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Genome polyprotein (p254) [Cleaved into: Protein p16; Protein p23; NTPase (EC 3.6.1.15) (2C-like protein) (P2C) (p37); Precursor p41; Protein p29; Protein p23/2; Protein p18; Viral genome-linked protein (VPg) (p13); 3C-like protease (3CLpro) (EC 3.4.22.66) (Calicivirin) (Thiol protease P3C) (p15); RNA-directed RNA polymerase (EC 2.7.7.48) (3Dpol) (p58); Capsid protein VP60]

 POLG_RHDVF              Reviewed;        2344 AA.
P27410;
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
10-MAY-2017, entry version 124.
RecName: Full=Genome polyprotein;
AltName: Full=p254;
Contains:
RecName: Full=Protein p16;
Contains:
RecName: Full=Protein p23;
Contains:
RecName: Full=NTPase;
EC=3.6.1.15;
AltName: Full=2C-like protein;
AltName: Full=P2C;
AltName: Full=p37;
Contains:
RecName: Full=Precursor p41;
Contains:
RecName: Full=Protein p29;
Contains:
RecName: Full=Protein p23/2;
Contains:
RecName: Full=Protein p18;
Contains:
RecName: Full=Viral genome-linked protein;
AltName: Full=VPg;
AltName: Full=p13;
Contains:
RecName: Full=3C-like protease;
Short=3CLpro;
EC=3.4.22.66;
AltName: Full=Calicivirin;
AltName: Full=Thiol protease P3C;
AltName: Full=p15;
Contains:
RecName: Full=RNA-directed RNA polymerase;
EC=2.7.7.48;
AltName: Full=3Dpol;
AltName: Full=p58;
Contains:
RecName: Full=Capsid protein VP60;
ORFNames=ORF1;
Rabbit hemorrhagic disease virus (strain Rabbit/Germany/FRG/1989)
(Ra/LV/RHDV/GH/1989/GE) (RHDV-FRG).
Viruses; ssRNA viruses; ssRNA positive-strand viruses, no DNA stage;
Caliciviridae; Lagovirus.
NCBI_TaxID=314536;
NCBI_TaxID=9986; Oryctolagus cuniculus (Rabbit).
[1]
NUCLEOTIDE SEQUENCE [GENOMIC RNA].
PubMed=1840711; DOI=10.1016/0042-6822(91)90436-F;
Meyers G., Wirblich C., Thiel H.-J.;
"Rabbit hemorrhagic disease virus -- molecular cloning and nucleotide
sequencing of a calicivirus genome.";
Virology 184:664-676(1991).
[2]
FUNCTION OF VPG.
PubMed=1887589; DOI=10.1016/0042-6822(91)90437-G;
Meyers G., Wirblich C., Thiel H.-J.;
"Genomic and subgenomic RNAs of rabbit hemorrhagic disease virus are
both protein-linked and packaged into particles.";
Virology 184:677-686(1991).
[3]
MUTAGENESIS OF HIS-1135; ASP-1152; ASP-1175; CYS-1212 AND HIS-1227.
PubMed=8083986;
Boniotti B., Wirblich C., Sibilia M., Meyers G., Thiel H.J., Rossi C.;
"Identification and characterization of a 3C-like protease from rabbit
hemorrhagic disease virus, a calicivirus.";
J. Virol. 68:6487-6495(1994).
[4]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=7474137;
Wirblich C., Sibilia M., Boniotti M.B., Rossi C., Thiel H.-J.,
Meyers G.;
"3C-like protease of rabbit hemorrhagic disease virus: identification
of cleavage sites in the ORF1 polyprotein and analysis of cleavage
specificity.";
J. Virol. 69:7159-7168(1995).
[5]
SUBGENOMIC ORIGIN OF VP60.
PubMed=7637026;
Sibilia M., Boniotti M.B., Angoscini P., Capucci L., Rossi C.;
"Two independent pathways of expression lead to self-assembly of the
rabbit hemorrhagic disease virus capsid protein.";
J. Virol. 69:5812-5815(1995).
[6]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=9557747;
Konig M., Thiel H.J., Meyers G.;
"Detection of viral proteins after infection of cultured hepatocytes
with rabbit hemorrhagic disease virus.";
J. Virol. 72:4492-4497(1998).
[7]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=11040126; DOI=10.1006/viro.2000.0545;
Meyers G., Wirblich C., Thiel H.J., Thumfart J.O.;
"Rabbit hemorrhagic disease virus: genome organization and polyprotein
processing of a calicivirus studied after transient expression of cDNA
constructs.";
Virology 276:349-363(2000).
[8]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=10644847;
Joubert P., Pautigny C., Madelaine M.-F., Rasschaert D.;
"Identification of a new cleavage site of the 3C-like protease of
rabbit haemorrhagic disease virus.";
J. Gen. Virol. 81:481-488(2000).
[9]
CHARACTERIZATION OF RNA-DIRECTED RNA POLYMERASE.
PubMed=11266218; DOI=10.1007/s007050170191;
Lopez Vazquez A.L., Martin Alonso J.M., Parra F.;
"Characterisation of the RNA-dependent RNA polymerase from Rabbit
hemorrhagic disease virus produced in Escherichia coli.";
Arch. Virol. 146:59-69(2001).
[10]
PROTEOLYTIC PROCESSING OF POLYPROTEIN.
PubMed=12504575; DOI=10.1006/viro.2002.1660;
Thumfart J.O., Meyers G.;
"Rabbit hemorrhagic disease virus: identification of a cleavage site
in the viral polyprotein that is not processed by the known
calicivirus protease.";
Virology 304:352-363(2002).
[11]
FUNCTION OF CAPSID PROTEIN VP60.
PubMed=15063122; DOI=10.1016/j.virol.2004.01.021;
Barcena J., Verdaguer N., Roca R., Morales M., Angulo I., Risco C.,
Carrascosa J.L., Torres J.M., Caston J.R.;
"The coat protein of Rabbit hemorrhagic disease virus contains a
molecular switch at the N-terminal region facing the inner surface of
the capsid.";
Virology 322:118-134(2004).
[12]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 1252-1767.
PubMed=11677245; DOI=10.1074/jbc.M109261200;
Ng K.K.S., Cherney M.M., Vazquez A.L., Machin A., Martin-Alonso J.M.,
Parra F., James M.N.G.;
"Crystal structures of active and inactive conformations of a
caliciviral RNA-dependent RNA polymerase.";
J. Biol. Chem. 277:1381-1387(2002).
-!- FUNCTION: NTPase presumably plays a role in replication.
{ECO:0000250}.
-!- FUNCTION: Viral genome-linked protein is covalently linked to the
5'-end of the positive-strand, negative-strand genomic RNAs and
subgenomic RNA. Acts as a genome-linked replication primer. May
recruit ribosome to viral RNA thereby promoting viral proteins
translation (By similarity). {ECO:0000250}.
-!- FUNCTION: 3C-like protease processes the polyprotein: 3CLpro-RdRp
(p72) is first released by autocleavage, then all other proteins
are cleaved. {ECO:0000250}.
-!- FUNCTION: RNA-directed RNA polymerase replicates genomic and
antigenomic RNA by recognizing replications specific signals.
Transcribes also a subgenomic mRNA by initiating RNA synthesis
internally on antigenomic RNA. This sgRNA codes for structural
proteins. Catalyzes the covalent attachment VPg with viral RNAs
(By similarity). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- FUNCTION: Capsid protein VP60 self assembles to form an
icosahedral capsid with a T=3 symmetry, about 35 nm in diameter,
and consisting of 180 capsid proteins. A smaller form of capsid
with a diameter of 23 nm might be capsid proteins assembled as
icosahedron with T=1 symmetry. The capsid encapsulate VP2 proteins
and genomic or subgenomic RNA. Attaches virion to target cells by
binding histo-blood group antigens, inducing endocytosis of the
viral particle. Acidification of the endosome induces
conformational change of capsid protein thereby injecting virus
genomic RNA into host cytoplasm (By similarity). {ECO:0000250}.
-!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate.
-!- CATALYTIC ACTIVITY: Endopeptidase with a preference for cleavage
when the P1 position is occupied by Glu-|-Xaa and the P1' position
is occupied by Gly-|-Yaa.
-!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate
+ RNA(n+1). {ECO:0000255|PROSITE-ProRule:PRU00539}.
-!- SUBUNIT: Binds to histo-blood group antigens at surface of target
cells. {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Capsid protein VP60: Virion. Host cytoplasm
{ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage; Named isoforms=2;
Name=Genome polyprotein;
IsoId=P27410-1; Sequence=Displayed;
Note=Produced from the genomic RNA.;
Name=Subgenomic capsid protein VP60; Synonyms=VP1;
IsoId=P27410-2; Sequence=VSP_034381;
Note=Produced from the subgenomic RNA.;
-!- PTM: Specific enzymatic cleavages by its own cysteine protease
yield mature proteins. The protease cleaves itself from the
nascent polyprotein autocatalytically. Precursor p41 can be
cleaved by viral 3CLpro into protein p19 and VPg, or cleaved by
host protease into protein p23/2 and protein p18.
{ECO:0000269|PubMed:10644847, ECO:0000269|PubMed:11040126,
ECO:0000269|PubMed:12504575, ECO:0000269|PubMed:7474137,
ECO:0000269|PubMed:9557747}.
-!- PTM: VPg is uridylylated by the polymerase and is covalently
attached to the 5'-end of the polyadenylated genomic and
subgenomic RNAs. This uridylylated form acts as a nucleotide-
peptide primer for the polymerase (By similarity). {ECO:0000250}.
-!- MISCELLANEOUS: Two different RNAs lead the expression of the
capsid protein. One arises from the cleavage of the polyprotein
translated from the genomic RNA and the other from the translation
of a subgenomic RNA derived from the (-)RNA template. Capsid
protein expressed from the subgenomic mRNA is produced in much
larger amounts than the cleaved one (By similarity).
{ECO:0000250}.
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EMBL; M67473; AAA47285.1; -; Genomic_RNA.
PIR; A41039; RRWWRH.
RefSeq; NP_062875.1; NC_001543.1.
PDB; 1KHV; X-ray; 2.50 A; A/B=1252-1767.
PDB; 1KHW; X-ray; 2.70 A; A/B=1252-1767.
PDBsum; 1KHV; -.
PDBsum; 1KHW; -.
ProteinModelPortal; P27410; -.
SMR; P27410; -.
PRIDE; P27410; -.
GeneID; 1491968; -.
KEGG; vg:1491968; -.
OrthoDB; VOG0900006M; -.
BRENDA; 3.4.22.B15; 5265.
EvolutionaryTrace; P27410; -.
Proteomes; UP000000413; Genome.
GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0019028; C:viral capsid; IEA:UniProtKB-KW.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0004197; F:cysteine-type endopeptidase activity; IEA:InterPro.
GO; GO:0003723; F:RNA binding; IEA:InterPro.
GO; GO:0003724; F:RNA helicase activity; IEA:InterPro.
GO; GO:0003968; F:RNA-directed 5'-3' RNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0018144; P:RNA-protein covalent cross-linking; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro.
GO; GO:0039694; P:viral RNA genome replication; IEA:InterPro.
CDD; cd00205; rhv_like; 1.
InterPro; IPR004005; Calicivirus_coat.
InterPro; IPR004004; Helic/Pol/Pept_Calicivir-typ.
InterPro; IPR000605; Helicase_SF3_ssDNA/RNA_vir.
InterPro; IPR014759; Helicase_SF3_ssRNA_vir.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR000317; Peptidase_C24.
InterPro; IPR009003; Peptidase_S1_PA.
InterPro; IPR033703; Rhv-like.
InterPro; IPR001205; RNA-dir_pol_C.
InterPro; IPR007094; RNA-dir_pol_PSvirus.
Pfam; PF00915; Calici_coat; 1.
Pfam; PF03510; Peptidase_C24; 1.
Pfam; PF00680; RdRP_1; 1.
Pfam; PF00910; RNA_helicase; 1.
PRINTS; PR00916; 2CENDOPTASE.
PRINTS; PR00918; CALICVIRUSNS.
SUPFAM; SSF50494; SSF50494; 1.
SUPFAM; SSF52540; SSF52540; 1.
PROSITE; PS50507; RDRP_SSRNA_POS; 1.
PROSITE; PS51218; SF3_HELICASE_2; 1.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; ATP-binding; Capsid protein;
Complete proteome; Covalent protein-RNA linkage; Disulfide bond;
Helicase; Host cytoplasm; Hydrolase; Nucleotide-binding;
Nucleotidyltransferase; Phosphoprotein; Protease; Reference proteome;
RNA-directed RNA polymerase; Thiol protease; Transferase;
Viral RNA replication; Virion.
CHAIN 1 2344 Genome polyprotein.
/FTId=PRO_0000341645.
CHAIN 1 143 Protein p16.
/FTId=PRO_0000036959.
CHAIN 144 339 Protein p23.
/FTId=PRO_0000036960.
CHAIN 340 718 NTPase.
/FTId=PRO_0000036961.
CHAIN 719 1108 Precursor p41.
/FTId=PRO_0000341646.
CHAIN 719 993 Protein p29.
/FTId=PRO_0000036962.
CHAIN 719 936 Protein p23/2.
/FTId=PRO_0000341647.
CHAIN 937 1108 Protein p18.
/FTId=PRO_0000341648.
CHAIN 994 1108 Viral genome-linked protein.
/FTId=PRO_0000036963.
CHAIN 1109 1251 3C-like protease.
/FTId=PRO_0000036964.
CHAIN 1252 1767 RNA-directed RNA polymerase.
/FTId=PRO_0000036965.
CHAIN 1768 2344 Capsid protein VP60.
/FTId=PRO_0000036967.
DOMAIN 492 653 SF3 helicase. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
DOMAIN 1120 1218 Peptidase C24.
DOMAIN 1495 1619 RdRp catalytic. {ECO:0000255|PROSITE-
ProRule:PRU00539}.
NP_BIND 522 529 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00551}.
ACT_SITE 1135 1135 For 3CLpro activity. {ECO:0000250}.
ACT_SITE 1159 1159 For 3CLpro activity. {ECO:0000250}.
ACT_SITE 1212 1212 For 3CLpro activity. {ECO:0000250}.
SITE 143 144 Cleavage; by 3CLpro.
SITE 339 340 Cleavage; by 3CLpro.
SITE 718 719 Cleavage; by 3CLpro.
SITE 936 937 Cleavage; by host.
SITE 993 994 Cleavage; by 3CLpro.
SITE 1108 1109 Cleavage; by 3CLpro.
SITE 1251 1252 Cleavage; by 3CLpro.
SITE 1767 1768 Cleavage; by 3CLpro.
MOD_RES 1014 1014 O-(5'-phospho-RNA)-tyrosine.
{ECO:0000250}.
DISULFID 1584 1591
VAR_SEQ 1 1765 Missing (in isoform Subgenomic capsid
protein VP60). {ECO:0000305}.
/FTId=VSP_034381.
MUTAGEN 1135 1135 H->N: Complete loss of 3CLpro activity in
vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1152 1152 D->E: Partial loss of 3CLpro activity in
vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1152 1152 D->G,N: Complete loss of 3CLpro activity
in vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1175 1175 D->G,E: Complete loss of 3CLpro activity
in vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1175 1175 D->N: Partial loss of 3CLpro activity in
vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1212 1212 C->G: Complete loss of 3CLpro activity in
vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1212 1212 C->S: Partial loss of 3CLpro activity in
vitro. {ECO:0000269|PubMed:8083986}.
MUTAGEN 1227 1227 H->L,N: Complete loss of 3CLpro activity
in vitro. {ECO:0000269|PubMed:8083986}.
STRAND 1257 1263 {ECO:0000244|PDB:1KHV}.
STRAND 1266 1271 {ECO:0000244|PDB:1KHV}.
STRAND 1282 1287 {ECO:0000244|PDB:1KHV}.
HELIX 1293 1295 {ECO:0000244|PDB:1KHV}.
STRAND 1300 1302 {ECO:0000244|PDB:1KHV}.
HELIX 1305 1307 {ECO:0000244|PDB:1KHV}.
HELIX 1315 1324 {ECO:0000244|PDB:1KHV}.
HELIX 1325 1327 {ECO:0000244|PDB:1KHV}.
HELIX 1337 1353 {ECO:0000244|PDB:1KHV}.
TURN 1354 1356 {ECO:0000244|PDB:1KHV}.
HELIX 1364 1370 {ECO:0000244|PDB:1KHV}.
STRAND 1373 1376 {ECO:0000244|PDB:1KHW}.
STRAND 1379 1381 {ECO:0000244|PDB:1KHV}.
HELIX 1385 1387 {ECO:0000244|PDB:1KHV}.
STRAND 1391 1393 {ECO:0000244|PDB:1KHV}.
HELIX 1396 1410 {ECO:0000244|PDB:1KHV}.
STRAND 1418 1423 {ECO:0000244|PDB:1KHV}.
STRAND 1440 1444 {ECO:0000244|PDB:1KHV}.
HELIX 1446 1465 {ECO:0000244|PDB:1KHV}.
TURN 1466 1469 {ECO:0000244|PDB:1KHV}.
STRAND 1470 1472 {ECO:0000244|PDB:1KHV}.
HELIX 1482 1493 {ECO:0000244|PDB:1KHV}.
STRAND 1495 1502 {ECO:0000244|PDB:1KHV}.
HELIX 1505 1508 {ECO:0000244|PDB:1KHV}.
HELIX 1511 1522 {ECO:0000244|PDB:1KHV}.
HELIX 1529 1539 {ECO:0000244|PDB:1KHV}.
STRAND 1543 1545 {ECO:0000244|PDB:1KHV}.
STRAND 1547 1551 {ECO:0000244|PDB:1KHV}.
HELIX 1564 1586 {ECO:0000244|PDB:1KHV}.
HELIX 1594 1597 {ECO:0000244|PDB:1KHV}.
STRAND 1600 1603 {ECO:0000244|PDB:1KHV}.
STRAND 1606 1611 {ECO:0000244|PDB:1KHV}.
HELIX 1613 1617 {ECO:0000244|PDB:1KHV}.
HELIX 1619 1628 {ECO:0000244|PDB:1KHV}.
STRAND 1633 1637 {ECO:0000244|PDB:1KHV}.
HELIX 1647 1649 {ECO:0000244|PDB:1KHV}.
STRAND 1655 1660 {ECO:0000244|PDB:1KHV}.
STRAND 1663 1668 {ECO:0000244|PDB:1KHV}.
HELIX 1670 1678 {ECO:0000244|PDB:1KHV}.
STRAND 1679 1689 {ECO:0000244|PDB:1KHV}.
HELIX 1698 1712 {ECO:0000244|PDB:1KHV}.
HELIX 1716 1729 {ECO:0000244|PDB:1KHV}.
TURN 1730 1732 {ECO:0000244|PDB:1KHV}.
HELIX 1740 1750 {ECO:0000244|PDB:1KHV}.
SEQUENCE 2344 AA; 257068 MW; 1454C248F81E9212 CRC64;
MAAMSRLTGM TTAILPEKKP LDFFLDLRDK TPPCCIRATG RLAWPVFPGQ NGKEGPLETC
NKCGKWLNGF GNFGLEDLGD VCLCSIAQQK HKFGPVCLCN RVYIHDCGRW RRRSRFLKHY
KALNKVIPCA YQFDESFPTP IFEGEVDDLF VELGAPTSMG FMDKKLLKKG KKLMDKFVDV
DEPCLTSRDT SLLDSIASDN TIRAKLEEEY GVEMVQAARD RKDFMKNLRL ALDNRPANPV
TWYTKLGNIT EKGKQWAKKV VYGARKVTDP LKTLASILLV GLHNVIAVDT TVMLSTFKPV
NLLAILMDWN NDLTGFITTL VRLLELYGVV QATVNLIIEG VKSFWDKVVC ATDRCFDLLK
RLFDTFEDSV PTGPTAGCLI FMAFVFSTVV GYLPNNSVIT TFMKGAGKLT TFAGVVGAIR
TLWITINQHM VAKDLTSVQQ KVMTVVKMAN EAATLDQLEI VSCLCSDLET TLTNRCTLPS
YNQHLGILNA SQKVISDLHT MVLGKINMTK QRPQPVAVIF KGAPGIGKTY LVHRIARDLG
CQHPSTINFG LDHFDSYTGE EVAIADEFNT CGDGESWVEL FIQMVNTNPC PLNCDKAENK
NKVFNSKYLL CTTNSNMILN ATHPRAGAFY RRVMIVEARN KAVESWQATR HGSKPGKSCY
SKDMSHLTFQ VYPHNMPAPG FVFVGDKLVK SQVTPREYKY SELLDLIKSE HPDVASFEGA
NKFNFVYPDA QYDQALLMWK QYFVMYGCVA RLAKNFVDDI PYNQVHISRA SDPKIEGCVE
YQCKFQHLWR MVPQFVLGCV NMTNQLGTPL TQQQLDRITN GVEGVTVTTV NNILPFHSQT
TLINPSFIKL IWAVRKHLKG LSGVTKVAQF IWRVMTNPVD AYGTLVRTLT GAATFSDDPV
STTIICSNCT IQLHSCGGLL VRYSRDPVPV ASDNVDRGDQ GVDVFTDPNL ISGFSWRQIA
HLFVEVISHL CANHLVNLAT MAALGAVATK AFQGVKGKTK RGRGARVNLG NDEYDEWQAA
RREFVNAHDM TAEEYLAMKN KAAMGSDDQD SIMFRSWWTR RQLRPEEDQV TIVGRSGVRN
EVIRTRVRQT PRGPKTLDDG GFYDNDYEGL PGFMRHNGSG WMIHIGNGLY ISNTHTARSS
CSEIVTCSPT TDLCLVKGES IRSVAQIAEG TPVCDWKKSP ISTYGIKKTL SDSTKIDVLA
YDGCTQTTHG DCGLPLYDSS GKIVAIHTGK LLGFSKMCTL IDLTITKGVY ETSNFFCGEP
IDYRGITAHR LVGAEPRPPV SGTRYAKVPG VPDEYKTGYR PANLGRSDPD SDKSLMNIAV
KNLQVYQQEP KLDKVDEFIE RAAADVLGYL RFLTKGERQA NLNFKAAFNT LDLSTSCGPF
VPGKKIDHVK DGVMDQVLAK HLYKCWSVAN SGKALHHIYA CGLKDELRPL DKVKEGKKRL
LWGCDVGVAV CAAAVFHNIC YKLKMVARFG PIAVGVDMTS RDVDVIINNL TSKASDFLCL
DYSKWDSTMS PCVVRLAIDI LADCCEQTEL TKSVVLTLKS HPMTILDAMI VQTKRGLPSG
MPFTSVINSI CHWLLWSAAV YKSCAEIGLH CSNLYEDAPF YTYGDDGVYA MTPMMVSLLP
AIIENLRDYG LSPTAADKTE FIDVCPLNKI SFLKRTFELT DIGWVSKLDK SSILRQLEWS
KTTSRHMVIE ETYDLAKEER GVQLEELQVA AAAHGQEFFN FVCRELERQQ AYTQFSVYSY
DAARKILADR KRVVSVVPDD EFVNVMEGKA RAAPQGEAAG TATTASVPGT TTDGMDPGVV
ATTSVITAEN SSASIATAGI GGPPQQVDQQ ETWRTNFYYN DVFTWSVADA PGSILYTVQH
SPQNNPFTAV LSQMYAGWAG GMQFRFIVAG SGVFGGRLVR AVIPPGIEIG PGLEVRQFPH
VVIDARSLEP VTITMPDLRP NMYHPTGDPG LVPTLVLSVY NNLINPFGGS TSAIQVTVET
RPSEDFEFVM IRAPSSKTVD SISPAGLLTT PVLTGVGNDN RWNGQIVGLQ PVPGGFSTCN
RHWNLNGSTY GWSSPRFGDI DHRRGSASYS GSNATNVLQF WYANAGSAID NPISQVAPDG
FPDMSFVPFN GPGIPAAGWV GFGAIWNSNS GAPNVTTVQA YELGFATGAP GNLQPTTNTS
GAQTVAKSIY AVVTGTAQNP AGLFVMASGI ISTPNASAIT YTPQPDRIVT TPGTPAAAPV
GKNTPIMFAS VVRRTGDVNA TAGSANGTQY GTGSQPLPVT IGLSLNNYSS ALMPGQFFVW
QLTFASGFME IGLSVDGYFY AGTGASTTLI DLTELIDVRP VGPRPSKSTL VFNLGGTANG
FSYV


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18-272-195346 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.05 ml
18-272-196327 Amyloid Precursor Protein - Rabbit polyclonal to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; PreA4 0.5 ml
20-272-190769 Amyloid Precursor Protein - Mouse monoclonal [3E9] to Amyloid Precursor Protein; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin-II; PN-II; APPI; 0.05 mg
18-272-196328 Amyloid Precursor Protein prediluted - Rabbit polyclonal to Amyloid Precursor Protein prediluted; APP; ABPP; Alzheimer disease amyloid protein; Cerebral vascular amyloid peptide; CVAP; Protease nexin- 7 ml
EIAAB35745 A34.5,Anti-sense to ERCC-1 protein,Ase1,ASE-1,Cd3eap,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Mouse,Mus musculus,Paf49,RNA polymerase I-associ
EIAAB35359 BLAP75,BLM-associated protein of 75 kDa,C9orf76,FAAP75,Homo sapiens,Human,RecQ-mediated genome instability protein 1,RMI1
EIAAB35365 BLAP18,BLM-associated protein of 18 kDa,C16orf75,Homo sapiens,hRMI2,Human,RecQ-mediated genome instability protein 2,RMI2
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
18-001-30061 Caspase recruitment domain-containing protein 12 - Ice protease-activating factor; Ipaf; CARD. LRR. and NACHT-containing protein; Clan protein Polyclonal 0.1 mg
18-003-42864 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
EIAAB35746 A34.5,Antisense to ERCC-1 protein,ASE1,ASE-1,CAST,CAST,CD3EAP,CD3E-associated protein,CD3-epsilon-associated protein,DNA-directed RNA polymerase I subunit RPA34,Homo sapiens,Human,PAF49,RNA polymerase
25-375 This protein is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein complex formed by t 0.05 mg
EIAAB45903 ERVK6,HERV-K(C7) Pro protein,HERV-K(HML-2.HOM) Pro protein,HERV-K_7p22.1 provirus ancestral Pro protein,HERV-K108 Pro protein,Homo sapiens,Human,PR,Protease,Proteinase
28-544 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-533 MCM3 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM protein 0.05 mg
28-534 MCM3 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein complex formed by MCM protein 0.05 mg
28-535 The protein encoded by MCM2 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are involved in the initiation of eukaryotic genome replication. The hexameric protein comple 0.1 mg
28-536 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-539 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-540 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg


 

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