQRAM SVVSIMTSVI EELEESKLKC PPCLISFAQK YLIWECCPKW RKFKMALFEL
VTDPFAELTI TLCIVVNTVF MAMEHYPMTD AFDAMLQAGN IVFTVFFTME MAFKIIAFDP
YYYFQKKWNI FDCVIVTVSL LELSASKKGS LSVLRTFRLL RVFKLAKSWP TLNTLIKIIG
NSVGALGNLT FILAIIVFIF ALVGKQLLSE DYGCRKDGVS VWNGEKLRWH MCDFFHSFLV
VFRILCGEWI ENMWVCMEVS QKSICLILFL TVMVLGNLVV LNLFIALLLN SFSADNLTAP
EDDGEVNNLQ LALARIQVLG HRASRAIASY ISSHCRFRWP KVETQLGMKP PLTSSEAKNH
IATDAVSAAV GNLTKPALSS PKENHGDFIT DPNVWVSVPI AEGESDLDEL EEDMEQASQS
SWQEEDPKGQ QEQLPQVQKC ENHQAARSPA SMMSSEDLAP YLGESWKRKD SPQVPAEGVD
DTSSSEGSTV DCPDPEEILR KIPELADDLD EPDDCFTEGC TRRCPCCNVN TSKSPWATGW
QVRKTCYRIV EHSWFESFII FMILLSSGAL AFEDNYLEEK PRVKSVLEYT DRVFTFIFVF
EMLLKWVAYG FKKYFTNAWC WLDFLIVNIS LTSLIAKILE YSDVASIKAL RTLRALRPLR
ALSRFEGMRV VVDALVGAIP SIMNVLLVCL IFWLIFSIMG VNLFAGKFSK CVDTRNNPFS
NVNSTMVNNK SECHNQNSTG HFFWVNVKVN FDNVAMGYLA LLQVATFKGW MDIMYAAVDS
GEINSQPNWE NNLYMYLYFV VFIIFGGFFT LNLFVGVIID NFNQQKKKLG GQDIFMTEEQ
KKYYNAMKKL GSKKPQKPIP RPLNKYQGFV FDIVTRQAFD IIIMVLICLN MITMMVETDE
QGEEKTKVLG RINQFFVAVF TGECVMKMFA LRQYYFTNGW NVFDFIVVIL SIGSLLFSAI
LKSLENYFSP TLFRVIRLAR IGRILRLIRA AKGIRTLLFA LMMSLPALFN IGLLLFLVMF
IYSIFGMASF ANVVDEAGID DMFNFKTFGN SMLCLFQITT SAGWDGLLSP ILNTGPPYCD
PNLPNSNGSR GNCGSPAVGI IFFTTYIIIS FLIVVNMYIA VILENFNVAT EESTEPLSED
DFDMFYETWE KFDPEATQFI AFSALSDFAD TLSGPLRIPK PNQNILIQMD LPLVPGDKIH
CLDILFAFTK NVLGESGELD SLKTNMEEKF MATNLSKASY EPIATTLRWK QEDLSATVIQ
KAYRSYMLHR SLTLSNTLHV PRAEEDGVSL PGEGYVTFMA NSGLPDKSET ASATSFPPSY
DSVTRGLSDR ANINPSSSMQ NEDEVAAKEG NSPGPQ


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EIAAB37609 Peripheral sodium channel 1,PN1,Rat,Rattus norvegicus,Scn9a,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.7
EIAAB37608 NaCh6,Peripheral nerve protein type 4,PN4,Rat,Rattus norvegicus,Scn8a,Sodium channel 6,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium c
EIAAB37612 Kiaa4197,Mouse,Mus musculus,Peripheral sodium channel 1,PN1,Scn9a,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha Na
EIAAB37611 hNE-Na,Homo sapiens,Human,NENA,Neuroendocrine sodium channel,Peripheral sodium channel 1,PN1,SCN9A,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gate
EIAAB37610 Nas,Oryctolagus cuniculus,Rabbit,Schwann cell sodium channel,SCN9A,Sodium channel protein type 9 subunit alpha,Sodium channel protein type IX subunit alpha,Voltage-gated sodium channel subunit alpha N
EIAAB37596 Homo sapiens,Human,SCN4A,SkM1,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium channel
EIAAB37575 Homo sapiens,Human,NAC1,SCN1,SCN1A,Sodium channel protein brain I subunit alpha,Sodium channel protein type 1 subunit alpha,Sodium channel protein type I subunit alpha,Voltage-gated sodium channel sub
EIAAB37606 Homo sapiens,Human,MED,SCN8A,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.6
EIAAB37607 Mouse,Mus musculus,Nbna1,Scn8a,Sodium channel protein type 8 subunit alpha,Sodium channel protein type VIII subunit alpha,Voltage-gated sodium channel subunit alpha Nav1.6
EIAAB37595 Mouse,Mus musculus,Scn4a,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium channel subu
EIAAB37604 HH1,Homo sapiens,Human,SCN5A,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel su
EIAAB37605 Homo sapiens,Human,Putative voltage-gated sodium channel subunit alpha Nax,SCN6A,SCN7A,Sodium channel protein cardiac and skeletal muscle subunit alpha,Sodium channel protein type 7 subunit alpha,Sodi
EIAAB37589 Rat,Rattus norvegicus,Scn3a,Sodium channel protein brain III subunit alpha,Sodium channel protein type 3 subunit alpha,Sodium channel protein type III subunit alpha,Voltage-gated sodium channel subtyp
EIAAB37602 mH1,Mouse,Mus musculus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel su
EIAAB37603 Rat,Rattus norvegicus,Scn5a,Sodium channel protein cardiac muscle subunit alpha,Sodium channel protein type 5 subunit alpha,Sodium channel protein type V subunit alpha,Voltage-gated sodium channel sub
EIAAB37583 Rat,Rattus norvegicus,Scn2a,Scn2a1,Sodium channel protein brain II subunit alpha,Sodium channel protein type 2 subunit alpha,Sodium channel protein type II subunit alpha,Voltage-gated sodium channel s
EIAAB37590 Homo sapiens,Human,KIAA1356,NAC3,SCN3A,Sodium channel protein brain III subunit alpha,Sodium channel protein type 3 subunit alpha,Sodium channel protein type III subunit alpha,Voltage-gated sodium cha
EIAAB37576 Rat,Rattus norvegicus,Scn1a,Sodium channel protein brain I subunit alpha,Sodium channel protein type 1 subunit alpha,Sodium channel protein type I subunit alpha,Voltage-gated sodium channel subunit al
EIAAB37597 Mu-1,Rat,Rattus norvegicus,Scn4a,SkM1,Sodium channel protein skeletal muscle subunit alpha,Sodium channel protein type 4 subunit alpha,Sodium channel protein type IV subunit alpha,Voltage-gated sodium


 

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