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Gag-Pro-Pol polyprotein (Pr160Gag-Pro-Pol) [Cleaved into: Matrix protein p19 (MA); Capsid protein p24 (CA); Nucleocapsid protein p15-pro (NC') (NC-pro); Protease (PR) (EC 3.4.23.-); p1; 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_HTL1C               Reviewed;        1462 AA.
P14078; O56228;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
20-DEC-2017, entry version 142.
RecName: Full=Gag-Pro-Pol polyprotein;
AltName: Full=Pr160Gag-Pro-Pol;
Contains:
RecName: Full=Matrix protein p19;
Short=MA;
Contains:
RecName: Full=Capsid protein p24;
Short=CA;
Contains:
RecName: Full=Nucleocapsid protein p15-pro;
Short=NC';
Short=NC-pro;
Contains:
RecName: Full=Protease;
Short=PR;
EC=3.4.23.- {ECO:0000255|PROSITE-ProRule:PRU00275};
Contains:
RecName: Full=p1;
Contains:
RecName: Full=Reverse transcriptase/ribonuclease H, p49 subunit;
Short=p49 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=Reverse transcriptase/ribonuclease H, p62 subunit;
Short=p62 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:P03363};
EC=3.1.-.- {ECO:0000250|UniProtKB:P03363};
Name=gag-pro-pol;
Human T-cell leukemia virus 1 (isolate Caribbea HS-35 subtype A)
(HTLV-1).
Viruses; Retro-transcribing viruses; Retroviridae; Orthoretrovirinae;
Deltaretrovirus.
NCBI_TaxID=11927;
NCBI_TaxID=9606; Homo sapiens (Human).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=2899128; DOI=10.1099/0022-1317-69-7-1695;
Malik K.T.A., Even J., Karpas A.;
"Molecular cloning and complete nucleotide sequence of an adult T cell
leukaemia virus/human T cell leukaemia virus type I (ATLV/HTLV-I)
isolate of Caribbean origin: relationship to other members of the
ATLV/HTLV-I subgroup.";
J. Gen. Virol. 69:1695-1710(1988).
-!- FUNCTION: Gag-Pro-Pol polyprotein: The matrix domain targets Gag,
Gag-Pro and Gag-Pro-Pol polyproteins to the plasma membrane via a
multipartite membrane binding signal, that includes its
myristoylated N-terminus. {ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Matrix protein p19: Matrix protein.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Capsid protein p24: Forms the spherical core of the
virus that encapsulates the genomic RNA-nucleocapsid complex.
{ECO:0000250|UniProtKB:P03362}.
-!- FUNCTION: Nucleocapsid protein p15-pro: Binds strongly to viral
nucleic acids and promote their aggregation. Also destabilizes the
nucleic acids duplexes via highly structured zinc-binding motifs.
{ECO:0000250|UniProtKB:P03345}.
-!- FUNCTION: Protease: 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 (Potential). Cleaves the translation initiation factor eIF4G
leading to the inhibition of host cap-dependent translation (By
similarity). {ECO:0000250|UniProtKB:P03362, ECO:0000255|PROSITE-
ProRule:PRU00275}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H, p49 subunit: RT is
a multifunctional enzyme that converts the viral 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-Pro 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
primer. 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}.
-!- FUNCTION: Reverse transcriptase/ribonuclease H, p62 subunit: RT is
a multifunctional enzyme that converts the viral 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-Pro 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
primer. 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}.
-!- FUNCTION: Integrase: Catalyzes viral DNA integration into the host
chromosome, by performing a series of DNA cutting and joining
reactions. {ECO:0000250|UniProtKB:P03362}.
-!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'-
phosphomonoester. {ECO:0000255|PROSITE-ProRule:PRU00408}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00405}.
-!- 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};
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity.
{ECO:0000250};
-!- SUBUNIT: Gag-Pro-Pol polyprotein: Homodimer; the homodimers are
part of the immature particles. Gag-Pro-Pol polyprotein: Interacts
with human TSG101 and NEDD4; these interactions are essential for
budding and release of viral particles. Matrix protein p19:
Homodimer; further assembles as homohexamers.
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Matrix protein p19: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Capsid protein p24: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- SUBCELLULAR LOCATION: Nucleocapsid protein p15-pro: Virion
{ECO:0000250|UniProtKB:P03345}.
-!- ALTERNATIVE PRODUCTS:
Event=Ribosomal frameshifting; Named isoforms=3;
Comment=This strategy of translation probably allows the virus
to modulate the quantity of each viral protein. {ECO:0000305};
Name=Gag-Pol polyprotein;
IsoId=P14078-1; Sequence=Displayed;
Note=Produced by -1 ribosomal frameshifting at the gag-pol genes
boundary. {ECO:0000305};
Name=Gag-Pro polyprotein;
IsoId=P14074-1; Sequence=External;
Note=Produced by -1 ribosomal frameshifting at the gag-pro genes
boundary. {ECO:0000305};
Name=Gag polyprotein;
IsoId=P14076-1; Sequence=External;
Note=Produced by conventional translation. {ECO:0000305};
-!- 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. Matrix protein p19 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. {ECO:0000250|UniProtKB:P03345}.
-!- DOMAIN: Capsid protein p24: The capsid protein N-terminus seems to
be involved in Gag-Gag interactions.
{ECO:0000250|UniProtKB:P03362}.
-!- PTM: Matrix protein p19: Phosphorylation of the matrix protein p19
by MAPK1 seems to play a role in budding.
{ECO:0000250|UniProtKB:P03345}.
-!- 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:P03345}.
-!- PTM: Gag-Pro-Pol polyprotein: Specific enzymatic cleavages by the
viral protease yield mature proteins. The polyprotein is cleaved
during and after budding, this process is termed maturation. The
protease is autoproteolytically processed at its N- and C-termini.
{ECO:0000250|UniProtKB:P03362}.
-!- 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 switching
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}.
-!- MISCELLANEOUS: HTLV-1 lineages are divided in four clades, A
(Cosmopolitan), B (Central African group), C (Melanesian group)
and D (New Central African group). {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAA02931.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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EMBL; D13784; BAA02931.1; ALT_SEQ; Genomic_DNA.
EMBL; AF033817; AAC82581.1; -; Genomic_DNA.
PIR; C28136; GNLJCN.
RefSeq; NP_057860.1; NC_001436.1.
PDB; 4ZNY; X-ray; 2.40 A; B=121-130.
PDBsum; 4ZNY; -.
ProteinModelPortal; P14078; -.
SMR; P14078; -.
ELM; P14078; -.
GeneID; 1724740; -.
KEGG; vg:1724740; -.
OrthoDB; VOG09000057; -.
Proteomes; UP000001061; Genome.
Proteomes; UP000110593; 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-EC.
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:0005198; F:structural molecule activity; IEA:InterPro.
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:0039657; P:suppression by virus of host gene expression; 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.
Gene3D; 1.10.1200.30; -; 1.
Gene3D; 1.10.185.10; -; 1.
Gene3D; 1.10.375.10; -; 1.
Gene3D; 2.40.70.10; -; 1.
Gene3D; 3.30.420.10; -; 2.
Gene3D; 4.10.60.10; -; 3.
InterPro; IPR001969; Aspartic_peptidase_AS.
InterPro; IPR003139; D_retro_matrix.
InterPro; IPR036989; D_retro_matrix_sf.
InterPro; IPR000721; Gag_p24.
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; 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; IPR001878; Znf_CCHC.
InterPro; IPR036875; Znf_CCHC_sf.
Pfam; PF02228; Gag_p19; 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; PF00098; zf-CCHC; 1.
SMART; SM00343; ZnF_C2HC; 2.
SUPFAM; SSF47353; SSF47353; 1.
SUPFAM; SSF47836; SSF47836; 1.
SUPFAM; SSF47943; SSF47943; 1.
SUPFAM; SSF50122; SSF50122; 1.
SUPFAM; SSF50630; SSF50630; 1.
SUPFAM; SSF53098; SSF53098; 1.
SUPFAM; SSF57756; SSF57756; 1.
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.
1: Evidence at protein level;
3D-structure; Aspartyl protease; Capsid protein; Complete proteome;
DNA integration; DNA recombination; DNA-binding; Endonuclease;
Eukaryotic host gene expression shutoff by virus;
Eukaryotic host translation shutoff by virus;
Host gene expression shutoff by virus; Host-virus interaction;
Hydrolase; Lipoprotein; Magnesium; Metal-binding;
Multifunctional enzyme; Myristate; Nuclease; Nucleotidyltransferase;
Phosphoprotein; Protease; Reference proteome; Repeat;
Ribosomal frameshifting; RNA-directed DNA polymerase; Transferase;
Viral genome integration; Viral nucleoprotein; Virion;
Virus entry into host cell; Zinc; Zinc-finger.
INIT_MET 1 1 Removed; by host. {ECO:0000255}.
CHAIN 2 1462 Gag-Pro-Pol polyprotein.
/FTId=PRO_0000259940.
CHAIN 2 130 Matrix protein p19.
/FTId=PRO_0000259941.
CHAIN 131 344 Capsid protein p24.
/FTId=PRO_0000259942.
CHAIN 345 449 Nucleocapsid protein p15-pro.
/FTId=PRO_0000259943.
CHAIN 450 574 Protease.
/FTId=PRO_0000259944.
PEPTIDE 575 582 p1.
/FTId=PRO_0000259945.
CHAIN 583 1167 Reverse transcriptase/ribonuclease H, p62
subunit.
/FTId=PRO_0000038875.
CHAIN 583 1021 Reverse transcriptase/ribonuclease H, p49
subunit.
/FTId=PRO_0000442548.
CHAIN 1168 1462 Integrase.
/FTId=PRO_0000038876.
DOMAIN 476 554 Peptidase A2. {ECO:0000255|PROSITE-
ProRule:PRU00275}.
DOMAIN 614 804 Reverse transcriptase.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
DOMAIN 1031 1165 RNase H. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
DOMAIN 1219 1388 Integrase catalytic.
{ECO:0000255|PROSITE-ProRule:PRU00457}.
ZN_FING 355 372 CCHC-type 1. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
ZN_FING 378 395 CCHC-type 2. {ECO:0000255|PROSITE-
ProRule:PRU00047}.
DNA_BIND 1393 1443 Integrase-type. {ECO:0000255|PROSITE-
ProRule:PRU00506}.
MOTIF 118 121 PPXY motif.
{ECO:0000250|UniProtKB:P03345}.
MOTIF 124 127 PTAP/PSAP motif.
{ECO:0000250|UniProtKB:P03345}.
COMPBIAS 95 144 Pro-rich.
COMPBIAS 657 660 Poly-Ser.
ACT_SITE 481 481 Protease; shared with dimeric partner.
{ECO:0000255|PROSITE-ProRule:PRU00275}.
METAL 680 680 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 755 755 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 756 756 Magnesium; catalytic; for reverse
transcriptase activity.
{ECO:0000255|PROSITE-ProRule:PRU00405}.
METAL 1040 1040 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1074 1074 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1096 1096 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1157 1157 Magnesium; catalytic; for RNase H
activity. {ECO:0000255|PROSITE-
ProRule:PRU00408}.
METAL 1230 1230 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
METAL 1287 1287 Magnesium; catalytic; for integrase
activity. {ECO:0000255|PROSITE-
ProRule:PRU00457}.
SITE 130 131 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 344 345 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 449 450 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 574 575 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 582 583 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 1021 1022 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
SITE 1167 1168 Cleavage; by viral protease.
{ECO:0000250|UniProtKB:P03362}.
MOD_RES 105 105 Phosphoserine; by host MAPK1.
{ECO:0000250|UniProtKB:P03345}.
LIPID 2 2 N-myristoyl glycine; by host.
{ECO:0000255}.
SEQUENCE 1462 AA; 162686 MW; 89F03B47B8BA7805 CRC64;
MGQIFSRSAS PIPRPPRGLA AHHWLNFLQA AYRLEPGPSS YDFHQLKKFL KIALETPVWI
CPINYSLLAS LLPKGYPGRV NEILHILIQT QAQIPSRPAP PPPSSSTHDP PDSDPQIPPP
YVEPTAPQVL PVMHPHGAPP NHRPWQMKDL QAIKQEVSQA APGSPQFMQT IRLAVQQFDP
TAKDLQDLLQ YLCSSLVASL HHQQLDSLIS EAETRGITGY NPLAGPLRVQ ANNPQQQGLR
REYQQLWLAA FAALPGSAKD PSWASILQGL EEPYHAFVER LNIALDNGLP EGTPKDPILR
SLAYSNANKE CQKLLQARGH TNSPLGDMLR ACQAWTPKDK TKVLVVQPKK PPPNQPCFRC
GKAGHWSRDC TQPRPPPGPC PLCQDPTHWK RDCPRLKPTI PEPEPEEDAL LLDLPADIPH
PKNLHRGGGL TSPPTLQQVL PNQDPTSILP VIPLDPARRP VIKAQIDTQT SHPKTIEALL
DTGADMTVLP IALFSSNTPL KNTSVLGAGG QTQDHFKLTS LPVLIRLPFR TTPIVLTSCL
VDTKNNWAII GRDALQQCQG VLYLPEAKRP PVILPIQAPA VLGLEHLPRP PEISQFPLNP
ERLQALQHLV RKALEAGHIE PYTGPGNNPV FPVKKANGTW RFIHDLRATN SLTIDLSSSS
PGPPDLSSLP TTLAHLQTID LKDAFFQIPL PKQFQPYFAF TVPQQCNYGP GTRYAWRVLP
QGFKNSPTLF EMQLAHILQP IRQAFPQCTI LQYMDDILLA SPSHADLQLL SEATMASLIS
HGLPVSENKT QQTPGTIKFL GQIISPNHLT YDAVPKVPIR SRWALPELQA LLGEIQWVSK
GTPTLRQPLH SLYCALQRHT DPRDQIYLNP SQVQSLVQLR QALSQNCRSR LVQTLPLLGA
IMLTLTGTTT VVFQSKQQWP LVWLHAPLPH TSQCPWGQLL ASAVLLLDKY TLQSYGLLCQ
TIHHNISTQT FNQFIQTSDH PSVPILLHHS HRFKNLGAQT GELWNTFLKT TAPLAPVKAL
MPVFTLSPVI INTAPCLFSD GSTSQAAYIL WDKHILSQRS FPLPPPHKSA QRAELLGLLH
GLSSARSWRC LNIFLDSKYL YHYLRTLALG TFQGRSSQAP FQALLPRLLS RKVVYLHHVR
SHTNLPDPIS RLNALTDALL ITPVLQLSPA DLHSFTHCGQ TALTLQGATT TEASNILRSC
HACRKNNPQH QMPQGHIRRG LLPNHIWQGD ITHFKYKNTL YRLHVWVDTF SGAISATQKR
KETSSEAISS LLQAIAYLGK PSYINTDNGP AYISQDFLNM CTSLAIRHTT HVPYNPTSSG
LVERSNGILK TLLYKYFTDK PDLPMDNALS IALWTINHLN VLTNCHKTRW QLHHSPRLQP
IPETHSLSNK QTHWYYFKLP GLNSRQWKGP QEALQEAAGA ALIPVSASSA QWIPWRLLKR
AACPRPVGGP ADPKEKDHQH HG


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PCR-505L SCRIPT Reverse Transcriptase, L pack Reverse Transcriptase with increased thermal stability 50000 units
PCR-505L SCRIPT Reverse Transcriptase, L pack Reverse Transcriptase with increased thermal stability 50000units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10000 units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10000units
PCR-505S SCRIPT Reverse Transcriptase, S pack Reverse Transcriptase with increased thermal stability 10kunits
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
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
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-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
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
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-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
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
PCR-501S M_MLV Reverse Transcriptase (RNase H_), S pack Reverse Transcriptase 10000units
PCR-501L M_MLV Reverse Transcriptase (RNase H_), L pack Reverse Transcriptase 50000units
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
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
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
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


 

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