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Blood group Rh(D) polypeptide (RHXIII) (Rh polypeptide 2) (RhPII) (Rhesus D antigen) (CD antigen CD240D)

 RHD_HUMAN               Reviewed;         417 AA.
Q02161; Q02162; Q07618; Q16147; Q16235; Q16355; Q5VSK0; Q5XLS9;
Q5XLT1; Q5XLT2; Q9NPK0; Q9UQ20; Q9UQ21; Q9UQ22; Q9UQ23;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
12-SEP-2018, entry version 163.
RecName: Full=Blood group Rh(D) polypeptide;
AltName: Full=RHXIII;
AltName: Full=Rh polypeptide 2;
Short=RhPII;
AltName: Full=Rhesus D antigen;
AltName: CD_antigen=CD240D;
Name=RHD;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT ILE-218.
TISSUE=Bone marrow;
PubMed=1438298; DOI=10.1073/pnas.89.22.10925;
le van Kim C., Mouro I., Cherif-Zahar B., Raynal V., Cherrier C.,
Cartron J.-P., Colin Y.;
"Molecular cloning and primary structure of the human blood group RhD
polypeptide.";
Proc. Natl. Acad. Sci. U.S.A. 89:10925-10929(1992).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Bone marrow;
PubMed=1379850;
le van Kim C., Cherif-Zahar B., Raynal V., Mouro I., Lopez M.,
Cartron J.-P., Colin Y.;
"Multiple Rh messenger RNA isoforms are produced by alternative
splicing.";
Blood 80:1074-1078(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8329718;
Arce M.A., Thompson E.S., Wagner S., Coyne K.E., Ferdman B.A.,
Lublin D.M.;
"Molecular cloning of RhD cDNA derived from a gene present in RhD-
positive, but not RhD-negative individuals.";
Blood 82:651-655(1993).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=7916743; DOI=10.1007/BF00222717;
Kajii E., Umenishi F., Iwamoto S., Ikemoto S.;
"Isolation of a new cDNA clone encoding an Rh polypeptide associated
with the Rh blood group system.";
Hum. Genet. 91:157-162(1993).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
PubMed=8180407;
Westhoff C.M., Wylie D.E.;
"Identification of a new RhD-specific mRNA from K562 cells.";
Blood 83:3098-3100(1994).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT CYS-16.
PubMed=7606008;
Huang C.-H., Reid M.E., Chen Y.;
"Identification of a partial internal deletion in the RH locus causing
the human erythrocyte D-phenotype.";
Blood 86:784-790(1995).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
PubMed=8080999;
Suyama K., Lunn R., Haller S., Goldstein J.;
"Rh(D) antigen expression and isolation of a new Rh(D) cDNA isoform in
human erythroleukemic K562 cells.";
Blood 84:1975-1981(1994).
[8]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5 AND 6), AND ALTERNATIVE
SPLICING.
PubMed=16510313; DOI=10.1016/j.transci.2005.10.001;
Shao C.P., Xiong W., Zhou Y.Y.;
"Multiple isoforms excluding normal RhD mRNA detected in Rh blood
group Del phenotype with RHD 1227A allele.";
Transfus. Apher. Sci. 34:145-152(2006).
[9]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS VAL-223; GLN-233; MET-238 AND
LEU-245.
Hyodo H., Ishikawa Y., Kashiwase K., Ogawa A., Watanabe Y.,
Tsuneyama H., Toyoda C., Uchikawa M., Akaza T., Fujii T.;
"Polymorphisms of RhDVa in Japanese.";
Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[11]
PROTEIN SEQUENCE OF 2-33.
PubMed=3146980; DOI=10.1042/bj2561043;
Avent N.D., Ridgwell K., Mawby W.J., Tanner M.J.A., Anstee D.J.,
Kumpel B.;
"Protein-sequence studies on Rh-related polypeptides suggest the
presence of at least two groups of proteins which associate in the
human red-cell membrane.";
Biochem. J. 256:1043-1046(1988).
[12]
PROTEIN SEQUENCE OF 2-21.
PubMed=3131772; DOI=10.1073/pnas.85.11.4042;
Saboori A.M., Smith B.L., Agre P.;
"Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive
and -negative erythrocytes.";
Proc. Natl. Acad. Sci. U.S.A. 85:4042-4045(1988).
[13]
PROTEIN SEQUENCE OF 2-17.
PubMed=3135863;
Bloy C., Blanchard D., Dahr W., Beyreuther K., Salmon C.,
Cartron J.-P.;
"Determination of the N-terminal sequence of human red cell Rh(D)
polypeptide and demonstration that the Rh(D), (c), and (E) antigens
are carried by distinct polypeptide chains.";
Blood 72:661-666(1988).
[14]
PROTEIN SEQUENCE OF 401-407.
PubMed=1898705;
Suyama K., Goldstein J., Aebersold R., Kent S.;
"Regarding the size of Rh proteins.";
Blood 77:411-411(1991).
[15]
SUBCELLULAR LOCATION, AND PALMITOYLATION.
PubMed=3142870;
de Vetten M.P., Agre P.;
"The Rh polypeptide is a major fatty acid-acylated erythrocyte
membrane protein.";
J. Biol. Chem. 263:18193-18196(1988).
[16]
SUBCELLULAR LOCATION, AND PALMITOYLATION.
PubMed=1544931;
Hartel-Schenk S., Agre P.;
"Mammalian red cell membrane Rh polypeptides are selectively
palmitoylated subunits of a macromolecular complex.";
J. Biol. Chem. 267:5569-5574(1992).
[17]
VARIANT TAR ANTIGEN PRO-110.
PubMed=7741145; DOI=10.1002/ajh.2830490115;
Rouillac C., le van Kim C., Beolet M., Cartron J.-P., Colin Y.;
"Leu110Pro substitution in the RhD polypeptide is responsible for the
DVII category blood group phenotype.";
Am. J. Hematol. 49:87-88(1995).
[18]
VARIANT [LARGE SCALE ANALYSIS] CYS-103.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: May be part of an oligomeric complex which is likely to
have a transport or channel function in the erythrocyte membrane.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1544931,
ECO:0000269|PubMed:3142870}; Multi-pass membrane protein
{ECO:0000255}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=Long;
IsoId=Q02161-1; Sequence=Displayed;
Name=2; Synonyms=Short 1;
IsoId=Q02161-2; Sequence=VSP_005706;
Name=3; Synonyms=Short 2;
IsoId=Q02161-3; Sequence=VSP_005707, VSP_005708;
Name=4;
IsoId=Q02161-4; Sequence=VSP_047797;
Name=5;
IsoId=Q02161-5; Sequence=VSP_047796;
Name=6;
IsoId=Q02161-6; Sequence=VSP_047795, VSP_047798;
-!- TISSUE SPECIFICITY: Restricted to tissues or cell lines expressing
erythroid characters.
-!- PTM: Palmitoylated. {ECO:0000269|PubMed:1544931,
ECO:0000269|PubMed:3142870}.
-!- POLYMORPHISM: RHD and RHCE are responsible for the Rh blood group
system. The molecular basis of the Tar=Rh40 blood group antigen is
a polymorphism in position 110.
-!- SIMILARITY: Belongs to the ammonium transporter (TC 2.A.49)
family. Rh subfamily. {ECO:0000305}.
-!- WEB RESOURCE: Name=dbRBC/BGMUT; Note=Blood group antigen gene
mutation database;
URL="https://www.ncbi.nlm.nih.gov/gv/mhc/xslcgi.cgi?cmd=bgmut/systems_info&system=rh";
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EMBL; X63097; CAA44811.1; -; mRNA.
EMBL; X63094; CAA44808.1; -; mRNA.
EMBL; L08429; AAA02679.1; -; mRNA.
EMBL; S57971; AAB26081.1; -; mRNA.
EMBL; S70174; AAB30756.1; -; mRNA.
EMBL; S78509; AAB34852.1; -; mRNA.
EMBL; S73913; AAB31911.1; -; mRNA.
EMBL; AY751492; AAU93636.1; -; mRNA.
EMBL; AY751493; AAU93637.1; -; mRNA.
EMBL; AY751495; AAU93639.1; -; mRNA.
EMBL; AB018966; BAA81899.1; -; mRNA.
EMBL; AB018967; BAA81900.1; -; mRNA.
EMBL; AB018968; BAA81901.1; -; mRNA.
EMBL; AB018969; BAA82159.1; -; mRNA.
EMBL; AL928711; CAH72602.1; -; Genomic_DNA.
CCDS; CCDS262.1; -. [Q02161-1]
CCDS; CCDS53285.1; -. [Q02161-2]
CCDS; CCDS60028.1; -. [Q02161-4]
CCDS; CCDS60030.1; -. [Q02161-5]
CCDS; CCDS60031.1; -. [Q02161-6]
PIR; A46368; A46368.
PIR; I52615; I52615.
RefSeq; NP_001121163.1; NM_001127691.2. [Q02161-2]
RefSeq; NP_001269797.1; NM_001282868.1. [Q02161-6]
RefSeq; NP_001269798.1; NM_001282869.1. [Q02161-5]
RefSeq; NP_001269800.1; NM_001282871.1. [Q02161-4]
RefSeq; NP_057208.2; NM_016124.4.
UniGene; Hs.449968; -.
ProteinModelPortal; Q02161; -.
BioGrid; 111939; 1.
IntAct; Q02161; 7.
STRING; 9606.ENSP00000331871; -.
ChEMBL; CHEMBL3712996; -.
TCDB; 1.A.11.4.3; the ammonium transporter channel (amt) family.
iPTMnet; Q02161; -.
PhosphoSitePlus; Q02161; -.
BioMuta; RHD; -.
DMDM; 296452980; -.
PaxDb; Q02161; -.
PeptideAtlas; Q02161; -.
PRIDE; Q02161; -.
ProteomicsDB; 58055; -.
ProteomicsDB; 58056; -. [Q02161-2]
ProteomicsDB; 58057; -. [Q02161-3]
DNASU; 6007; -.
Ensembl; ENST00000328664; ENSP00000331871; ENSG00000187010. [Q02161-1]
Ensembl; ENST00000342055; ENSP00000339577; ENSG00000187010. [Q02161-4]
Ensembl; ENST00000357542; ENSP00000350150; ENSG00000187010. [Q02161-5]
Ensembl; ENST00000417538; ENSP00000396420; ENSG00000187010. [Q02161-6]
Ensembl; ENST00000454452; ENSP00000413849; ENSG00000187010. [Q02161-2]
GeneID; 6007; -.
KEGG; hsa:6007; -.
UCSC; uc001bjz.5; human. [Q02161-1]
CTD; 6007; -.
DisGeNET; 6007; -.
EuPathDB; HostDB:ENSG00000187010.18; -.
GeneCards; RHD; -.
HGNC; HGNC:10009; RHD.
MalaCards; RHD; -.
MIM; 111680; gene.
neXtProt; NX_Q02161; -.
OpenTargets; ENSG00000187010; -.
Orphanet; 71275; Rh deficiency syndrome.
PharmGKB; PA34387; -.
eggNOG; KOG3796; Eukaryota.
eggNOG; ENOG410XTF8; LUCA.
GeneTree; ENSGT00390000005787; -.
HOVERGEN; HBG004374; -.
InParanoid; Q02161; -.
KO; K06579; -.
OMA; MTHIHNA; -.
OrthoDB; EOG091G06KX; -.
PhylomeDB; Q02161; -.
TreeFam; TF314450; -.
GeneWiki; RHD_(gene); -.
GenomeRNAi; 6007; -.
PRO; PR:Q02161; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000187010; Expressed in 102 organ(s), highest expression level in trabecular bone tissue.
ExpressionAtlas; Q02161; baseline and differential.
Genevisible; Q02161; HS.
GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central.
GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central.
GO; GO:0015695; P:organic cation transport; IBA:GO_Central.
Gene3D; 1.10.3430.10; -; 1.
InterPro; IPR029020; Ammonium/urea_transptr.
InterPro; IPR024041; NH4_transpt_AmtB-like_dom.
InterPro; IPR002229; RhesusRHD.
Pfam; PF00909; Ammonium_transp; 1.
PRINTS; PR00342; RHESUSRHD.
1: Evidence at protein level;
Alternative splicing; Blood group antigen; Cell membrane;
Complete proteome; Direct protein sequencing; Lipoprotein; Membrane;
Palmitate; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
INIT_MET 1 1 Removed. {ECO:0000269|PubMed:3131772,
ECO:0000269|PubMed:3135863,
ECO:0000269|PubMed:3146980}.
CHAIN 2 417 Blood group Rh(D) polypeptide.
/FTId=PRO_0000168190.
TRANSMEM 12 32 Helical. {ECO:0000255}.
TRANSMEM 44 64 Helical. {ECO:0000255}.
TRANSMEM 77 97 Helical. {ECO:0000255}.
TRANSMEM 107 127 Helical. {ECO:0000255}.
TRANSMEM 130 150 Helical. {ECO:0000255}.
TRANSMEM 167 187 Helical. {ECO:0000255}.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TRANSMEM 238 258 Helical. {ECO:0000255}.
TRANSMEM 287 307 Helical. {ECO:0000255}.
TRANSMEM 334 354 Helical. {ECO:0000255}.
TRANSMEM 358 378 Helical. {ECO:0000255}.
VAR_SEQ 314 409 Missing (in isoform 2).
{ECO:0000303|PubMed:8180407}.
/FTId=VSP_005706.
VAR_SEQ 314 378 GCCNRVLGIPHSSIMGYNFSLLGLLGEIIYIVLLVLDTVGA
GNGMIGFQVLLSIGELSLAIVIAL -> DWLPGPPQHWGTQ
LGHRDSSHVWSPDSFLIWLLDFKQKHPRKTRPVQKQDNFLS
LLPAFVREKRS (in isoform 6).
{ECO:0000303|PubMed:16510313}.
/FTId=VSP_047795.
VAR_SEQ 316 316 C -> S (in isoform 3).
{ECO:0000303|PubMed:8080999}.
/FTId=VSP_005707.
VAR_SEQ 317 417 Missing (in isoform 3).
{ECO:0000303|PubMed:8080999}.
/FTId=VSP_005708.
VAR_SEQ 358 417 MIGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHE
AKYFDDQVFWKFPHLAVGF -> IFLIWLLDFKQKHPRKTR
PVQKQDNFLSLLPAFVREKRS (in isoform 5).
{ECO:0000303|PubMed:16510313}.
/FTId=VSP_047796.
VAR_SEQ 359 417 IGFQVLLSIGELSLAIVIALMSGLLTGLLLNLKIWKAPHEA
KYFDDQVFWKFPHLAVGF -> SLGWNLAVKMAEAGDEELM
RLDVSQRNHGGAAVPTGSWMPSTETTIAPNYRDHISVVSSF
GCWILSKSIQEKQGLFKNKTTSSHCCLHLYVRNAHDSKVSN
VRAGTGVRENGVESFLCHSLRRISPFIMHCRIQQ (in
isoform 4).
{ECO:0000303|PubMed:16510313}.
/FTId=VSP_047797.
VAR_SEQ 379 417 Missing (in isoform 6).
{ECO:0000303|PubMed:16510313}.
/FTId=VSP_047798.
VARIANT 16 16 W -> C (in dbSNP:rs772865539).
{ECO:0000269|PubMed:7606008}.
/FTId=VAR_034455.
VARIANT 103 103 S -> C (in a breast cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_035615.
VARIANT 110 110 L -> P (in Tar antigen;
dbSNP:rs121912762).
{ECO:0000269|PubMed:7741145}.
/FTId=VAR_006919.
VARIANT 193 193 E -> K (in dbSNP:rs1053352).
/FTId=VAR_034456.
VARIANT 201 201 T -> R (in dbSNP:rs1053355).
/FTId=VAR_034457.
VARIANT 218 218 M -> I (in dbSNP:rs141540728).
{ECO:0000269|PubMed:1438298}.
/FTId=VAR_006920.
VARIANT 223 223 F -> V (found in RhDVa(FK) and RhDVa(TT);
dbSNP:rs1053356). {ECO:0000269|Ref.9}.
/FTId=VAR_013304.
VARIANT 233 233 E -> Q (found in RhDVa(FK), RhDVa(TO),
RhDVa(TT) and RhDYo; dbSNP:rs1053359).
{ECO:0000269|Ref.9}.
/FTId=VAR_013305.
VARIANT 238 238 V -> M (found in RhDVa(TO) and RhDVa(TT);
dbSNP:rs1053360). {ECO:0000269|Ref.9}.
/FTId=VAR_013306.
VARIANT 245 245 V -> L (found in RhDVa(TT);
dbSNP:rs150073306). {ECO:0000269|Ref.9}.
/FTId=VAR_013307.
VARIANT 263 263 G -> R (in dbSNP:rs3118454).
/FTId=VAR_047996.
VARIANT 306 306 V -> I (in dbSNP:rs590813).
/FTId=VAR_047997.
VARIANT 311 311 Y -> C (in dbSNP:rs590787).
/FTId=VAR_047998.
CONFLICT 39 39 E -> G (in Ref. 4; AAB26081).
{ECO:0000305}.
CONFLICT 103 103 S -> P (in Ref. 4; AAB26081).
{ECO:0000305}.
CONFLICT 127 127 V -> A (in Ref. 4; AAB26081).
{ECO:0000305}.
CONFLICT 174 174 V -> M (in Ref. 6; AAB34852).
{ECO:0000305}.
CONFLICT 182 182 S -> T (in Ref. 4; AAB26081).
{ECO:0000305}.
CONFLICT 314 314 G -> V (in Ref. 4; AAB26081 and 7;
AAB31911). {ECO:0000305}.
CONFLICT 323 323 P -> H (in Ref. 4; AAB26081).
{ECO:0000305}.
CONFLICT 379 379 M -> T (in Ref. 1; CAA44811/CAA44808, 3;
AAA02679, 4; AAB26081, 6; AAB34852 and 8;
BAA81899/BAA81900/BAA81901/BAA82159).
{ECO:0000305}.
CONFLICT 398 398 E -> V (in Ref. 6; AAB34852).
{ECO:0000305}.
SEQUENCE 417 AA; 45211 MW; 38721BFA664AE199 CRC64;
MSSKYPRSVR RCLPLWALTL EAALILLFYF FTHYDASLED QKGLVASYQV GQDLTVMAAI
GLGFLTSSFR RHSWSSVAFN LFMLALGVQW AILLDGFLSQ FPSGKVVITL FSIRLATMSA
LSVLISVDAV LGKVNLAQLV VMVLVEVTAL GNLRMVISNI FNTDYHMNMM HIYVFAAYFG
LSVAWCLPKP LPEGTEDKDQ TATIPSLSAM LGALFLWMFW PSFNSALLRS PIERKNAVFN
TYYAVAVSVV TAISGSSLAH PQGKISKTYV HSAVLAGGVA VGTSCHLIPS PWLAMVLGLV
AGLISVGGAK YLPGCCNRVL GIPHSSIMGY NFSLLGLLGE IIYIVLLVLD TVGAGNGMIG
FQVLLSIGEL SLAIVIALMS GLLTGLLLNL KIWKAPHEAK YFDDQVFWKF PHLAVGF


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137-A Blood Group Antibodies: anti-Rh(o)D and Rh(o)Dii human Rhesus system antigen IgG1 , Clone: 55_2_376 1mg
137-A Blood Group Antibodies: anti-Rh(o)D and Rh(o)Dii human Rhesus system antigen IgG1 , Clone: 55_2_376 100 ug/vial
99-812-L001 Mouse Monoclonal to Blood Group ABH Antigen Blood Group ABH Isotype IgM Antigen Blood Group ABH Isotype IgM 1.0 ml
99-806-L001 Mouse Monoclonal to Blood Group B Antigen Blood Group B Isotype IgM Antigen Blood Group B Isotype IgM 1.0 ml
99-809-L001 Mouse Monoclonal to Blood Group A Antigen Blood Group A Isotype IgM Antigen Blood Group A Isotype IgM 1.0 ml
99-807-L001 Mouse Monoclonal to Blood Group A1B Antigen Blood Group A1B Isotype IgM Antigen Blood Group A1B Isotype IgM 1.0 ml
99-805-L001 Mouse Monoclonal to Blood Group A Antigen Blood Group A Isotype IgM Antigen Blood Group A Isotype IgM 1.0 ml
E0391m Rat ELISA Kit FOR Blood group Rh(D) polypeptide 96T
OGRL1_RAT Rat ELISA Kit FOR Blood group Rh(D) polypeptide 96T
E1713m Mouse ELISA Kit FOR Blood group Rh(D) polypeptide 96T
E0742Ge Human ELISA Kit FOR Blood group Rh(CE) polypeptide
ZN175_HUMAN Human ELISA Kit FOR Blood group Rh(CE) polypeptide 96T
11-385-C025 Mouse Monoclonal to Blood Group Lewis a Antigen Blood Group Lewis a Isotype IgG1 Antigen Blood Group Lewis a Isotype IgG1 0.025 mg
11-386-C100 Mouse Monoclonal to Blood Group Lewis b Antigen Blood Group Lewis b Isotype IgG1 Antigen Blood Group Lewis b Isotype IgG1 0.1 mg


 

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