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Sarcoplasmic/endoplasmic reticulum calcium ATPase 2 (SERCA2) (SR Ca(2 )-ATPase 2) (EC 3.6.3.8) (Calcium pump 2) (Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform) (Endoplasmic reticulum class 1/2 Ca(2 ) ATPase)

 AT2A2_MOUSE             Reviewed;        1044 AA.
O55143; Q9R2A9; Q9WUT5;
01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
01-DEC-2000, sequence version 2.
25-OCT-2017, entry version 180.
RecName: Full=Sarcoplasmic/endoplasmic reticulum calcium ATPase 2;
Short=SERCA2;
Short=SR Ca(2+)-ATPase 2;
EC=3.6.3.8;
AltName: Full=Calcium pump 2;
AltName: Full=Calcium-transporting ATPase sarcoplasmic reticulum type, slow twitch skeletal muscle isoform;
AltName: Full=Endoplasmic reticulum class 1/2 Ca(2+) ATPase;
Name=Atp2a2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1 AND 2).
STRAIN=129/SvJ, and NIH Swiss; TISSUE=Embryo;
PubMed=10656932; DOI=10.1007/s003350010030;
Ver Heyen M., Reed T.D., Blough R.E., Zilberman A.L., Loukianov E.,
Van Baelen K., Raeymaekers L., Periasamy M., Wutack F.;
"Structure and organization of the mouse Atp2a2 gene encoding the
sarco(endo)plasmic reticulum Ca(2+)-ATPase 2 (SERCA2) isoforms.";
Mamm. Genome 11:159-163(2000).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
STRAIN=C57BL/6J; TISSUE=Brain;
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]
PROTEIN SEQUENCE OF 604-611 AND 638-655, AND IDENTIFICATION BY MASS
SPECTROMETRY.
STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[4]
INTERACTION WITH TRAM2.
PubMed=14749390; DOI=10.1128/MCB.24.4.1758-1768.2004;
Stefanovic B., Stefanovic L., Schnabl B., Bataller R., Brenner D.A.;
"TRAM2 protein interacts with endoplasmic reticulum Ca2+ pump Serca2b
and is necessary for collagen type I synthesis.";
Mol. Cell. Biol. 24:1758-1768(2004).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[6]
INTERACTION WITH S100A8 AND S100A9.
PubMed=18403730; DOI=10.1161/CIRCRESAHA.107.167544;
Boyd J.H., Kan B., Roberts H., Wang Y., Walley K.R.;
"S100A8 and S100A9 mediate endotoxin-induced cardiomyocyte dysfunction
via the receptor for advanced glycation end products.";
Circ. Res. 102:1239-1246(2008).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-663, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38; SER-531 AND SER-663,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
FUNCTION, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
PubMed=22355118; DOI=10.1073/pnas.1120172109;
Swift F., Franzini-Armstrong C., Oeyehaug L., Enger U.H.,
Andersson K.B., Christensen G., Sejersted O.M., Louch W.E.;
"Extreme sarcoplasmic reticulum volume loss and compensatory T-tubule
remodeling after Serca2 knockout.";
Proc. Natl. Acad. Sci. U.S.A. 109:3997-4001(2012).
[10]
FUNCTION, INTERACTION WITH PLN, AND ENZYME REGULATION.
PubMed=22971924; DOI=10.1007/s10974-012-9319-4;
Ha K.N., Gustavsson M., Veglia G.;
"Tuning the structural coupling between the transmembrane and
cytoplasmic domains of phospholamban to control sarcoplasmic reticulum
Ca(2+)-ATPase (SERCA) function.";
J. Muscle Res. Cell Motil. 33:485-492(2012).
[11]
FUNCTION, INTERACTION WITH TMEM64 AND PDIA3, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=23395171; DOI=10.1016/j.cmet.2013.01.002;
Kim H., Kim T., Jeong B.C., Cho I.T., Han D., Takegahara N.,
Negishi-Koga T., Takayanagi H., Lee J.H., Sul J.Y., Prasad V.,
Lee S.H., Choi Y.;
"Tmem64 modulates calcium signaling during RANKL-mediated osteoclast
differentiation.";
Cell Metab. 17:249-260(2013).
-!- FUNCTION: This magnesium-dependent enzyme catalyzes the hydrolysis
of ATP coupled with the translocation of calcium from the cytosol
to the sarcoplasmic reticulum lumen. Isoform SERCA2A is involved
in the regulation of the contraction/relaxation cycle. Acts as a
regulator of TNFSF11-mediated Ca(2+) signaling pathways via its
interaction with TMEM64 which is critical for the TNFSF11-induced
CREB1 activation and mitochondrial ROS generation necessary for
proper osteoclast generation. Association between TMEM64 and
SERCA2 in the ER leads to cytosolic Ca (2+) spiking for activation
of NFATC1 and production of mitochondrial ROS, thereby triggering
Ca (2+) signaling cascades that promote osteoclast differentiation
and activation (PubMed:23395171). {ECO:0000269|PubMed:22355118,
ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:23395171}.
-!- CATALYTIC ACTIVITY: ATP + H(2)O + Ca(2+)(Side 1) = ADP + phosphate
+ Ca(2+)(Side 2).
-!- ENZYME REGULATION: Reversibly inhibited by phospholamban (PLN) at
low calcium concentrations (PubMed:22971924). Inhibited by
sarcolipin (SLN) and myoregulin (MRLN) (By similarity). Enhanced
by DWORF; DWORF increases activity by displacing sarcolipin (SLN),
phospholamban (PLN) and myoregulin (MRLN) (By similarity).
{ECO:0000250|UniProtKB:P04191, ECO:0000250|UniProtKB:Q8R429,
ECO:0000269|PubMed:22971924}.
-!- SUBUNIT: Interacts with sarcolipin (SLN) (By similarity).
Interacts with phospholamban (PLN) (PubMed:22971924). Interacts
with myoregulin (MRLN) (By similarity). Interacts with DWORF (By
similarity). Isoform 1 interacts with TRAM2 (via C-terminus)
(PubMed:14749390). Interacts with HAX1. Interacts with S100A8 and
S100A9 (PubMed:18403730). Interacts with SLC35G1 and STIM1.
Interacts with TMEM203 (By similarity). Interacts with TMEM64 and
PDIA3 (PubMed:23395171). {ECO:0000250|UniProtKB:P04191,
ECO:0000250|UniProtKB:P16615, ECO:0000250|UniProtKB:Q8R429,
ECO:0000269|PubMed:14749390, ECO:0000269|PubMed:18403730,
ECO:0000269|PubMed:22971924, ECO:0000269|PubMed:23395171}.
-!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
{ECO:0000269|PubMed:23395171}; Multi-pass membrane protein
{ECO:0000255}. Sarcoplasmic reticulum membrane
{ECO:0000269|PubMed:22355118}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=Atp2a2b, SERCA2b;
IsoId=O55143-1; Sequence=Displayed;
Name=2; Synonyms=Atp2a2a, SERCA2a;
IsoId=O55143-2; Sequence=VSP_000359;
-!- TISSUE SPECIFICITY: Isoform 2 is highly expressed in heart and
slow twitch skeletal muscle. Isoform 2 is widely expressed.
-!- INDUCTION: Highly up-regulated during osteoclast differentiation.
{ECO:0000269|PubMed:23395171}.
-!- PTM: Nitrated under oxidative stress. Nitration on the two
tyrosine residues inhibits catalytic activity.
{ECO:0000250|UniProtKB:P16615}.
-!- DISRUPTION PHENOTYPE: Sarcoplasmic reticulum collapse and volume
reduction. Although dimensions of cardiomyocyte are not affected,
total surface area is significantly increased, resulting in
increased T-tubule density. {ECO:0000269|PubMed:22355118}.
-!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC
3.A.3) family. Type IIA subfamily. {ECO:0000305}.
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EMBL; AJ131821; CAB72436.1; -; mRNA.
EMBL; AJ223584; CAA11450.1; -; mRNA.
EMBL; AF029982; AAD01889.1; -; Genomic_DNA.
EMBL; AJ131870; CAB41017.1; -; Genomic_DNA.
EMBL; AJ131870; CAB41018.1; -; Genomic_DNA.
EMBL; BC054531; AAH54531.1; -; mRNA.
EMBL; BC054748; AAH54748.1; -; mRNA.
CCDS; CCDS57378.1; -. [O55143-1]
CCDS; CCDS57379.1; -. [O55143-2]
RefSeq; NP_001103610.1; NM_001110140.3. [O55143-1]
RefSeq; NP_033852.1; NM_009722.3. [O55143-2]
UniGene; Mm.227583; -.
ProteinModelPortal; O55143; -.
SMR; O55143; -.
BioGrid; 198249; 38.
IntAct; O55143; 41.
MINT; MINT-1853527; -.
STRING; 10090.ENSMUSP00000031423; -.
iPTMnet; O55143; -.
PhosphoSitePlus; O55143; -.
SwissPalm; O55143; -.
EPD; O55143; -.
MaxQB; O55143; -.
PaxDb; O55143; -.
PeptideAtlas; O55143; -.
PRIDE; O55143; -.
Ensembl; ENSMUST00000031423; ENSMUSP00000031423; ENSMUSG00000029467. [O55143-1]
Ensembl; ENSMUST00000177974; ENSMUSP00000136104; ENSMUSG00000029467. [O55143-2]
Ensembl; ENSMUST00000179939; ENSMUSP00000135935; ENSMUSG00000029467. [O55143-1]
GeneID; 11938; -.
KEGG; mmu:11938; -.
UCSC; uc008zli.2; mouse. [O55143-2]
CTD; 488; -.
MGI; MGI:88110; Atp2a2.
eggNOG; KOG0202; Eukaryota.
eggNOG; COG0474; LUCA.
GeneTree; ENSGT00890000139334; -.
HOGENOM; HOG000265621; -.
HOVERGEN; HBG105648; -.
InParanoid; O55143; -.
KO; K05853; -.
OMA; YNNTQQF; -.
OrthoDB; EOG091G01LE; -.
PhylomeDB; O55143; -.
TreeFam; TF300651; -.
BRENDA; 3.6.3.8; 3474.
Reactome; R-MMU-418359; Reduction of cytosolic Ca++ levels.
Reactome; R-MMU-5578775; Ion homeostasis.
Reactome; R-MMU-936837; Ion transport by P-type ATPases.
ChiTaRS; Atp2a2; mouse.
PRO; PR:O55143; -.
Proteomes; UP000000589; Chromosome 5.
Bgee; ENSMUSG00000029467; -.
Genevisible; O55143; MM.
GO; GO:0090534; C:calcium ion-transporting ATPase complex; ISO:MGI.
GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IEA:Ensembl.
GO; GO:0014801; C:longitudinal sarcoplasmic reticulum; ISO:MGI.
GO; GO:0016020; C:membrane; IDA:MGI.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0043234; C:protein complex; IEA:Ensembl.
GO; GO:0097470; C:ribbon synapse; IDA:MGI.
GO; GO:0016529; C:sarcoplasmic reticulum; IDA:MGI.
GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
GO; GO:0012506; C:vesicle membrane; IEA:Ensembl.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0005509; F:calcium ion binding; ISO:MGI.
GO; GO:0005388; F:calcium-transporting ATPase activity; IDA:MGI.
GO; GO:0086039; F:calcium-transporting ATPase activity involved in regulation of cardiac muscle cell membrane potential; IEA:Ensembl.
GO; GO:0019899; F:enzyme binding; IPI:BHF-UCL.
GO; GO:0031775; F:lutropin-choriogonadotropic hormone receptor binding; IEA:Ensembl.
GO; GO:0008022; F:protein C-terminus binding; IPI:UniProtKB.
GO; GO:0044548; F:S100 protein binding; ISO:MGI.
GO; GO:1990036; P:calcium ion import into sarcoplasmic reticulum; IEA:Ensembl.
GO; GO:0070588; P:calcium ion transmembrane transport; ISO:MGI.
GO; GO:1903515; P:calcium ion transport from cytosol to endoplasmic reticulum; ISO:MGI.
GO; GO:0014898; P:cardiac muscle hypertrophy in response to stress; IDA:MGI.
GO; GO:0006874; P:cellular calcium ion homeostasis; IDA:MGI.
GO; GO:0034599; P:cellular response to oxidative stress; IGI:MGI.
GO; GO:0032469; P:endoplasmic reticulum calcium ion homeostasis; ISO:MGI.
GO; GO:0006984; P:ER-nucleus signaling pathway; IMP:MGI.
GO; GO:0045822; P:negative regulation of heart contraction; IGI:MGI.
GO; GO:0006996; P:organelle organization; IMP:MGI.
GO; GO:0032470; P:positive regulation of endoplasmic reticulum calcium ion concentration; ISO:MGI.
GO; GO:1903233; P:regulation of calcium ion-dependent exocytosis of neurotransmitter; IMP:MGI.
GO; GO:0098909; P:regulation of cardiac muscle cell action potential involved in regulation of contraction; IEA:Ensembl.
GO; GO:0010882; P:regulation of cardiac muscle contraction by calcium ion signaling; ISO:MGI.
GO; GO:0006937; P:regulation of muscle contraction; TAS:MGI.
GO; GO:0002026; P:regulation of the force of heart contraction; IGI:MGI.
GO; GO:0055119; P:relaxation of cardiac muscle; ISO:MGI.
GO; GO:0070296; P:sarcoplasmic reticulum calcium ion transport; IMP:MGI.
GO; GO:0033292; P:T-tubule organization; IMP:MGI.
GO; GO:0014883; P:transition between fast and slow fiber; IDA:MGI.
Gene3D; 3.40.1110.10; -; 2.
Gene3D; 3.40.50.1000; -; 1.
InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
InterPro; IPR023299; ATPase_P-typ_cyto_domN.
InterPro; IPR018303; ATPase_P-typ_P_site.
InterPro; IPR023298; ATPase_P-typ_TM_dom.
InterPro; IPR008250; ATPase_P-typ_transduc_dom_A.
InterPro; IPR036412; HAD-like_sf.
InterPro; IPR023214; HAD_sf.
InterPro; IPR005782; P-type_ATPase_IIA.
InterPro; IPR001757; P_typ_ATPase.
Pfam; PF00689; Cation_ATPase_C; 1.
Pfam; PF00690; Cation_ATPase_N; 1.
PRINTS; PR00120; HATPASE.
SMART; SM00831; Cation_ATPase_N; 1.
SUPFAM; SSF56784; SSF56784; 1.
SUPFAM; SSF81653; SSF81653; 1.
SUPFAM; SSF81660; SSF81660; 1.
SUPFAM; SSF81665; SSF81665; 3.
TIGRFAMs; TIGR01116; ATPase-IIA1_Ca; 1.
TIGRFAMs; TIGR01494; ATPase_P-type; 2.
PROSITE; PS00154; ATPASE_E1_E2; 1.
1: Evidence at protein level;
Alternative splicing; ATP-binding; Calcium; Calcium transport;
Complete proteome; Direct protein sequencing; Endoplasmic reticulum;
Hydrolase; Ion transport; Magnesium; Membrane; Metal-binding;
Nitration; Nucleotide-binding; Phosphoprotein; Reference proteome;
Sarcoplasmic reticulum; Transmembrane; Transmembrane helix; Transport.
CHAIN 1 1044 Sarcoplasmic/endoplasmic reticulum
calcium ATPase 2.
/FTId=PRO_0000046197.
TOPO_DOM 1 48 Cytoplasmic. {ECO:0000250}.
TRANSMEM 49 69 Helical; Name=1. {ECO:0000250}.
TOPO_DOM 70 89 Lumenal. {ECO:0000250}.
TRANSMEM 90 110 Helical; Name=2. {ECO:0000250}.
TOPO_DOM 111 253 Cytoplasmic. {ECO:0000250}.
TRANSMEM 254 273 Helical; Name=3. {ECO:0000250}.
TOPO_DOM 274 295 Lumenal. {ECO:0000250}.
TRANSMEM 296 313 Helical; Name=4. {ECO:0000250}.
TOPO_DOM 314 756 Cytoplasmic. {ECO:0000250}.
TRANSMEM 757 776 Helical; Name=5. {ECO:0000250}.
TOPO_DOM 777 786 Lumenal. {ECO:0000250}.
TRANSMEM 787 807 Helical; Name=6. {ECO:0000250}.
TOPO_DOM 808 827 Cytoplasmic. {ECO:0000250}.
TRANSMEM 828 850 Helical; Name=7. {ECO:0000250}.
TOPO_DOM 851 896 Lumenal. {ECO:0000250}.
TRANSMEM 897 916 Helical; Name=8. {ECO:0000250}.
TOPO_DOM 917 929 Cytoplasmic. {ECO:0000250}.
TRANSMEM 930 948 Helical; Name=9. {ECO:0000250}.
TOPO_DOM 949 963 Lumenal. {ECO:0000250}.
TRANSMEM 964 984 Helical; Name=10. {ECO:0000250}.
TOPO_DOM 985 1044 Cytoplasmic. {ECO:0000250}.
REGION 370 400 Interaction with phospholamban 1.
{ECO:0000250|UniProtKB:P04191}.
REGION 575 594 Interaction with HAX1. {ECO:0000250}.
REGION 787 807 Interaction with phospholamban 2.
{ECO:0000250|UniProtKB:P04191}.
REGION 788 1044 Interaction with TMEM64 and PDIA3.
{ECO:0000269|PubMed:23395171}.
ACT_SITE 351 351 4-aspartylphosphate intermediate.
{ECO:0000250|UniProtKB:P04191}.
METAL 304 304 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 305 305 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 307 307 Calcium 2; via carbonyl oxygen.
{ECO:0000250|UniProtKB:P04191}.
METAL 309 309 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 702 702 Magnesium. {ECO:0000250}.
METAL 706 706 Magnesium. {ECO:0000250}.
METAL 767 767 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 770 770 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 795 795 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 798 798 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
METAL 799 799 Calcium 2.
{ECO:0000250|UniProtKB:P04191}.
METAL 907 907 Calcium 1.
{ECO:0000250|UniProtKB:P04191}.
MOD_RES 38 38 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 294 294 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P16615}.
MOD_RES 295 295 Nitrated tyrosine.
{ECO:0000250|UniProtKB:P16615}.
MOD_RES 441 441 Phosphothreonine.
{ECO:0000250|UniProtKB:Q64578}.
MOD_RES 531 531 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 580 580 Phosphoserine.
{ECO:0000250|UniProtKB:P16615}.
MOD_RES 661 661 Phosphoserine.
{ECO:0000250|UniProtKB:P11507}.
MOD_RES 663 663 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 995 1044 GKECVQPATKSSCSLSACTDGISWPFVLLIMPLVVWVYSTD
TNFSDMFWS -> AILE (in isoform 2).
{ECO:0000303|PubMed:10656932}.
/FTId=VSP_000359.
SEQUENCE 1044 AA; 114858 MW; 06A753982116C421 CRC64;
MENAHTKTVE EVLGHFGVNE STGLSLEQVK KLKERWGSNE LPAEEGKTLL ELVIEQFEDL
LVRILLLAAC ISFVLAWFEE GEETITAFVE PFVILLILVA NAIVGVWQER NAENAIEALK
EYEPEMGKVY RQDRKSVQRI KAKDIVPGDI VEIAVGDKVP ADIRLTSIKS TTLRVDQSIL
TGESVSVIKH TDPVPDPRAV NQDKKNMLFS GTNIAAGKAM GVVVATGVNT EIGKIRDEMV
ATEQERTPLQ QKLDEFGEQL SKVISLICIA VWIINIGHFN DPVHGGSWIR GAIYYFKIAV
ALAVAAIPEG LPAVITTCLA LGTRRMAKKN AIVRSLPSVE TLGCTSVICS DKTGTLTTNQ
MSVCRMFILD KVEGDTCSLN EFSITGSTYA PIGEVQKDDK PVKCHQYDGL VELATICALC
NDSALDYNEA KGVYEKVGEA TETALTCLVE KMNVFDTELK GLSKIERANA CNSVIKQLMK
KEFTLEFSRD RKSMSVYCTP NKPSRTSMSK MFVKGAPEGV IDRCTHIRVG STKVPMTPGV
KQKIMSVIRE WGSGSDTLRC LALATHDNPL KREEMHLEDS ANFIKYETNL TFVGCVGMLD
PPRIEVASSV KLCRQAGIRV IMITGDNKGT AVAICRRIGI FGQDEDVTSK AFTGREFDEL
SPSAQRDACL NARCFARVEP SHKSKIVEFL QSFDEITAMT GDGVNDAPAL KKSEIGIAMG
SGTAVAKTAS EMVLADDNFS TIVAAVEEGR AIYNNMKQFI RYLISSNVGE VVCIFLTAAL
GFPEALIPVQ LLWVNLVTDG LPATALGFNP PDLDIMNKPP RNPKEPLISG WLFFRYLAIG
CYVGAATVGA AAWWFIAADG GPRVSFYQLS HFLQCKEDNP DFDGVDCAIF ESPYPMTMAL
SVLVTIEMCN ALNSLSENQS LLRMPPWENI WLVGSICLSM SLHFLILYVE PLPLIFQITP
LNLTQWLMVL KISLPVILMD ETLKFVARNY LEQPGKECVQ PATKSSCSLS ACTDGISWPF
VLLIMPLVVW VYSTDTNFSD MFWS


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G8945 Sarcoplasmic endoplasmic reticulum calcium ATPase 3 (ATP2A3), Human, ELISA Kit 96T
G8944 Sarcoplasmic endoplasmic reticulum calcium ATPase 3 (ATP2A3), Chicken, ELISA Kit 96T
G8931 Sarcoplasmic endoplasmic reticulum calcium ATPase 1 (ATP2A1), Chicken, ELISA Kit 96T
G8932 Sarcoplasmic endoplasmic reticulum calcium ATPase 1 (ATP2A1), Human, ELISA Kit 96T
CSB-EL002332HU Human Sarcoplasmic per endoplasmic reticulum calcium ATPase 1(ATP2A1) ELISA kit 96T
G8933 Sarcoplasmic endoplasmic reticulum calcium ATPase 1 (ATP2A1), Mouse, ELISA Kit 96T


 

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