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

Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein pp21; Protein p3; Protein p8; Protein n; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase); Protease (EC 3.4.23.-); Reverse transcriptase/ribonuclease H (RT) (EC 2.7.7.49) (EC 2.7.7.7) (EC 3.1.26.4); Integrase (IN) (EC 2.7.7.-) (EC 3.1.-.-)]

 POL_MMTVC               Reviewed;        1755 AA.
P11283; Q9IZT3;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
11-JAN-2011, sequence version 2.
10-MAY-2017, entry version 90.
RecName: Full=Gag-Pro-Pol polyprotein;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein pp21;
Contains:
RecName: Full=Protein p3;
Contains:
RecName: Full=Protein p8;
Contains:
RecName: Full=Protein n;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein-dUTPase;
Short=NC-dUTPase;
Contains:
RecName: Full=Protease;
EC=3.4.23.-;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49;
EC=2.7.7.7;
EC=3.1.26.4;
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000305|PubMed:24124581};
EC=3.1.-.- {ECO:0000305|PubMed:24124581};
Name=gag-pro-pol;
Mouse mammary tumor virus (strain C3H) (MMTV).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11759;
NCBI_TaxID=10090; Mus musculus (Mouse).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=10982330; DOI=10.1128/JVI.74.19.8876-8883.2000;
Hook L.M., Agafonova Y., Ross S.R., Turner S.J., Golovkina T.V.;
"Genetics of mouse mammary tumor virus-induced mammary tumors: linkage
of tumor induction to the gag gene.";
J. Virol. 74:8876-8883(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC RNA] OF 359-591 AND 857-970, AND
RIBOSOMAL FRAMESHIFT.
PubMed=3035577; DOI=10.1073/pnas.84.12.4298;
Jacks T., Townsley K., Varmus H.E., Majors J.;
"Two efficient ribosomal frameshifting events are required for
synthesis of mouse mammary tumor virus gag-related polyproteins.";
Proc. Natl. Acad. Sci. U.S.A. 84:4298-4302(1987).
[3]
PROTEIN SEQUENCE OF 2-58; 65-116; 194-218; 227-241; 251-252; 270-276
AND 362-591, PROTEOLYTIC PROCESSING OF POLYPROTEIN, AND MYRISTOYLATION
AT GLY-2.
PubMed=2542570;
Hizi A., Henderson L.E., Copeland T.D., Sowder R.C., Krutzsch H.C.,
Oroszlan S.;
"Analysis of gag proteins from mouse mammary tumor virus.";
J. Virol. 63:2543-2549(1989).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=1331110;
Menendez-Arias L., Young M., Oroszlan S.;
"Purification and characterization of the mouse mammary tumor virus
protease expressed in Escherichia coli.";
J. Biol. Chem. 267:24134-24139(1992).
[5]
RIBOSOMAL FRAMESHIFT, SUBUNIT, AND CHARACTERIZATION OF NC-DUTPASE.
PubMed=8091672; DOI=10.1006/viro.1994.1547;
Bergman A.C., Bjornberg O., Nord J., Nyman P.O., Rosengren A.M.;
"The protein p30, encoded at the gag-pro junction of mouse mammary
tumor virus, is a dUTPase fused with a nucleocapsid protein.";
Virology 204:420-424(1994).
[6]
FUNCTION (INTEGRASE).
PubMed=24124581; DOI=10.1371/journal.pone.0076638;
Ballandras-Colas A., Naraharisetty H., Li X., Serrao E., Engelman A.;
"Biochemical characterization of novel retroviral integrase
proteins.";
PLoS ONE 8:E76638-E76638(2013).
-!- FUNCTION: Matrix protein p10: Matrix protein. {ECO:0000250}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein. Binds to
single-stranded DNA (By similarity). {ECO:0000250}.
-!- FUNCTION: Capsid protein p27: capsid protein. {ECO:0000250}.
-!- FUNCTION: NC-dUTPase has dUTPase activity, thereby preventing
incorporation of uracil into DNA.
-!- FUNCTION: The aspartyl protease mediates proteolytic cleavages of
Gag, Gag-Pro and Gag-Pro-Pol polyproteins during or shortly after
the release of the virion from the plasma membrane. Cleavages take
place as an ordered, step-wise cascade to yield mature proteins.
This process is called maturation. Displays maximal activity
during the budding process just prior to particle release from the
cell (By similarity). {ECO:0000250}.
-!- FUNCTION: RT is a multifunctional enzyme that converts the viral
dimeric RNA genome into dsDNA in the cytoplasm, shortly after
virus entry into the cell. This enzyme displays a DNA polymerase
activity that can copy either DNA or RNA templates, and a
ribonuclease H (RNase H) activity that cleaves the RNA strand of
RNA-DNA heteroduplexes in a partially processive 3' to 5'
endonucleasic mode. Conversion of viral genomic RNA into dsDNA
requires many steps. A tRNA binds to the primer-binding site (PBS)
situated at the 5' end of the viral RNA. RT uses the 3' end of the
tRNA primer to perform a short round of RNA-dependent minus-strand
DNA synthesis. The reading proceeds through the U5 region and ends
after the repeated (R) region which is present at both ends of
viral RNA. The portion of the RNA-DNA heteroduplex is digested by
the RNase H, resulting in a ssDNA product attached to the tRNA
primer. This ssDNA/tRNA hybridizes with the identical R region
situated at the 3' end of viral RNA. This template exchange, known
as minus-strand DNA strong stop transfer, can be either intra- or
intermolecular. RT uses the 3' end of this newly synthesized short
ssDNA to perform the RNA-dependent minus-strand DNA synthesis of
the whole template. RNase H digests the RNA template except for a
polypurine tract (PPT) situated at the 5' end of the genome. It is
not clear if both polymerase and RNase H activities are
simultaneous. RNase H probably can proceed both in a polymerase-
dependent (RNA cut into small fragments by the same RT performing
DNA synthesis) and a polymerase-independent mode (cleavage of
remaining RNA fragments by free RTs). Secondly, RT performs DNA-
directed plus-strand DNA synthesis using the PPT that has not been
removed by RNase H as primers. PPT and tRNA primers are then
removed by RNase H. The 3' and 5' ssDNA PBS regions hybridize to
form a circular dsDNA intermediate. Strand displacement synthesis
by RT to the PBS and PPT ends produces a blunt ended, linear dsDNA
copy of the viral genome that includes long terminal repeats
(LTRs) at both ends (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=RT polymerase domain binds 2 magnesium ions. {ECO:0000250};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Note=Magnesium ions are required for NC-dUTPase activity.;
-!- SUBUNIT: NC-dUTPase is a homotrimer. {ECO:0000269|PubMed:8091672}.
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion {ECO:0000305}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein-dUTPase: Virion
{ECO:0000305}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Comment=Translation results in the formation of the Gag-Pro.
Ribosomal frameshifting at the gag-pro/pol genes boundary
produces the Gag-Pro-Pol polyprotein.
{ECO:0000269|PubMed:3035577, ECO:0000269|PubMed:8091672};
Name=Gag-Pro-Pol polyprotein;
IsoId=P11283-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting between gag-pro and
pro-pol.;
Name=Gag-Pro polyprotein;
IsoId=Q9IZT2-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.;
Name=Gag polyprotein;
IsoId=P11284-1; Sequence=External;
Note=Produced by conventional translation.;
-!- PTM: Specific enzymatic cleavages in vivo yield mature proteins.
{ECO:0000269|PubMed:1331110, ECO:0000269|PubMed:2542570}.
-!- PTM: p10 is myristoylated. {ECO:0000269|PubMed:2542570}.
-!- MISCELLANEOUS: The reverse transcriptase is an error-prone enzyme
that lacks a proof-reading function. High mutations rate is a
direct consequence of this characteristic. RT also displays
frequent template swiching leading to high recombination rate.
Recombination mostly occurs between homologous regions of the two
copackaged RNA genomes. If these two RNA molecules derive from
different viral strains, reverse transcription will give rise to
highly recombinated proviral DNAs. {ECO:0000255|PROSITE-
ProRule:PRU00405}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF228552; AAF31474.1; -; Genomic_DNA.
EMBL; M16766; AAA66623.1; -; Genomic_RNA.
EMBL; M16766; AAA66625.1; -; Genomic_RNA.
PIR; B29029; B29029.
ProteinModelPortal; P11283; -.
SMR; P11283; -.
OrthoDB; VOG09000135; -.
Proteomes; UP000006540; Genome.
GO; GO:0019013; C:viral nucleocapsid; IEA:UniProtKB-KW.
GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0003964; F:RNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IEA:UniProtKB-EC.
GO; GO:0039660; F:structural constituent of virion; IEA:UniProtKB-KW.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW.
GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW.
GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW.
GO; GO:0044826; P:viral genome integration into host DNA; IEA:UniProtKB-KW.
CDD; cd05482; HIV_retropepsin_like; 1.
CDD; cd07557; trimeric_dUTPase; 1.
Gene3D; 1.10.10.200; -; 1.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR033704; dUTPase_trimeric.
InterPro; IPR000721; Gag_p24.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR017856; Integrase_Zn-bd_dom-like_N.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom.
InterPro; IPR034170; Retropepsin-like_cat_dom.
InterPro; IPR018061; Retropepsins.
InterPro; IPR008916; Retrov_capsid_C.
InterPro; IPR008919; Retrov_capsid_N.
InterPro; IPR010999; Retrovr_matrix.
InterPro; IPR012337; RNaseH-like_dom.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR000477; RT_dom.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
Pfam; PF00692; dUTPase; 1.
Pfam; PF02337; Gag_p10; 1.
Pfam; PF00607; Gag_p24; 1.
Pfam; PF00552; IN_DBD_C; 1.
Pfam; PF02022; Integrase_Zn; 1.
Pfam; PF00075; RNase_H; 1.
Pfam; PF00665; rve; 1.
Pfam; PF00077; RVP; 1.
Pfam; PF00078; RVT_1; 1.
Pfam; PF06817; RVT_thumb; 1.
Pfam; PF00098; zf-CCHC; 1.
ProDom; PD004265; B_retro_matrix_N; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF46919; SSF46919; 1.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF51283; SSF51283; 1.
SUPFAM; SSF53098; SSF53098; 2.
SUPFAM; SSF57756; SSF57756; 2.
PROSITE; PS50175; ASP_PROT_RETROV; 1.
PROSITE; PS00141; ASP_PROTEASE; 1.
PROSITE; PS50994; INTEGRASE; 1.
PROSITE; PS51027; INTEGRASE_DBD; 1.
PROSITE; PS50879; RNASE_H; 1.
PROSITE; PS50878; RT_POL; 1.
PROSITE; PS50158; ZF_CCHC; 1.
PROSITE; PS50876; ZF_INTEGRASE; 1.
1: Evidence at protein level;
Aspartyl protease; Capsid protein; Complete proteome;
Direct protein sequencing; DNA integration; DNA recombination;
DNA-binding; DNA-directed DNA polymerase; Endonuclease; Hydrolase;
Lipoprotein; Magnesium; Metal-binding; Multifunctional enzyme;
Myristate; Nuclease; Nucleotide-binding; Nucleotidyltransferase;
Phosphoprotein; Protease; Reference proteome; Repeat;
Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
Viral genome integration; Viral matrix protein; Viral nucleoprotein;
Virion; Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000250}.
CHAIN 2 1755 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000125493.
CHAIN 2 99 Matrix protein p10.
/FTId=PRO_0000403612.
CHAIN 100 195 Phosphorylated protein pp21.
/FTId=PRO_0000403613.
CHAIN 196 228 Protein p3.
/FTId=PRO_0000403614.
CHAIN 229 252 Protein p8. {ECO:0000255}.
/FTId=PRO_0000403615.
CHAIN 253 269 Protein n.
/FTId=PRO_0000403616.
CHAIN 270 496 Capsid protein p27.
/FTId=PRO_0000403617.
CHAIN 497 745 Nucleocapsid protein-dUTPase.
{ECO:0000255}.
/FTId=PRO_0000403618.
CHAIN 746 833 Protease. {ECO:0000255}.
/FTId=PRO_0000403619.
CHAIN 834 1437 Reverse transcriptase/ribonuclease H.
{ECO:0000255}.
/FTId=PRO_0000403620.
CHAIN 1438 1755 Integrase. {ECO:0000255}.
/FTId=PRO_0000403621.
DOMAIN 766 841 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 905 1093 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1307 1435 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1490 1647 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 525 542 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 552 569 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1436 1477 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1653 1702 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
COMPBIAS 278 281 Poly-Asp.
COMPBIAS 716 719 Poly-Leu.
ACT_SITE 771 771 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 970 970 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1045 1045 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1046 1046 Magnesium; catalytic; for reverse
transcriptase activity. {ECO:0000250}.
METAL 1316 1316 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1346 1346 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1366 1366 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1429 1429 Magnesium; catalytic; for RNase H
activity. {ECO:0000250}.
METAL 1501 1501 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
METAL 1558 1558 Magnesium; catalytic; for integrase
activity. {ECO:0000250}.
SITE 99 100 Cleavage; by viral protease.
{ECO:0000250}.
SITE 195 196 Cleavage; by viral protease.
{ECO:0000250}.
SITE 228 229 Cleavage; by viral protease.
{ECO:0000250}.
SITE 252 253 Cleavage; by viral protease.
{ECO:0000250}.
SITE 269 270 Cleavage; by viral protease.
{ECO:0000250}.
SITE 496 497 Cleavage; by viral protease.
{ECO:0000250}.
SITE 745 746 Cleavage; by viral protease.
{ECO:0000250}.
SITE 833 834 Cleavage; by viral protease.
{ECO:0000250}.
SITE 1437 1438 Cleavage; by viral protease.
{ECO:0000250}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250}.
VARIANT 523 523 E -> K.
CONFLICT 857 860 SQDL -> FTGF (in Ref. 2; AAA66625).
{ECO:0000305}.
CONFLICT 867 867 S -> T (in Ref. 2; AAA66625).
{ECO:0000305}.
CONFLICT 952 952 P -> L (in Ref. 2; AAA66625).
{ECO:0000305}.
SEQUENCE 1755 AA; 197329 MW; 0E99A2ADD96823A4 CRC64;
MGVSGSKGQK LFVSVLQRLL SERGLHVKES SAIEFYQFLI KVSPWFPEEG GLNLQDWKRV
GREMKKYAAE HGTDSIPKQA YPIWLQLREI LTEQSDLVLL SAEAKSVTEE ELEEGLTGLL
SASSQEKTYG TRGTAYAEID TEVDKLSEHI YDEPYEEKEK ADKNEEKDHV RKVKKIVQRK
ENSEHKRKEK DQKAFLATDW NNDDLSPEDW DDLEEQAAHY HDDDELILPV KRKVDKKKPL
ALRRKPLPPV GFAGAMAEAR EKGDLTFTFP VVFMGESDDD DTPVWEPLPL KTLKELQSAV
RTMGPSAPYT LQVVDMVASQ WLTPSDWHQT ARATLSPGDY VLWRTEYEEK SKETVQKTAG
KRKGKVSLDM LLGTGQFLSP SSQIKLSKDV LKDVTTNAVL AWRAIPPPGV KKTVLAGLKQ
GNEESYETFI SRLEEAVYRM MPRGEGSDIL IKQLAWENAN SLCQDLIRPM RKTGTMQDYI
RACLDASPAV VQGMAYAAAM RGQKYSTFVK QTYGGGKGGQ GSEGPVCFSC GKTGHIKRDC
KEEKGSKRAP PGLCPRCKKG YHWKSECKSK FDKDGNPLPP LETNAENSKN LVKGQSPSPT
QKGDKGKDSG LNPEAPPFTI HDLPRGTPGS AGLDLSSQKD LILSLEDGVS LVPTLVKGTL
PEGTTGLIIG RSSNYKKGLE VLPGVIDSDF QGEIKVMVKA AKNAVIIHKG ERIAQLLLLP
YLKLPNPIIK EERGSEGFGS TSHVHWVQEI SDSRPMLHIS LNGRRFLGLL DTGADKTCIA
GRDWPANWPI HQTESSLQGL GMACGVARSS QPLRWQHEDK SGIIHPFVIP TLPFTLWGRD
IMKEIKVRLM TDSPDDSQDL MIGAIESNLF ADQISWKSDQ PVWLNQWPLK QEKLQALQQL
VTEQLQLGHL EESNSPWNTP VFVIKKKSGK WRLLQDLRAV NATMHDMGAL QPGLPSPVAV
PKGWEIIIID LQDCFFNIKL HPEDCKRFAF SVPSPNFKRP YQRFQWKVLP QGMKNSPTLC
QKFVDKAILT VRDKYQDSYI VHYMDDILLA HPSRSIVDEI LTSMIQALNK HGLVVSTEKI
QKYDNLKYLG THIQGDAVSY QKLQIRTDKL RTLNDFQKLL GNINWIRPFL KLTTGELKPL
FEILNGDSNP ISIRKLTPEA CKALQLVNER LSIARVKRLD LSRPWSLCIL KTEYTPTACL
WQNGVLEWIH LPHISPKVIT PYDIFCTQLI IKGRHRSKEL FSKDPDYIVV PYTKVQFDLL
LQEKEDWPIS LLGFLGEVHF HLPKDPLLTF TLQTAIIFPH MTSTTPLEKG IVIFTDGSAN
GRSVTYIQGR EPIIKENTQN TAQQAEIVAV ITAFEEVSQS FNLYTDSKYV TGLFPEIETA
TLSPRTKIYT ELRHLQRLIH KRQEKFYIGH IRGHTGLPGP LAQGNAYADS LTRILTALES
AQESHALHHQ NAAALRFQFH ITREQAREIV KLCPNCPDWG HAPQLGVNPR GLKPRVLWQM
DVTHVSEFGK LKYVHVTVDT YSHFTFATAR TGEATKDVLQ HLAQSFAYMG FPQKIKTDNA
PAYVSRSIQE FLARWKISHV TGIPYNPQGQ AIVERTHQNI KAQLNKLQKA GKYYTPHHLL
AHALFVLNHV NMDNQGHTAA ERHWGPISAD PKPMVMWKDL LAGSWKGPDV LITAGRGYAC
VFPQDAETPI WVPDRFIRPF TERKEATPTP GTAEKTPPRD EKDQQKSPED ESSPHQREDG
LATSAGVNLR SGGGS


Related products :

Catalog number Product name Quantity
orb90082 Thermostable dUTPase protein Thermostable dUTPase (pyrococcus fruriosus) maximizes the efficiency of high-fidelity PCR (using proofreading DNA polymerases). It removes contaminating dUTP present in PC 500 IU
OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
SCH-OBT1904X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa340_390), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Appli 1 mg
OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
SCH-OBT1905X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , Applicat 1 mg
SCH-OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
SCH-OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
OBT1906 RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 0.1 mg
OBT1906X RECOMBINANT SARS NUCLEOCAPSID PROTEIN (aa1_49 192_220), Product Type Recombinant Protein, Specificity SARS NUCLEOCAPSID PROTEIN , Target Species Viral, Host N_A, Format Rec. Protein, Isotypes , 1 mg
orb81720 HIV-1 pol Integrase protein The E.coli derived 26 kDa recombinant protein is non-glycosylated polypeptide chain, containing the HIV-1 immunodominant regions from the pol protein (intergrase) and fused 100
orb81721 HIV-1 p31 Integrase protein The E.coli derived recombinant protein is non-glycosylated polypeptide chain, containing the HIV-1 immunodominant regions from the p31 protein (intergrase) 9-289 amino acid 100
EIAAB12944 Ectoderm-neural cortex protein 1,ENC1,ENC-1,Homo sapiens,Human,Kelch-like protein 37,KLHL37,NRPB,Nuclear matrix protein NRP_B,p53-induced gene 10 protein,PIG10
orb81561 Hepatitis Virus Nucleocapsid (core) Genotype-4 protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81556 Hepatitis Virus Nucleocapsid (core) Genotype-1b protein The E.coli derived recombinant multimer protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fus 100
orb81559 Hepatitis Virus Nucleocapsid (core) Genotype-3a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81557 Hepatitis Virus Nucleocapsid (core) Genotype-2a protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81558 Hepatitis Virus Nucleocapsid (core) Genotype-2b protein The E.coli derived recombinant protein contains the HCV core nucleocapsid immunodominant regions, amino acids 2-119. The protein is fused to GST 100
orb81567 Hepatitis Virus Nucleocapsid (core) (105-302) protein The E.coli derived recombinant protein from E1 region contains the HCV core nucleocapsid immunodominant regions, amino acids 105-302. The protein 100
orb90082 Thermostable dUTPase protein Enzymes 500 IU
E1639p ELISA kit 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
U1639p CLIA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
orb81536 SARS Associated Coronavirus Matrix protein The E.coli derived 30kDa recombinant protein contains the Matrix protein 182-216 amino acids immunodominant regions. For research use only. 100
E1639p ELISA 22 kDa extracellular matrix protein,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,Pig,Sus scrofa,TRAMP,Tyrosine-rich acidic matrix protein 96T
25-986 LECT1 is a glycosylated transmembrane protein that is cleaved to form a mature, secreted protein. The mature protein promotes chondrocyte growth and inhibits angiogenesis. The mature protein likely pl 0.05 mg
U1639b CLIA 22 kDa extracellular matrix protein,Bos taurus,Bovine,Dermatan sulfate proteoglycan-associated protein 22K,Dermatopontin,DPT,TRAMP,Tyrosine-rich acidic matrix protein 96T


 

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