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Annexin A4 (35-beta calcimedin) (Annexin IV) (Annexin-4) (Carbohydrate-binding protein p33/p41) (Chromobindin-4) (Endonexin I) (Lipocortin IV) (P32.5) (PP4-X) (Placental anticoagulant protein II) (PAP-II) (Protein II)

 ANXA4_HUMAN             Reviewed;         319 AA.
P09525; B4DDF9; Q96F33; Q9BWK1;
01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 4.
27-SEP-2017, entry version 187.
RecName: Full=Annexin A4;
AltName: Full=35-beta calcimedin;
AltName: Full=Annexin IV;
AltName: Full=Annexin-4;
AltName: Full=Carbohydrate-binding protein p33/p41;
AltName: Full=Chromobindin-4;
AltName: Full=Endonexin I;
AltName: Full=Lipocortin IV;
AltName: Full=P32.5;
AltName: Full=PP4-X;
AltName: Full=Placental anticoagulant protein II;
Short=PAP-II;
AltName: Full=Protein II;
Name=ANXA4; Synonyms=ANX4;
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).
PubMed=2970257;
Grundmann U., Amann E., Abel K.-J., Kuepper H.A.;
"Isolation and expression of cDNA coding for a new member of the
phospholipase A2 inhibitor family.";
Behring Inst. Mitt. 82:59-67(1988).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=1346776; DOI=10.1016/0888-7543(92)90379-7;
Tait J.F., Smith C., Frankenberry D.A., Miao C.H., Adler D.A.,
Disteche C.M.;
"Chromosomal mapping of the human annexin IV (ANX4) gene.";
Genomics 12:313-318(1992).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=9084877; DOI=10.1248/bpb.20.224;
Satoh A., Takayama E., Kojima K., Ogawa H., Katsura Y., Kina T.,
Matsumoto I.;
"Characterization of human p33/41 (annexin IV), a Ca2+ dependent
carbohydrate-binding protein with monoclonal anti-annexin IV
antibodies, AS11 and AS17.";
Biol. Pharm. Bull. 20:224-229(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Adrenal gland;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Eye, and Uterus;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-15; 28-72; 100-144 AND 281-319.
PubMed=2975506; DOI=10.1021/bi00417a011;
Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T.,
Hendrickson L.E., Fujikawa K.;
"Placental anticoagulant proteins: isolation and comparative
characterization four members of the lipocortin family.";
Biochemistry 27:6268-6276(1988).
[8]
PROTEIN SEQUENCE OF 27-56; 99-124 AND 280-308.
TISSUE=Placenta;
PubMed=2974032;
Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
de Haen C.;
"Sedimentation equilibrium analysis of five lipocortin-related
phospholipase A2 inhibitors from human placenta. Evidence against a
mechanistically relevant association between enzyme and inhibitor.";
J. Biol. Chem. 263:18657-18663(1988).
[9]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213; LYS-293 AND LYS-300,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[11]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[13]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=2254922; DOI=10.1016/S0022-2836(05)80310-9;
Freemont P.S., Driessen H.P.C., Verbi W., Crumpton M.J.;
"Crystallization and preliminary X-ray crystallographic studies of
human placental annexin IV.";
J. Mol. Biol. 216:219-221(1990).
-!- FUNCTION: Calcium/phospholipid-binding protein which promotes
membrane fusion and is involved in exocytosis. {ECO:0000250}.
-!- INTERACTION:
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-2556852, EBI-717399;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P09525-1; Sequence=Displayed;
Name=2;
IsoId=P09525-2; Sequence=VSP_056396;
Note=No experimental confirmation available.;
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAC41689.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH00182.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH11659.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=BAA11227.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; M19383; AAC41689.1; ALT_INIT; mRNA.
EMBL; M82809; AAA51740.1; -; mRNA.
EMBL; D78152; BAA11227.1; ALT_INIT; mRNA.
EMBL; AK293177; BAG56720.1; -; mRNA.
EMBL; AC019206; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC092431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC112787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000182; AAH00182.1; ALT_INIT; mRNA.
EMBL; BC011659; AAH11659.1; ALT_INIT; mRNA.
PIR; A42077; A42077.
RefSeq; NP_001144.1; NM_001153.4.
RefSeq; NP_001307627.1; NM_001320698.1.
RefSeq; NP_001307629.1; NM_001320700.1.
RefSeq; NP_001307631.1; NM_001320702.1. [P09525-2]
RefSeq; XP_016859432.1; XM_017003943.1.
RefSeq; XP_016859433.1; XM_017003944.1. [P09525-2]
UniGene; Hs.422986; -.
PDB; 2ZOC; X-ray; 2.00 A; A/B=1-319.
PDBsum; 2ZOC; -.
ProteinModelPortal; P09525; -.
SMR; P09525; -.
BioGrid; 106804; 21.
IntAct; P09525; 6.
MINT; MINT-4528752; -.
STRING; 9606.ENSP00000377833; -.
iPTMnet; P09525; -.
PhosphoSitePlus; P09525; -.
SwissPalm; P09525; -.
BioMuta; ANXA4; -.
DMDM; 1703319; -.
DOSAC-COBS-2DPAGE; P09525; -.
OGP; P09525; -.
REPRODUCTION-2DPAGE; IPI00793199; -.
REPRODUCTION-2DPAGE; P09525; -.
SWISS-2DPAGE; P09525; -.
EPD; P09525; -.
MaxQB; P09525; -.
PaxDb; P09525; -.
PeptideAtlas; P09525; -.
PRIDE; P09525; -.
DNASU; 307; -.
Ensembl; ENST00000394295; ENSP00000377833; ENSG00000196975.
Ensembl; ENST00000536030; ENSP00000441931; ENSG00000196975.
GeneID; 307; -.
KEGG; hsa:307; -.
CTD; 307; -.
DisGeNET; 307; -.
EuPathDB; HostDB:ENSG00000196975.15; -.
GeneCards; ANXA4; -.
HGNC; HGNC:542; ANXA4.
HPA; CAB005076; -.
HPA; CAB017560; -.
HPA; HPA007393; -.
MIM; 106491; gene.
neXtProt; NX_P09525; -.
PharmGKB; PA24832; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
HOVERGEN; HBG061815; -.
InParanoid; P09525; -.
KO; K17093; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P09525; -.
TreeFam; TF105452; -.
ChiTaRS; ANXA4; human.
EvolutionaryTrace; P09525; -.
GeneWiki; ANXA4; -.
GenomeRNAi; 307; -.
PRO; PR:P09525; -.
Proteomes; UP000005640; Chromosome 2.
Bgee; ENSG00000196975; -.
CleanEx; HS_ANXA4; -.
ExpressionAtlas; P09525; baseline and differential.
Genevisible; P09525; HS.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0012506; C:vesicle membrane; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL.
GO; GO:0004859; F:phospholipase inhibitor activity; NAS:UniProtKB.
GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:2000483; P:negative regulation of interleukin-8 secretion; IMP:BHF-UCL.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IDA:BHF-UCL.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR002391; ANX4.
PANTHER; PTHR10502:SF166; PTHR10502:SF166; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Annexin; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Phosphoprotein; Polymorphism;
Reference proteome; Repeat.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:22814378,
ECO:0000269|PubMed:2975506}.
CHAIN 2 319 Annexin A4.
/FTId=PRO_0000067482.
REPEAT 23 83 Annexin 1.
REPEAT 95 155 Annexin 2.
REPEAT 179 239 Annexin 3.
REPEAT 254 314 Annexin 4.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 7 7 Phosphothreonine.
{ECO:0000250|UniProtKB:P08132}.
MOD_RES 12 12 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 213 213 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 293 293 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 300 300 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
VAR_SEQ 1 82 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_056396.
VARIANT 85 85 T -> M (in dbSNP:rs2228203).
/FTId=VAR_055500.
CONFLICT 96 96 R -> Q (in Ref. 1; AAC41689).
{ECO:0000305}.
HELIX 16 26 {ECO:0000244|PDB:2ZOC}.
STRAND 28 31 {ECO:0000244|PDB:2ZOC}.
HELIX 34 41 {ECO:0000244|PDB:2ZOC}.
HELIX 46 59 {ECO:0000244|PDB:2ZOC}.
HELIX 64 71 {ECO:0000244|PDB:2ZOC}.
HELIX 74 84 {ECO:0000244|PDB:2ZOC}.
HELIX 87 99 {ECO:0000244|PDB:2ZOC}.
STRAND 100 103 {ECO:0000244|PDB:2ZOC}.
HELIX 106 115 {ECO:0000244|PDB:2ZOC}.
HELIX 118 132 {ECO:0000244|PDB:2ZOC}.
HELIX 136 143 {ECO:0000244|PDB:2ZOC}.
HELIX 146 155 {ECO:0000244|PDB:2ZOC}.
TURN 156 158 {ECO:0000244|PDB:2ZOC}.
HELIX 168 181 {ECO:0000244|PDB:2ZOC}.
TURN 182 184 {ECO:0000244|PDB:2ZOC}.
STRAND 185 187 {ECO:0000244|PDB:2ZOC}.
HELIX 190 199 {ECO:0000244|PDB:2ZOC}.
HELIX 202 216 {ECO:0000244|PDB:2ZOC}.
HELIX 220 227 {ECO:0000244|PDB:2ZOC}.
HELIX 230 244 {ECO:0000244|PDB:2ZOC}.
HELIX 246 258 {ECO:0000244|PDB:2ZOC}.
STRAND 259 262 {ECO:0000244|PDB:2ZOC}.
HELIX 265 275 {ECO:0000244|PDB:2ZOC}.
TURN 276 279 {ECO:0000244|PDB:2ZOC}.
HELIX 280 291 {ECO:0000244|PDB:2ZOC}.
HELIX 295 302 {ECO:0000244|PDB:2ZOC}.
HELIX 305 315 {ECO:0000244|PDB:2ZOC}.
SEQUENCE 319 AA; 35883 MW; 3799FE80A93AB215 CRC64;
MATKGGTVKA ASGFNAMEDA QTLRKAMKGL GTDEDAIISV LAYRNTAQRQ EIRTAYKSTI
GRDLIDDLKS ELSGNFEQVI VGMMTPTVLY DVQELRRAMK GAGTDEGCLI EILASRTPEE
IRRISQTYQQ QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DEGNYLDDAL VRQDAQDLYE
AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV
KCMRNKSAYF AEKLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRAHFKRL YGKSLYSFIK
GDTSGDYRKV LLVLCGGDD


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E1731p ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Chromobindin-4,Endonexin I,Lipocortin IV,P32.5,PAP-II,Pig,Placental anticoagulant protein II,PP4-X,Protein II,Sus scrofa 96T
E1731h ELISA kit 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoa 96T
E1731h ELISA 35-beta calcimedin,Annexin A4,Annexin IV,Annexin-4,ANX4,ANXA4,Carbohydrate-binding protein p33_p41,Chromobindin-4,Endonexin I,Homo sapiens,Human,Lipocortin IV,P32.5,PAP-II,Placental anticoagulan 96T
U0259m CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
U0259r CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattus norv 96T
U0259b CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,T 96T
E0259m ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I 96T
E0259b ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I, 96T
E0259r ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattu 96T
E0259r ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant protein I,PP4,Rat,Rattus nor 96T
E0259b ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Bos taurus,Bovine,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prote 96T
E0259m ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,Anx5,Anxa5,Calphobindin I,CBP-I,Endonexin II,Lipocortin V,Mouse,Mus musculus,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prot 96T
E0259h ELISA kit Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant 96T
U0259h CLIA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prote 96T
E0259h ELISA Anchorin CII,Annexin A5,Annexin V,Annexin-5,ANX5,ANXA5,Calphobindin I,CBP-I,Endonexin II,ENX2,Homo sapiens,Human,Lipocortin V,PAP-I,Placental anticoagulant protein 4,Placental anticoagulant prot 96T
18-272-196776 Annexin II - Rabbit polyclonal to Annexin II; Annexin-2; Annexin II; Lipocortin II; Calpactin I heavy chain; Chromobindin-8; p36; Protein I; Placental anticoagulant protein IV; PAP-IV Polyclonal 0.1 mg
10-664-50002 Annexin A3 - Annexin III; Lipocortin III; Placental anticoagulant protein III; PAP-III; 35-alpha calcimedin; Inositol 1.2-cyclic phosphate 2-phosphohydrolase N_A 0.05 mg


 

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