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Gag-Pro-Pol polyprotein [Cleaved into: Matrix protein p10; Phosphorylated protein; p12; Capsid protein p27; Nucleocapsid protein-dUTPase (NC-dUTPase) (EC 3.6.1.23); Protease 17 kDa (EC 3.4.23.-); Protease 13 kDa (EC 3.4.23.-); G-patch peptide; 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_JSRV                Reviewed;        1726 AA.
P31623;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
28-FEB-2018, sequence version 2.
20-JUN-2018, entry version 107.
RecName: Full=Gag-Pro-Pol polyprotein;
Contains:
RecName: Full=Matrix protein p10;
Contains:
RecName: Full=Phosphorylated protein;
Contains:
RecName: Full=p12;
Contains:
RecName: Full=Capsid protein p27;
Contains:
RecName: Full=Nucleocapsid protein-dUTPase;
Short=NC-dUTPase;
EC=3.6.1.23 {ECO:0000250|UniProtKB:P11283};
Contains:
RecName: Full=Protease 17 kDa {ECO:0000250|UniProtKB:P07572};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=Protease 13 kDa {ECO:0000250|UniProtKB:P07572};
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=G-patch peptide {ECO:0000250|UniProtKB:P07572};
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H;
Short=RT;
EC=2.7.7.49 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=2.7.7.7 {ECO:0000255|PROSITE-ProRule:PRU00405};
EC=3.1.26.4 {ECO:0000255|PROSITE-ProRule:PRU00408};
Contains:
RecName: Full=Integrase;
Short=IN;
EC=2.7.7.- {ECO:0000250|UniProtKB:P11283};
EC=3.1.-.- {ECO:0000250|UniProtKB:P11283};
Name=pol;
Sheep pulmonary adenomatosis virus (Jaagsiekte sheep retrovirus)
(JSRV).
Viruses; Ortervirales; Retroviridae; Orthoretrovirinae;
Betaretrovirus.
NCBI_TaxID=11746;
NCBI_TaxID=9940; Ovis aries (Sheep).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
STRAIN=JSRV-SA;
PubMed=1629959;
York D.F., Vigne R., Verwoerd D.W., Querat G.;
"Nucleotide sequence of the jaagsiekte retrovirus, an exogenous and
endogenous type D and B retrovirus of sheep and goats.";
J. Virol. 66:4930-4939(1992).
[2]
RIBOSOMAL FRAMESHIFT.
PubMed=24298557; DOI=10.1155/2013/984028;
Huang X., Cheng Q., Du Z.;
"A genome-wide analysis of RNA pseudoknots that stimulate efficient -1
ribosomal frameshifting or readthrough in animal viruses.";
Biomed. Res. Int. 2013:984028-984028(2013).
[3]
REVIEW (INTEGRASE).
PubMed=28458055; DOI=10.1016/j.sbi.2017.04.005;
Engelman A.N., Cherepanov P.;
"Retroviral intasomes arising.";
Curr. Opin. Struct. Biol. 47:23-29(2017).
-!- FUNCTION: Matrix protein p10: Matrix protein.
{ECO:0000250|UniProtKB:P07572}.
-!- FUNCTION: Nucleocapsid protein p14: Nucleocapsid protein.
{ECO:0000250|UniProtKB:P07572}.
-!- FUNCTION: Capsid protein p27: Capsid protein.
{ECO:0000250|UniProtKB:P07572}.
-!- FUNCTION: Protease 17 kDa: The aspartyl protease mediates
proteolytic cleavages of Gag and Gag-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. {ECO:0000250|UniProtKB:P07572,
ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: Protease 13 kDa: The aspartyl protease mediates
proteolytic cleavages of Gag and Gag-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. {ECO:0000250|UniProtKB:P07572,
ECO:0000255|PROSITE-ProRule:PRU00275}.
-!- FUNCTION: G-patch peptide: Enhances the activity of the reverse
transcriptase. May be part of the mature RT.
{ECO:0000250|UniProtKB:P07572}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H: 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 perfom 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 perfom 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.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- FUNCTION: Integrase: Catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. {ECO:0000305|PubMed:28458055}.
-!- 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}.
-!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate.
{ECO:0000250|UniProtKB:P07570}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000255|PROSITE-ProRule:PRU00405};
Note=The RT polymerase active site binds 2 magnesium ions.
{ECO:0000255|PROSITE-ProRule:PRU00405};
-!- SUBUNIT: Protease 17 kDa: Homodimer. Reverse
transcriptase/ribonuclease H: Interacts with the G-patch peptide.
G-patch peptide: Interacts with the reverse
transcriptase/ribonuclease H. Nucleocapsid protein-dUTPase:
Homotrimer. {ECO:0000250|UniProtKB:P07570}.
-!- SUBCELLULAR LOCATION: Matrix protein p10: Virion
{ECO:0000250|UniProtKB:P07572}.
-!- SUBCELLULAR LOCATION: Capsid protein p27: Virion
{ECO:0000250|UniProtKB:P07572}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein-dUTPase: Virion
{ECO:0000250|UniProtKB:P07572}.
-!- SUBCELLULAR LOCATION: Protease 13 kDa: Virion
{ECO:0000250|UniProtKB:P07572}.
-!- SUBCELLULAR LOCATION: Protease 17 kDa: Virion
{ECO:0000250|UniProtKB:P07572}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Name=Gag-Pro-Pol polyprotein;
IsoId=P31623-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshiftings between gag-pro and
pro-pol. {ECO:0000305|PubMed:24298557};
Name=Gag-Pro polyprotein;
IsoId=P31625-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting between gag-pro.
{ECO:0000305|PubMed:24298557};
Name=Gag polyprotein;
IsoId=P31622-1; Sequence=External;
Note=Produced by conventional translation.
{ECO:0000305|PubMed:24298557};
-!- DOMAIN: Gag polyprotein: Late-budding domains (L domains) are
short sequence motifs essential for viral particle release. They
can occur individually or in close proximity within structural
proteins. They interacts with sorting cellular proteins of the
multivesicular body (MVB) pathway. Most of these proteins are
class E vacuolar protein sorting factors belonging to ESCRT-I,
ESCRT-II or ESCRT-III complexes. Gag-p12 contains two L domains: a
PTAP/PSAP motif which interacts with the UEV domain of TSG101, and
a PPXY motif which binds to the WW domains of the ubiquitin ligase
NEDD4. Gag-p27 contains one L domain: a PTAP/PSAP motif which
interacts with the UEV domain of TSG101.
{ECO:0000250|UniProtKB:P07572}.
-!- DOMAIN: Protease 17 kDa: The glycine-rich G-patch domain (GPD) is
present at the C-terminus of the protease from which it is then
detached by the protease itself. {ECO:0000250|UniProtKB:P07572}.
-!- PTM: Protease 17 kDa: Released by autocatalytic processing. The
protease can undergo further autoprocessing to yield 2 shorter but
enzymatically active forms of 12 kDa and 13 kDa.
{ECO:0000250|UniProtKB:P07572}.
-!- PTM: Gag-Pro-Pol polyprotein: Myristoylated. Myristoylation of the
matrix (MA) domain mediates the transport and binding of Gag
polyproteins to the host plasma membrane and is required for the
assembly of viral particles. {ECO:0000250|UniProtKB:P10258}.
-!- PTM: Gag-Pro-Pol polyprotein: Specific enzymatic cleavages in vivo
yield mature proteins. {ECO:0000250|UniProtKB:P07572}.
-!- MISCELLANEOUS: Reverse transcriptase/ribonuclease H: 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}.
-!- SIMILARITY: Belongs to the retroviral Pol polyprotein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA89182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M80216; AAA89182.1; ALT_INIT; Genomic_RNA.
PIR; C42740; GNMVJA.
RefSeq; NP_041186.1; NC_001494.1.
ProteinModelPortal; P31623; -.
GeneID; 1490020; -.
KEGG; vg:1490020; -.
OrthoDB; VOG090000RG; -.
Proteomes; UP000007215; 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:0004170; F:dUTP diphosphatase activity; IEA:UniProtKB-EC.
GO; GO:0003723; F:RNA 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; 1.10.150.490; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.30.30.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 2.70.40.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003322; B_retro_matrix.
InterPro; IPR038124; B_retro_matrix_sf.
InterPro; IPR029054; dUTPase-like.
InterPro; IPR036157; dUTPase-like_sf.
InterPro; IPR033704; dUTPase_trimeric.
InterPro; IPR000467; G_patch_dom.
InterPro; IPR000721; Gag_p24.
InterPro; IPR017856; Integrase-like_N.
InterPro; IPR036862; Integrase_C_dom_sf_retrovir.
InterPro; IPR001037; Integrase_C_retrovir.
InterPro; IPR001584; Integrase_cat-core.
InterPro; IPR003308; Integrase_Zn-bd_dom_N.
InterPro; IPR001995; Peptidase_A2_cat.
InterPro; IPR021109; Peptidase_aspartic_dom_sf.
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_sf.
InterPro; IPR002156; RNaseH_domain.
InterPro; IPR036397; RNaseH_sf.
InterPro; IPR000477; RT_dom.
InterPro; IPR010661; RVT_thumb.
InterPro; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF00692; dUTPase; 1.
Pfam; PF01585; G-patch; 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; SM00443; G_patch; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF46919; SSF46919; 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; PS50174; G_PATCH; 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.
3: Inferred from homology;
Aspartyl protease; Complete proteome; DNA integration;
DNA recombination; DNA-binding; DNA-directed DNA polymerase;
Endonuclease; Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Protease; Repeat; Ribosomal frameshifting; RNA-binding;
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|UniProtKB:P07572}.
CHAIN 2 1726 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000125490.
CHAIN 2 99 Matrix protein p10.
/FTId=PRO_0000443130.
CHAIN 100 167 Phosphorylated protein.
/FTId=PRO_0000443131.
CHAIN 168 256 p12.
/FTId=PRO_0000443132.
CHAIN 257 477 Capsid protein p27.
/FTId=PRO_0000443133.
CHAIN 478 713 Nucleocapsid protein-dUTPase.
/FTId=PRO_0000443134.
CHAIN 714 865 Protease 17 kDa.
/FTId=PRO_0000443135.
CHAIN 714 831 Protease 13 kDa.
/FTId=PRO_0000443136.
PEPTIDE 832 865 G-patch peptide.
/FTId=PRO_0000443137.
CHAIN 866 1446 Reverse transcriptase/ribonuclease H.
/FTId=PRO_0000434769.
CHAIN 1447 1726 Integrase.
/FTId=PRO_0000434770.
DOMAIN 734 810 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 821 866 G-patch. {ECO:0000255|PROSITE-
ProRule:PRU00092}.
DOMAIN 911 1099 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1313 1444 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1500 1659 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 507 524 CCHC-type. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 1446 1487 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00450}.
DNA_BIND 1665 1714 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
MOTIF 202 205 PTAP/PSAP motif. {ECO:0000305}.
MOTIF 208 211 PPXY motif. {ECO:0000305}.
MOTIF 287 290 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P10258}.
COMPBIAS 121 127 Poly-Pro. {ECO:0000255}.
COMPBIAS 202 228 Pro-rich. {ECO:0000255|PROSITE-
ProRule:PRU00015}.
ACT_SITE 739 739 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 976 976 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1051 1051 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1052 1052 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1322 1322 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1351 1351 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1371 1371 Magnesium; for RNase H activity.
{ECO:0000255|PROSITE-ProRule:PRU00408}.
METAL 1436 1436 Magnesium. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1511 1511 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1568 1568 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1604 1604 Magnesium; catalytic; for integrase
activity. {ECO:0000250|UniProtKB:P03354}.
SITE 99 100 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 256 257 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 477 478 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07567}.
SITE 713 714 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07572}.
SITE 831 832 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07572}.
SITE 865 866 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P07572}.
SITE 1446 1447 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03365}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000250|UniProtKB:P11283}.
SEQUENCE 1726 AA; 193421 MW; ACA8108A7C6A1A5B CRC64;
MGHTHSRQLF VHMLSVMLKH RGITVSKTKL INFLSFIEEV CPWFPREGTV NLETWKKVGE
QIRTHYTLHG PEKVPVETLS FWTLIRDCLD FDNDELKRLG NLLKQEEDPL HTPDSVPSYD
PPPPPPPSLK MHPSDNDDSL SSTDEAELDE EAAKYHQEDW GFLAQEKGAL TSKDELVECF
KNLTIALQNA GIQLPSNNNT FPSAPPFPPA YTPTVMAGLD PPPGFPPPSK HMSPLQKALR
QAQRLGEVVS DFSLAFPVFE NNNQRYYESL PFKQLKELKI ACSQYGPTAP FTIAMIESLG
TQALPPNDWK QTARACLSGG DYLLWKSEFF EQCARIADVN RQQGIQTSYE MLIGEGPYQA
TDTQLNFLPG AYAQISNAAR QAWKKLPSSS TKTEDLSKVR QGPDEPYQDF VARLLDTIGK
IMSDEKAGMV LAKQLAFENA NSACQAALRP YRKKGDLSDF IRICADIGPS YMQGIAMAAA
LQGKSIKEVL FQQQARNKKG LQKSGNSGCF VCGQPGHRAA VCPQKHQTSV NTPNLCPRCK
KGKHWARDCR SKTDVQGNPL PPVSGNLGEG PAPGPETMLW GNTAGSKRTI ADLCRATRGS
AGLDLCATSY TVLTPEMGVQ TLATGVFGPL PPGTVGLLLG RSSASLKGIL IHPGVIDSDY
TGEIKILASA PNKIIVINAG QRIAQLLLVP LVIQGKTINR DRQDKGFGSS DAYWVQNVTE
ARPELELRIN ANFFRGVLDT GADISVISDK YWPTTWPKQM AISTLQGIGQ TTNPEQSSSL
LTWKDKDGHT GQFKPYILPY LPVNLWGRDI LSKMGVYLYS PSPTVTDLML DQGLLPNQGL
GKQHQGIILP LDLKPNQDRK GLGCFPLGTS DSPVTHADPI DWKSEEPVWV DQWPLTQEKL
SAAQQLVQEQ LRLGHIEPST SAWNSPIFVI KKKSGKWRLL QDLRKVNETM MHMGALQPGL
PTPSAIPDKS YIIVIDLKDC FYTIPLAPQD CKRFAFSLPS VNFKEPMQRY QWRVLPQGMT
NSPTLCQKFV ATAIAPVRQR FPQLYLVHYM DDILLAHTDE HLLYQAFSIL KQHLSLNGLV
IADEKIQTHF PYNYLGFSLY PRVYNTQLVK LQTDHLKTLN DFQKLLGDIN WIRPYLKLPT
YTLQPLFDIL KGDSDPASPR TLSLEGRTAL QSIEEAIRQQ QITYCDYQRS WGLYILPTPR
APTGVLYQDK PLRWIYLSAT PTKHLLPYYE LVAKIIAKGR HEAIQYFGME PPFICVPYAL
EQQDWLFQFS DNWSIAFANY PGQITHHYPS DKLLQFASSH AFIFPKIVRR QPIPEATLIF
TDGSSNGTAA LIINHQTYYA QTSFSSAQVV ELFAVHQALL TVPTSFNLFT DSSYVVGALQ
MIETVPIIGT TSPEVLNLFT LIQQVLHCRQ HPCFFGHIRA HSTLPGALVQ GNHTADVLTK
QVFFQSAIDA ARKSHDLHHQ NSHSLRLQFK ISREAARQIV KSCSTCPQFF VLPQYGVNPR
GLRPNHLWQT DVTHIPQFGR LKYVHVSIDT FSNFLMASLH TGESTRHCIQ HLLFCFSTSG
IPQTLKTDNG PGYTSRSFQR FCLSFQIHHK TGIPYNPQGQ GIVERAHQRI KHQLLKQKKG
NELYSPSPHN ALNHALYVLN FLTLDTEGNS AAQRFWGERS SCKKPLVRWK DPLTNLWYGP
DPVLIWGRGH VCVFPQDAEA PRWIPERLVR AAEELPDASD ATHDPE


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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
orb90001 GST_HRV Protease Protease Recombinant is fusion protein of glutathione S-transferase (GST) and human rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes subset of sequences whic 100 IU
orb90006 Tobacco Etch Virus Protease protein Recombinant TEV Protease (rTEV) is site-specific protease purified from E.coli The protease can be used for the removal of affinity tags from fusion proteins. The s 300 IU
orb82817 PreScission Protease enzyme PreScission Protease is a fusion protein of Glutathione S-Transferase (GST) and Human Rhinovirus (HRV) type 14 3C protease. The protease specifically recognizes a subset of 1000 U
29-695 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
29-694 SEMG1 is the predominant protein in semen. The secreted protein is involved in the formation of a gel matrix that encases ejaculated spermatozoa. The prostate-specific antigen (PSA) protease processes 0.1 mg
EIAAB29697 C2orf7,Homo sapiens,hPAP21,Human,PAP21,PRADC1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa,UNQ833_PRO1760
EIAAB32649 Complement factor D-like protein,Df2,Prss57,Prssl1,Rat,Rattus norvegicus,Serine protease 1-like protein 1,Serine protease 57
orb90082 Thermostable dUTPase protein Enzymes 500 IU
EIAAB44303 Cancer_testis antigen 20,CT20,Homo sapiens,Human,Probable threonine protease PRSS50,PRSS50,Serine protease 50,Testis-specific protease-like protein 50,TSP50
EIAAB29696 Mouse,Mus musculus,Pap21,Pradc1,Protease-associated domain-containing protein 1,Protease-associated domain-containing protein of 21 kDa
U0800m CLIA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
E0800m ELISA IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,Mouse,Mus musculus,Pappa,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
EIAAB42587 Airway trypsin-like protease 1,ECRG1,Epidermal type-II transmembrane serine protease,Esophageal cancer-susceptibility gene 1 protein,HATL1,HESP,Homo sapiens,Human,TMPRSS11A,Transmembrane protease seri
U0800h CLIA Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
E0800h ELISA Homo sapiens,Human,IGFBP-4ase,IGF-dependent IGFBP-4 protease,Insulin-like growth factor-dependent IGF-binding protein 4 protease,PAPPA,PAPP-A,Pappalysin-1,Pregnancy-associated plasma protein A 96T
orb84854 TEV Protease protein TEV Protease protein For research use only. 100 IU
EIAAB40101 Homo sapiens,Human,Matriptase,Membrane-type serine protease 1,MT-SP1,Prostamin,PRSS14,Serine protease 14,Serine protease TADG-15,SNC19,ST14,Suppressor of tumorigenicity 14 protein,TADG15,Tumor-associa
65-008 anti_HIV_1 Gag p17 antibody, rabbit serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indispens 50 ul
65-009 anti_HIV_1 Gag p17 antibody, rabbit serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is produced by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indispens 250 ul
65-010 anti_HIV_1 Gag p17 antibody, guinea pig serum HIV_1 Gag p17 is the matrix protein of AIDS virus HIV_1 and is processed by the digestion of its precursor Gag p55 by HIV_1 protease. This protein is indi 50 ul
LF-PA50025 anti-DUTPase , Rabbit polyclonal to DUTPase , Isotype IgG, Host Rabbit 200 ul
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-661-15141 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.05 mg Aff Pur


 

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