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Poly(A) polymerase alpha (PAP-alpha) (EC 2.7.7.19) (Polynucleotide adenylyltransferase alpha) [Cleaved into: Poly(A) polymerase alpha, N-terminally processed]

 PAPOA_BOVIN             Reviewed;         739 AA.
P25500;
01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 152.
RecName: Full=Poly(A) polymerase alpha;
Short=PAP-alpha;
EC=2.7.7.19;
AltName: Full=Polynucleotide adenylyltransferase alpha;
Name=PAPOLA; Synonyms=PAP;
Bos taurus (Bovine).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
Pecora; Bovidae; Bovinae; Bos.
NCBI_TaxID=9913;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT), AND PROTEIN
SEQUENCE OF 1-21; 207-255 AND 386-397.
TISSUE=Thymus;
PubMed=1756732;
Wahle E., Martin G., Schiltz E., Keller W.;
"Isolation and expression of cDNA clones encoding mammalian poly(A)
polymerase.";
EMBO J. 10:4251-4257(1991).
[2]
SEQUENCE REVISION.
Wahle E.;
Submitted (AUG-1992) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 97-103 AND
445-468.
TISSUE=Heart muscle;
PubMed=1896071; DOI=10.1038/353229a0;
Raabe T., Bollum F.J., Manley J.L.;
"Primary structure and expression of bovine poly(A) polymerase.";
Nature 353:229-234(1991).
[4]
DOMAINS, AND MUTAGENESIS OF ASP-113; ASP-115; 162-ASP-GLY-163;
ASP-167; ASP-186; ASP-194; ASP-208; GLU-209; GLU-291; GLU-292;
431-GLU-GLU-432; ASP-455; ASP-459 AND ASP-465.
PubMed=8665867;
Martin G., Keller W.;
"Mutational analysis of mammalian poly(A) polymerase identifies a
region for primer binding and catalytic domain, homologous to the
family X polymerases, and to other nucleotidyltransferases.";
EMBO J. 15:2593-2603(1996).
[5]
PHOSPHORYLATION, AND FUNCTION.
PubMed=9463383; DOI=10.1093/emboj/17.4.1053;
Colgan D.F., Murthy K.G., Zhao W., Prives C., Manley J.L.;
"Inhibition of poly(A) polymerase requires p34cdc2/cyclin B
phosphorylation of multiple consensus and non-consensus sites.";
EMBO J. 17:1053-1062(1998).
[6]
ACETYLATION AT LYS-635; LYS-644; LYS-730 AND LYS-734, INTERACTION WITH
NUDT21 AND KPBN1, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS
SPECTROMETRY, AND MUTAGENESIS OF LYS-635; LYS-644; LYS-730 AND
LYS-734.
PubMed=17172643; DOI=10.1074/jbc.M609745200;
Shimazu T., Horinouchi S., Yoshida M.;
"Multiple histone deacetylases and the CREB-binding protein regulate
pre-mRNA 3'-end processing.";
J. Biol. Chem. 282:4470-4478(2007).
[7]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1-513 IN COMPLEX WITH ATP
ANALOG AND MANGANESE IONS.
PubMed=10944102; DOI=10.1093/emboj/19.16.4193;
Martin G., Keller W., Doublie S.;
"Crystal structure of mammalian poly(A) polymerase in complex with an
analog of ATP.";
EMBO J. 19:4193-4203(2000).
[8]
X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-513 IN COMPLEX WITH
MAGNESIUM IONS; MANGANESE IONS AND ATP ANALOG, BIOPHYSICOCHEMICAL
PROPERTIES, CATALYTIC ACTIVITY, COFACTOR, AND MUTAGENESIS OF PHE-100;
PHE-153; VAL-156; ASP-167; ARG-199; ASN-202; GLY-203; LYS-228;
LYS-232; TYR-237 AND VAL-247.
PubMed=15328606; DOI=10.1016/j.jmb.2004.06.047;
Martin G., Moglich A., Keller W., Doublie S.;
"Biochemical and structural insights into substrate binding and
catalytic mechanism of mammalian poly(A) polymerase.";
J. Mol. Biol. 341:911-925(2004).
-!- FUNCTION: Polymerase that creates the 3'-poly(A) tail of mRNA's.
Also required for the endoribonucleolytic cleavage reaction at
some polyadenylation sites. May acquire specificity through
interaction with a cleavage and polyadenylation specificity factor
(CPSF) at its C-terminus. {ECO:0000250|UniProtKB:P51003,
ECO:0000269|PubMed:9463383}.
-!- CATALYTIC ACTIVITY: ATP + RNA(n) = diphosphate + RNA(n+1).
{ECO:0000269|PubMed:15328606}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:15328606};
Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
Evidence={ECO:0000269|PubMed:15328606};
Note=Binds 2 magnesium ions. Also active with manganese.
{ECO:0000269|PubMed:15328606};
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=0.229 mM for ATP {ECO:0000269|PubMed:15328606};
-!- SUBUNIT: Monomer (PubMed:10944102, PubMed:15328606). Found in a
complex with CPSF1, FIP1L1 and PAPOLA. Interacts with AHCYL1 and
FIP1L1; the interaction with AHCYL1 seems to increase interaction
with FIP1L1 (By similarity). Interacts with NUDT21; the
interaction is diminished by acetylation (PubMed:17172643).
Interacts with KPNB1; the interaction promotes PAP nuclear import
and is inhibited by acetylation of PAP (PubMed:17172643).
{ECO:0000250|UniProtKB:P51003, ECO:0000250|UniProtKB:Q61183,
ECO:0000269|PubMed:10944102, ECO:0000269|PubMed:15328606,
ECO:0000269|PubMed:17172643}.
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17172643}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Comment=Additional isoforms seem to exist.;
Name=Long;
IsoId=P25500-1; Sequence=Displayed;
Name=Short;
IsoId=P25500-2; Sequence=VSP_004524, VSP_004525, VSP_004526;
Note=No experimental confirmation available.;
-!- PTM: Polysumoylated. Varying sumolyation depending on tissue- and
cell-type. Highly sumoylated in bladder and NIH 3T3 cells.
Sumoylation is required for nuclear localization and enhances PAP
stability. Desumoylated by SENP1. Inhibits polymerase activity (By
similarity). {ECO:0000250}.
-!- PTM: Hyperphosphorylation on multiple CDK2 consensus and non-
consensus sites in the C-terminal Ser/Thr-rich region represses
PAP activity in late M-phase. Phosphorylation/dephosphorylation
may regulate the interaction between PAP and CPSF (By similarity).
{ECO:0000250}.
-!- PTM: Acetylated in the C-terminus. Acetylation decreases
interaction with NUDT21 and KPNB1, and inhibits nuclear
localization through inhibiting binding to the importin alpha/beta
complex. {ECO:0000269|PubMed:17172643}.
-!- SIMILARITY: Belongs to the poly(A) polymerase family.
{ECO:0000305}.
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EMBL; X61585; CAA43782.1; -; mRNA.
EMBL; X63436; CAA45031.1; -; mRNA.
PIR; S17875; S17875.
PIR; S17925; S17925.
PIR; S18642; S18642.
RefSeq; NP_788820.1; NM_176647.2. [P25500-1]
UniGene; Bt.109586; -.
PDB; 1F5A; X-ray; 2.50 A; A=1-513.
PDB; 1Q78; X-ray; 2.80 A; A=1-514.
PDB; 1Q79; X-ray; 2.15 A; A=1-514.
PDBsum; 1F5A; -.
PDBsum; 1Q78; -.
PDBsum; 1Q79; -.
ProteinModelPortal; P25500; -.
SMR; P25500; -.
STRING; 9913.ENSBTAP00000005300; -.
PaxDb; P25500; -.
PRIDE; P25500; -.
Ensembl; ENSBTAT00000005300; ENSBTAP00000005300; ENSBTAG00000004054. [P25500-1]
GeneID; 338051; -.
KEGG; bta:338051; -.
CTD; 10914; -.
eggNOG; KOG2245; Eukaryota.
eggNOG; COG5186; LUCA.
GeneTree; ENSGT00390000017928; -.
HOGENOM; HOG000204376; -.
HOVERGEN; HBG053502; -.
InParanoid; P25500; -.
KO; K14376; -.
OMA; MGIVVRH; -.
OrthoDB; EOG091G0571; -.
TreeFam; TF300842; -.
BRENDA; 2.7.7.19; 908.
Reactome; R-BTA-109688; Cleavage of Growing Transcript in the Termination Region.
Reactome; R-BTA-72163; mRNA Splicing - Major Pathway.
Reactome; R-BTA-72187; mRNA 3'-end processing.
Reactome; R-BTA-77595; Processing of Intronless Pre-mRNAs.
SABIO-RK; P25500; -.
EvolutionaryTrace; P25500; -.
Proteomes; UP000009136; Chromosome 21.
Bgee; ENSBTAG00000004054; -.
ExpressionAtlas; P25500; baseline and differential.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
GO; GO:0000287; F:magnesium ion binding; IDA:UniProtKB.
GO; GO:0030145; F:manganese ion binding; IDA:UniProtKB.
GO; GO:0004652; F:polynucleotide adenylyltransferase activity; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0006378; P:mRNA polyadenylation; ISS:UniProtKB.
GO; GO:0031440; P:regulation of mRNA 3'-end processing; ISS:UniProtKB.
GO; GO:0043631; P:RNA polyadenylation; IDA:UniProtKB.
InterPro; IPR011068; NuclTrfase_I_C.
InterPro; IPR007012; PolA_pol_cen_dom.
InterPro; IPR007010; PolA_pol_RNA-bd_dom.
InterPro; IPR014492; PolyA_polymerase.
InterPro; IPR002934; Polymerase_NTP_transf_dom.
PANTHER; PTHR10682; PTHR10682; 1.
Pfam; PF01909; NTP_transf_2; 1.
Pfam; PF04928; PAP_central; 1.
Pfam; PF04926; PAP_RNA-bind; 1.
PIRSF; PIRSF018425; PolyA_polymerase; 1.
SUPFAM; SSF55003; SSF55003; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; ATP-binding;
Complete proteome; Direct protein sequencing; Isopeptide bond;
Magnesium; Manganese; Metal-binding; mRNA processing;
Nucleotide-binding; Nucleus; Phosphoprotein; Reference proteome;
RNA-binding; Transferase; Ubl conjugation.
CHAIN 1 739 Poly(A) polymerase alpha.
/FTId=PRO_0000051611.
NP_BIND 100 102 ATP.
NP_BIND 113 115 ATP.
NP_BIND 246 247 ATP.
REGION 508 643 Ser/Thr-rich.
REGION 671 739 Required for interaction with NUDT21.
{ECO:0000269|PubMed:17172643}.
MOTIF 490 507 Nuclear localization signal 1.
MOTIF 644 659 Nuclear localization signal 2.
METAL 113 113 Magnesium 1; catalytic.
METAL 113 113 Magnesium 2; catalytic.
METAL 115 115 Magnesium 1; catalytic.
METAL 115 115 Magnesium 2; catalytic.
METAL 167 167 Magnesium 2; catalytic.
BINDING 109 109 ATP.
BINDING 167 167 ATP.
BINDING 228 228 ATP.
BINDING 237 237 ATP.
SITE 153 153 Interaction with RNA. {ECO:0000250}.
SITE 158 158 Interaction with RNA. {ECO:0000250}.
SITE 328 328 Interaction with RNA. {ECO:0000250}.
SITE 399 399 Interaction with RNA. {ECO:0000250}.
SITE 524 524 Interaction with RNA. {ECO:0000250}.
MOD_RES 10 10 Phosphoserine.
{ECO:0000250|UniProtKB:P51003}.
MOD_RES 24 24 Phosphoserine.
{ECO:0000250|UniProtKB:P51003}.
MOD_RES 537 537 Phosphoserine; by MAPK.
{ECO:0000250|UniProtKB:Q61183}.
MOD_RES 558 558 Phosphoserine.
{ECO:0000250|UniProtKB:P51003}.
MOD_RES 635 635 N6-acetyllysine.
{ECO:0000269|PubMed:17172643}.
MOD_RES 644 644 N6-acetyllysine.
{ECO:0000269|PubMed:17172643}.
MOD_RES 730 730 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17172643}.
MOD_RES 732 732 Phosphoserine.
{ECO:0000250|UniProtKB:P51003}.
MOD_RES 734 734 N6-acetyllysine; alternate.
{ECO:0000269|PubMed:17172643}.
CROSSLNK 444 444 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000305}.
CROSSLNK 445 445 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000305}.
CROSSLNK 506 506 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000305}.
CROSSLNK 507 507 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO).
{ECO:0000305}.
CROSSLNK 730 730 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
CROSSLNK 734 734 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO);
alternate. {ECO:0000250}.
VAR_SEQ 663 683 Missing (in isoform Short).
{ECO:0000303|PubMed:1756732}.
/FTId=VSP_004524.
VAR_SEQ 709 710 KT -> II (in isoform Short).
{ECO:0000303|PubMed:1756732}.
/FTId=VSP_004525.
VAR_SEQ 711 739 Missing (in isoform Short).
{ECO:0000303|PubMed:1756732}.
/FTId=VSP_004526.
MUTAGEN 100 100 F->D: Strongly decreased enzyme activity.
Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 113 115 DID->AIA: Abolishes most of the specific
and non-specific polyadenylation
activity.
MUTAGEN 113 113 D->H: Abolishes most of the specific and
non-specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 115 115 D->H: Abolishes most of the specific and
non-specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 153 153 F->A: Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 156 156 V->A: Strongly decreased enzyme activity.
Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 162 163 DG->HA: Small decrease in non-specific
and specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 167 167 D->A: Loss of enzyme activity.
{ECO:0000269|PubMed:15328606,
ECO:0000269|PubMed:8665867}.
MUTAGEN 167 167 D->H: Abolishes most of the specific and
non-specific polyadenylation activity.
{ECO:0000269|PubMed:15328606,
ECO:0000269|PubMed:8665867}.
MUTAGEN 167 167 D->N: Strongly decreased enzyme activity.
Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606,
ECO:0000269|PubMed:8665867}.
MUTAGEN 186 186 D->H: Small decrease in non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 194 194 D->H: No change in non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 199 199 R->A: Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 202 202 N->A: Strongly decreased enzyme activity.
Strongly reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 203 203 G->H: Loss of enzyme activity. Strongly
reduced affinity for RNA.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 208 209 DE->AA: Reduces by 60% non-specific and
specific polyadenylation activity.
MUTAGEN 208 208 D->A: Reduces by 60% non-specific rf and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 208 208 D->H: Reduces by 20% non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 209 209 E->A: No change in non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 228 228 K->A: Strongly decreased affinity for
ATP. {ECO:0000269|PubMed:15328606}.
MUTAGEN 232 232 K->A: Decreased affinity for ATP.
{ECO:0000269|PubMed:15328606}.
MUTAGEN 237 237 Y->A: Strongly decreased affinity for
ATP. {ECO:0000269|PubMed:15328606}.
MUTAGEN 247 247 V->A,R: Strongly reduced affinity for
RNA. {ECO:0000269|PubMed:15328606}.
MUTAGEN 291 292 EE->AA: Abolishes most of non-specific
polyadenylation activity.
MUTAGEN 291 291 E->A: Reduces by 60% non-specific
polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 292 292 E->A: No change in non-specific
polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 308 308 D->A: No change in non-specific and
specific polyadenylation activity.
MUTAGEN 317 317 T->G: Strongly decreased affinity for
ATP.
MUTAGEN 431 432 EE->AA: No change in non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 455 455 D->A: Reduces by 30% non-specific
polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 459 459 D->A: No change in non-specific
polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 465 465 D->A: No change in non-specific and
specific polyadenylation activity.
{ECO:0000269|PubMed:8665867}.
MUTAGEN 635 635 K->Q: Weak binding to KPBN1. Cytoplasmic
location; when associated with Q-644; Q-
730 and Q-734.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 635 635 K->R: Some decrease in acetylation. Binds
KPBN1 and localizes to the nucleus; when
associated with R-644; R-730 and R-734.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 644 644 K->Q: Weak binding to KPBN1. Cytoplasmic
location; when associated with Q-635; Q-
730 and Q-734.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 644 644 K->R: Large decrease in acetylation.
Binds KPBN1 and localizes to the nucleus;
when associated with R-635; R-730 and R-
734. {ECO:0000269|PubMed:17172643}.
MUTAGEN 730 730 K->Q: Weak binding to KPBN1. Cytoplasmic
location; when associated with Q-635; Q-
644 and Q-734.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 730 730 K->R: Some decrease in acetylation. Binds
KPBN1 and localizes to the nucleus; when
associated with R-635; R-644 and R-734.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 734 734 K->Q: Weak binding to KPBN1. Cytoplasmic
location; when associated with Q-635; Q-
644 and Q-730.
{ECO:0000269|PubMed:17172643}.
MUTAGEN 734 734 K->R: Some decrease in acetylation. Binds
KPBN1 and localizes to the nucleus; when
associated with R-635; R-644 and R-730.
{ECO:0000269|PubMed:17172643}.
CONFLICT 80 80 S -> R (in Ref. 3; CAA45031).
{ECO:0000305}.
STRAND 21 23 {ECO:0000244|PDB:1Q79}.
HELIX 33 46 {ECO:0000244|PDB:1Q79}.
HELIX 47 49 {ECO:0000244|PDB:1Q79}.
HELIX 55 82 {ECO:0000244|PDB:1Q79}.
HELIX 87 90 {ECO:0000244|PDB:1Q79}.
STRAND 96 100 {ECO:0000244|PDB:1Q79}.
HELIX 101 105 {ECO:0000244|PDB:1Q79}.
STRAND 114 120 {ECO:0000244|PDB:1Q79}.
HELIX 126 129 {ECO:0000244|PDB:1Q79}.
HELIX 132 138 {ECO:0000244|PDB:1Q79}.
STRAND 143 149 {ECO:0000244|PDB:1Q79}.
STRAND 152 154 {ECO:0000244|PDB:1Q79}.
STRAND 156 161 {ECO:0000244|PDB:1Q79}.
STRAND 164 172 {ECO:0000244|PDB:1Q79}.
STRAND 176 178 {ECO:0000244|PDB:1Q79}.
HELIX 187 190 {ECO:0000244|PDB:1Q79}.
HELIX 195 211 {ECO:0000244|PDB:1Q79}.
STRAND 213 215 {ECO:0000244|PDB:1Q79}.
HELIX 217 233 {ECO:0000244|PDB:1Q79}.
TURN 239 242 {ECO:0000244|PDB:1Q79}.
HELIX 246 259 {ECO:0000244|PDB:1Q79}.
HELIX 265 277 {ECO:0000244|PDB:1Q79}.
TURN 302 304 {ECO:0000244|PDB:1Q79}.
HELIX 306 310 {ECO:0000244|PDB:1Q79}.
STRAND 318 321 {ECO:0000244|PDB:1Q79}.
TURN 325 328 {ECO:0000244|PDB:1Q79}.
HELIX 331 352 {ECO:0000244|PDB:1Q79}.
HELIX 358 361 {ECO:0000244|PDB:1Q79}.
HELIX 367 370 {ECO:0000244|PDB:1Q79}.
STRAND 372 383 {ECO:0000244|PDB:1Q79}.
HELIX 384 395 {ECO:0000244|PDB:1Q79}.
HELIX 398 406 {ECO:0000244|PDB:1Q79}.
STRAND 411 416 {ECO:0000244|PDB:1Q79}.
STRAND 428 430 {ECO:0000244|PDB:1Q78}.
STRAND 433 443 {ECO:0000244|PDB:1Q79}.
HELIX 457 473 {ECO:0000244|PDB:1Q79}.
STRAND 482 489 {ECO:0000244|PDB:1Q79}.
HELIX 490 493 {ECO:0000244|PDB:1Q79}.
HELIX 494 496 {ECO:0000244|PDB:1Q79}.
SEQUENCE 739 AA; 82441 MW; 7C89C15E33232CFF CRC64;
MPFPVTTQGS QQTQPPQKHY GITSPISLAA PKETDCLLTQ KLVETLKPFG VFEEEEELQR
RILILGKLNN LVKEWIREIS ESKNLPQSVI ENVGGKIFTF GSYRLGVHTK GADIDALCVA
PRHVDRSDFF TSFYDKLKLQ EEVKDLRAVE EAFVPVIKLC FDGIEIDILF ARLALQTIPE
DLDLRDDSLL KNLDIRCIRS LNGCRVTDEI LHLVPNIDNF RLTLRAIKLW AKRHNIYSNI
LGFLGGVSWA MLVARTCQLY PNAIASTLVH KFFLVFSKWE WPNPVLLKQP EECNLNLPVW
DPRVNPSDRY HLMPIITPAY PQQNSTYNVS VSTRMVMVEE FKQGLAITDE ILLSKAEWSK
LFEAPNFFQK YKHYIVLLAS APTEKQRLEW VGLVESKIRI LVGSLEKNEF ITLAHVNPQS
FPAPKENPDK EEFRTMWVIG LVFKKTENSE NLSVDLTYDI QSFTDTVYRQ AINSKMFEVD
MKIAAMHVKR KQLHQLLPSH VLQKKKKHST EGVKLTPLND SSLDLSMDSD NSMSVPSPTS
AMKTSPLNSS GSSQGRNSPA PAVTAASVTN IQATEVSLPQ INSSESSGGT SSESIPQTAT
QPAISSPPKP TVSRVVSSTR LVNPPPRPSG NAAAKIPNPI VGVKRTSSPH KEESPKKTKT
EEDETSEDAN CLALSGHDKT ETKEQLDTET STTQSETIQT ATSLLASQKT SSTDLSDIPA
LPANPIPVIK NSIKLRLNR


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EIAAB29845 Mouse,Mus musculus,PAP-beta,Papolb,Papt,Poly(A) polymerase beta,Polynucleotide adenylyltransferase beta,Testis-specific poly(A) polymerase,Tpap
EIAAB29835 Mouse,Mtpap,Mus musculus,PAP,PAP-associated domain-containing protein 1,Papd1,Poly(A) RNA polymerase, mitochondrial,Polynucleotide adenylyltransferase
PAPOLG PAPOLA Gene poly(A) polymerase alpha
E13337h Human Poly A Polymerase Alpha ELISA Kit 96T
CSB-EL017432HU Human Poly(A) polymerase alpha (PAPOLA) ELISA kit 96T
CSB-EL017432BO Bovine Poly(A) polymerase alpha (PAPOLA) ELISA kit 96T
CSB-EL017432MO Mouse Poly(A) polymerase alpha (PAPOLA) ELISA kit 96T
EIAAB29834 Homo sapiens,Human,mtPAP,MTPAP,PAP,PAP-associated domain-containing protein 1,PAPD1,Poly(A) RNA polymerase, mitochondrial,Polynucleotide adenylyltransferase,Terminal uridylyltransferase 1,TUTase 1
EIAAB29847 Mouse,Mus musculus,PAP-gamma,Papolg,Poly(A) polymerase gamma,Polynucleotide adenylyltransferase gamma,SRP RNA 3'-adenylating enzyme
PAPOA_MOUSE ELISA Kit FOR Poly(A) polymerase alpha; organism: Mouse; gene name: Papola 96T
20-272-190970 cleaved IKB alpha - Mouse monoclonal to cleaved IKB alpha; Major histocompatibility complex enhancer-binding protein MAD3; I-kappa-B-alpha; IkappaBalpha; IKB-alpha Monoclonal 0.05 mg
CSB-EL017432MO Mouse poly(A) polymerase alpha (PAPOLA) ELISA kit, Species Mouse, Sample Type serum, plasma 96T
CSB-EL017432BO Bovine poly(A) polymerase alpha (PAPOLA) ELISA kit, Species Bovine, Sample Type serum, plasma 96T
CSB-EL017432HU Human poly(A) polymerase alpha (PAPOLA) ELISA kit, Species Human, Sample Type serum, plasma 96T
EIAAB11784 DNA polymerase alpha 70 kDa subunit,DNA polymerase alpha subunit B,Homo sapiens,Human,POLA2
EIAAB11786 DNA polymerase alpha 70 kDa subunit,DNA polymerase alpha subunit B,DNA polymerase subunit II,Pola2,Rat,Rattus norvegicus
EIAAB11785 Bos taurus,Bovine,DNA polymerase alpha 70 kDa subunit,DNA polymerase alpha subunit B,POLA2
EIAAB11787 DNA polymerase alpha 70 kDa subunit,DNA polymerase alpha subunit B,Mouse,Mus musculus,Pola2
EIAAB11823 DNA polymerase alpha catalytic subunit,DNA polymerase alpha catalytic subunit p180,Homo sapiens,Human,POLA,POLA1
EIAAB11824 DNA polymerase alpha catalytic subunit,DNA polymerase alpha catalytic subunit p180,Pola,Pola1,Rat,Rattus norvegicus


 

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