Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

DNA dC->dU-editing enzyme APOBEC-3 (EC 3.5.4.-) (Apolipoprotein B mRNA-editing complex 3) (Arp3) (CEM-15) (CEM15)

 ABEC3_MOUSE             Reviewed;         440 AA.
Q99J72; H3BJL0; Q8C7L0; Q8C8V7;
13-APR-2004, integrated into UniProtKB/Swiss-Prot.
20-DEC-2017, sequence version 3.
25-APR-2018, entry version 128.
RecName: Full=DNA dC->dU-editing enzyme APOBEC-3;
EC=3.5.4.-;
AltName: Full=Apolipoprotein B mRNA-editing complex 3;
Short=Arp3;
AltName: Full=CEM-15;
Short=CEM15;
Name=Apobec3;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND
VARIANTS ARG-45; 48-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146;
ASN-150; LYS-192; 244-VAL-HIS-LEU-246; GLY-269; ILE-317 AND HIS-415.
STRAIN=C57BL/6J; TISSUE=Hippocampus, and Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE (ISOFORM 4), AND VARIANTS.
STRAIN=C57BL/6J; TISSUE=Spleen;
Mariani R., Landau N.R.;
Submitted (FEB-2004) to UniProtKB.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
ARG-45; 48-ILE-ASP-49; 123-VAL-LEU-124; 145-ILE-ARG-146; ASN-150;
LYS-192; 244-VAL-HIS-LEU-246; GLY-269; ILE-317 AND HIS-415.
TISSUE=Mammary tumor;
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).
[5]
DNA C TO U EDITING ACTIVITY, AND TISSUE SPECIFICITY.
PubMed=12859895; DOI=10.1016/S0092-8674(03)00515-4;
Mariani R., Chen D., Schroefelbauer B., Navarro F., Koenig R.,
Bollman B., Muenk C., Nymark-McMahon H., Landau N.R.;
"Species-specific exclusion of APOBEC3G from HIV-1 virions by Vif.";
Cell 114:21-31(2003).
[6]
FUNCTION IN RETROTRANSPOSITION, AND SUBCELLULAR LOCATION.
PubMed=16527742; DOI=10.1016/j.cub.2006.01.031;
Chen H., Lilley C.E., Yu Q., Lee D.V., Chou J., Narvaiza I.,
Landau N.R., Weitzman M.D.;
"APOBEC3A is a potent inhibitor of adeno-associated virus and
retrotransposons.";
Curr. Biol. 16:480-485(2006).
[7]
DOMAIN CMP/DCMP DEAMINASE, SUBUNIT, AND MUTAGENESIS OF GLU-84 AND
GLU-301.
PubMed=17020885; DOI=10.1074/jbc.M604980200;
Hakata Y., Landau N.R.;
"Reversed functional organization of mouse and human APOBEC3 cytidine
deaminase domains.";
J. Biol. Chem. 281:36624-36631(2006).
[8]
FUNCTION IN SFV RESTRICTION.
PubMed=16378963; DOI=10.1128/JVI.80.2.605-614.2006;
Delebecque F., Suspene R., Calattini S., Casartelli N., Saib A.,
Froment A., Wain-Hobson S., Gessain A., Vartanian J.P., Schwartz O.;
"Restriction of foamy viruses by APOBEC cytidine deaminases.";
J. Virol. 80:605-614(2006).
[9]
FUNCTION IN MMTV RESTRICTION, AND INTERACTION WITH MMTV NUCLEOCAPSID
PROTEIN P14.
PubMed=17259974; DOI=10.1038/nature05540;
Okeoma C.M., Lovsin N., Peterlin B.M., Ross S.R.;
"APOBEC3 inhibits mouse mammary tumour virus replication in vivo.";
Nature 445:927-930(2007).
[10]
REVIEW.
PubMed=18304004; DOI=10.1146/annurev.immunol.26.021607.090350;
Chiu Y.L., Greene W.C.;
"The APOBEC3 cytidine deaminases: an innate defensive network opposing
exogenous retroviruses and endogenous retroelements.";
Annu. Rev. Immunol. 26:317-353(2008).
[11]
FUNCTION IN FRMLV RESTRICTION.
PubMed=18786991; DOI=10.1128/JVI.01311-08;
Takeda E., Tsuji-Kawahara S., Sakamoto M., Langlois M.A.,
Neuberger M.S., Rada C., Miyazawa M.;
"Mouse APOBEC3 restricts friend leukemia virus infection and
pathogenesis in vivo.";
J. Virol. 82:10998-11008(2008).
-!- FUNCTION: DNA deaminase (cytidine deaminase) which acts as an
inhibitor of retrovirus replication and retrotransposon mobility
via deaminase-dependent and -independent mechanisms. Selectively
targets single-stranded DNA and does not deaminate double-stranded
DNA or single-or double-stranded RNA. Exhibits antiviral activity
against HIV-1, simian immunodeficiency viruses (SIVs), mouse
mammary tumor virus (MMTV) and friend murine leukemia virus
(FrMLV) and may inhibit the mobility of LTR retrotransposons.
{ECO:0000269|PubMed:16378963, ECO:0000269|PubMed:16527742,
ECO:0000269|PubMed:17259974, ECO:0000269|PubMed:18786991}.
-!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3).
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
-!- SUBUNIT: Homodimer. Interacts with mouse mammary tumor virus
(MMTV) nucleocapsid protein p14. {ECO:0000269|PubMed:17020885,
ECO:0000269|PubMed:17259974}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16527742}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q99J72-1; Sequence=Displayed;
Name=2;
IsoId=Q99J72-2; Sequence=VSP_009832;
Name=3;
IsoId=Q99J72-3; Sequence=VSP_009831, VSP_009833;
Name=4;
IsoId=Q99J72-4; Sequence=VSP_009831;
Note=Lacks exon V. Found in cell line MDTF.;
-!- TISSUE SPECIFICITY: Expressed in spleen, node and lung.
{ECO:0000269|PubMed:12859895}.
-!- DOMAIN: The CMP/dCMP deaminase domain 1 confers deoxycytidine
deaminase activity, whereas the CMP/dCMP deaminase domain 2
mediates RNA-dependent oligomerization and virion incorporation.
{ECO:0000269|PubMed:17020885}.
-!- MISCELLANEOUS: Probable human APOBEC3G ortholog.
-!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH03314.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC31901.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=BAC34023.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; AK044394; BAC31901.1; ALT_INIT; mRNA.
EMBL; AK049998; BAC34023.1; ALT_INIT; mRNA.
EMBL; AC113595; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC003314; AAH03314.1; ALT_INIT; mRNA.
RefSeq; XP_017172295.1; XM_017316806.1. [Q99J72-3]
UniGene; Mm.284059; -.
UniGene; Mm.432615; -.
ProteinModelPortal; Q99J72; -.
SMR; Q99J72; -.
STRING; 10090.ENSMUSP00000105249; -.
iPTMnet; Q99J72; -.
PhosphoSitePlus; Q99J72; -.
MaxQB; Q99J72; -.
PaxDb; Q99J72; -.
PRIDE; Q99J72; -.
Ensembl; ENSMUST00000175714; ENSMUSP00000135027; ENSMUSG00000009585. [Q99J72-1]
Ensembl; ENSMUST00000175752; ENSMUSP00000135358; ENSMUSG00000009585. [Q99J72-4]
Ensembl; ENSMUST00000176325; ENSMUSP00000134838; ENSMUSG00000009585. [Q99J72-2]
Ensembl; ENSMUST00000177098; ENSMUSP00000135079; ENSMUSG00000009585. [Q99J72-3]
GeneID; 80287; -.
CTD; 80287; -.
MGI; MGI:1933111; Apobec3.
eggNOG; ENOG410JBA1; Eukaryota.
eggNOG; ENOG41119MS; LUCA.
GeneTree; ENSGT00530000062933; -.
HOGENOM; HOG000033755; -.
HOVERGEN; HBG050434; -.
InParanoid; Q99J72; -.
OMA; ITCYLTW; -.
OrthoDB; EOG091G0J2L; -.
PhylomeDB; Q99J72; -.
TreeFam; TF331356; -.
BRENDA; 3.5.4.1; 3474.
Reactome; R-MMU-72200; mRNA Editing: C to U Conversion.
Reactome; R-MMU-75094; Formation of the Editosome.
PRO; PR:Q99J72; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000009585; -.
CleanEx; MM_APOBEC3; -.
ExpressionAtlas; Q99J72; baseline and differential.
Genevisible; Q99J72; MM.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0047844; F:deoxycytidine deaminase activity; ISO:MGI.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0051607; P:defense response to virus; ISO:MGI.
GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0010529; P:negative regulation of transposition; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0050688; P:regulation of defense response to virus; IMP:MGI.
GO; GO:1903900; P:regulation of viral life cycle; IMP:MGI.
InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
InterPro; IPR013158; APOBEC_N.
InterPro; IPR002125; CMP_dCMP_dom.
InterPro; IPR016193; Cytidine_deaminase-like.
Pfam; PF08210; APOBEC_N; 2.
SUPFAM; SSF53927; SSF53927; 2.
PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 2.
PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 2.
1: Evidence at protein level;
Alternative splicing; Antiviral defense; Complete proteome; Cytoplasm;
Hydrolase; Immunity; Innate immunity; Metal-binding; Polymorphism;
Reference proteome; Repeat; Zinc.
CHAIN 1 440 DNA dC->dU-editing enzyme APOBEC-3.
/FTId=PRO_0000171772.
DOMAIN 49 165 CMP/dCMP-type deaminase 1.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
DOMAIN 249 368 CMP/dCMP-type deaminase 2.
{ECO:0000255|PROSITE-ProRule:PRU01083}.
ACT_SITE 84 84 Proton donor. {ECO:0000250}.
METAL 82 82 Zinc. {ECO:0000250}.
METAL 116 116 Zinc. {ECO:0000250}.
METAL 119 119 Zinc. {ECO:0000250}.
METAL 299 299 Zinc. {ECO:0000250}.
METAL 327 327 Zinc. {ECO:0000250}.
METAL 330 330 Zinc. {ECO:0000250}.
VAR_SEQ 209 241 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009831.
VAR_SEQ 420 440 SWGLQDLVNDFGNLQLGPPMS -> VRTTLLQGPAS (in
isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009832.
VAR_SEQ 420 440 SWGLQDLVNDFGNLQLGPPMS -> SRSHAS (in
isoform 3).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_009833.
VARIANT 31 31 L -> V (in cell line MDTF).
VARIANT 42 42 K -> E (in cell line MDTF).
VARIANT 45 46 GY -> PF (in cell line MDTF).
VARIANT 45 45 G -> R (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 48 49 KG -> ID (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 49 49 G -> K (in cell line MDTF; requires 2
nucleotide substitutions).
VARIANT 122 122 Q -> R (in cell line L1.2).
VARIANT 123 124 IV -> VL (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 123 123 I -> V (in cell line MDTF).
VARIANT 139 139 S -> F (in cell line MDTF).
VARIANT 145 150 VQDPET -> IRNPEN (in cell line MDTF).
VARIANT 145 146 VQ -> IR (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 150 151 TQ -> NQL (in cell line 3T3).
VARIANT 150 150 T -> N (in cell line L1.2).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 159 159 Q -> L (in cell line MDTF).
VARIANT 173 174 KK -> EE (in cell line MDTF).
VARIANT 192 192 R -> K (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 241 246 GRRMDP -> RRRVHL (in cell line 3T3).
VARIANT 244 246 MDP -> VHL. {ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 245 246 DP -> SL (in cell line MDTF).
VARIANT 259 259 Q -> L (in cell line MDTF).
VARIANT 269 270 RM -> GV (in cell line 3T3).
VARIANT 269 269 R -> G (in cell line L1.2).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 275 275 C -> F (in cell line MDTF).
VARIANT 280 280 Q -> W (in cell line MDTF; requires 2
nucleotide substitutions).
VARIANT 285 285 A -> E (in cell line MDTF).
VARIANT 295 307 Missing (in cell line MDTF).
VARIANT 317 317 T -> I (in cell lines L1.2 and 3T3).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
VARIANT 325 325 S -> G (in cell line EL4).
VARIANT 339 339 R -> K (in cell line MDTF).
VARIANT 392 392 N -> S (in cell line MDTF).
VARIANT 398 398 W -> R (in splenocytes).
VARIANT 405 406 II -> KT (in cell line MDTF).
VARIANT 410 410 T -> A (in cell line L1.2).
VARIANT 415 415 R -> C (in cell lines MDTF and 3T3).
VARIANT 415 415 R -> H (in cell line L1.2).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:16141072}.
MUTAGEN 84 84 E->A: Decrease in cytidine deaminase and
antiviral activity.
{ECO:0000269|PubMed:17020885}.
MUTAGEN 84 84 E->A: Decrease in cytidine deaminase and
antiviral activity; when associated with
A-301. {ECO:0000269|PubMed:17020885}.
MUTAGEN 301 301 E->A: Decrease in cytidine deaminase and
antiviral activity; when associated with
A-84. {ECO:0000269|PubMed:17020885}.
MUTAGEN 301 301 E->A: No effect on cytidine deaminase and
antiviral activity.
{ECO:0000269|PubMed:17020885}.
CONFLICT 6 6 L -> M (in Ref. 1; BAC31901 and 4;
AAH03314). {ECO:0000305}.
CONFLICT 214 214 S -> P (in Ref. 1; BAC31901 and 4;
AAH03314). {ECO:0000305}.
CONFLICT 238 238 W -> C (in Ref. 1; BAC31901 and 4;
AAH03314). {ECO:0000305}.
CONFLICT 241 241 G -> R (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 440 AA; 52213 MW; AA0DA7AC616252E9 CRC64;
MQPQRLGPRA GMGPFCLGCS HRKCYSPIRN LISQETFKFH FKNLGYAKGR KDTFLCYEVT
RKDCDSPVSL HHGVFKNKDN IHAEICFLYW FHDKVLKVLS PREEFKITWY MSWSPCFECA
EQIVRFLATH HNLSLDIFSS RLYNVQDPET QQNLCRLVQE GAQVAAMDLY EFKKCWKKFV
DNGGRRFRPW KRLLTNFRYQ DSKLQEILRP CYISVPSSSS STLSNICLTK GLPETRFWVE
GRRMDPLSEE EFYSQFYNQR VKHLCYYHRM KPYLCYQLEQ FNGQAPLKGC LLSEKGKQHA
EILFLDKIRS MELSQVTITC YLTWSPCPNC AWQLAAFKRD RPDLILHIYT SRLYFHWKRP
FQKGLCSLWQ SGILVDVMDL PQFTDCWTNF VNPKRPFWPW KGLEIISRRT QRRLRRIKES
WGLQDLVNDF GNLQLGPPMS


Related products :

Catalog number Product name Quantity
18-661-15176 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
18-003-42391 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.1 mg Protein A
18-003-42392 DNA dC->dU-editing enzyme APOBEC-3G - EC 3.5.4.-; APOBEC-related cytidine deaminase; ARCD; APOBEC-related protein; ARP-9; CEM15; CEM-15 Polyclonal 0.05 mg Aff Pur
E2466h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E2465h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3558h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E2464h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3557h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3559h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3561h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3562h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E2463h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
E3560h Human Apolipoprotein B mRNA Editing Enzyme Catalyt 96T
18-003-43623 Apolipoprotein B mRNA editing enzyme. catalytic polypeptide-like 2 variant - N_A Polyclonal 0.1 mg Protein A
APOBEC3G APOBEC3D Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3D
201-20-0378 APOBEC2{apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2}rabbit.pAb 0.1ml
201-20-6771 APOBEC3C{apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C}mouse.mAb 0.1ml
201-20-0379 APOBEC3C{apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C}rabbit.pAb 0.1ml
APOC1 APOBEC3H Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3H
APOBEC3B APOBEC2 Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 2
APOBEC3C APOBEC3A Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3A
APOBEC3D APOBEC3B Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3B
APOBEC3F APOBEC3C Gene apolipoprotein B mRNA editing enzyme, catalytic polypeptide-like 3C


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur