Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Protein S100-A11 (Calgizzarin) (Metastatic lymph node gene 70 protein) (MLN 70) (Protein S100-C) (S100 calcium-binding protein A11) [Cleaved into: Protein S100-A11, N-terminally processed]

 S10AB_HUMAN             Reviewed;         105 AA.
P31949; Q5VTK0;
01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 2.
18-JUL-2018, entry version 195.
RecName: Full=Protein S100-A11;
AltName: Full=Calgizzarin;
AltName: Full=Metastatic lymph node gene 70 protein;
Short=MLN 70;
AltName: Full=Protein S100-C;
AltName: Full=S100 calcium-binding protein A11;
Contains:
RecName: Full=Protein S100-A11, N-terminally processed;
Name=S100A11; Synonyms=MLN70, S100C;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=7889529; DOI=10.1016/0304-3835(94)03687-E;
Tanaka M., Adzuma K., Iwami M., Yoshimoto K., Monden Y., Itakura M.;
"Human calgizzarin; one colorectal cancer-related gene selected by a
large scale random cDNA sequencing and northern blot analysis.";
Cancer Lett. 89:195-200(1995).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Mammary carcinoma;
PubMed=7490069; DOI=10.1006/geno.1995.1163;
Tomasetto C.L., Regnier C.H., Moog-Lutz C., Mattei M.-G.,
Chenard M.-P., Lidereau R., Basset P., Rio M.-C.;
"Identification of four novel human genes amplified and overexpressed
in breast carcinoma and localized to the q11-q21.3 region of
chromosome 17.";
Genomics 28:367-376(1995).
[3]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Lung;
Nakatani K., Kato A., Sugimoto M., Kumano K., Komada T., Tsunoda H.,
Ito M., Nakano T., Shima T., Tanaka T.;
"Isolation and characterization of cDNA for human S100C protein and a
related gene.";
Submitted (OCT-1995) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Brain;
Fujiwara T., Kawai A., Shimizu F., Shinomiya K., Hirano H., Okuno S.,
Ozaki K., Katagiri T., Takeda S., Kuga Y., Shimada Y., Nagata M.,
Takaichi A., Watanabe T., Horie M., Nakamura Y., Takahashi E.,
Hirai Y.;
"Molecular cloning of a human homologue of the two calcium binding
protein, porcine S100 and rabbit calgizzarin.";
Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[6]
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).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Placenta, and Urinary bladder;
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).
[8]
PROTEIN SEQUENCE OF 4-12; 43-51 AND 56-62.
TISSUE=Keratinocyte;
PubMed=1286667; DOI=10.1002/elps.11501301199;
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E.,
Vandekerckhove J.;
"Microsequences of 145 proteins recorded in the two-dimensional gel
protein database of normal human epidermal keratinocytes.";
Electrophoresis 13:960-969(1992).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-3, 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).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND 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).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5 AND SER-6, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-6, 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).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[17]
STRUCTURE BY NMR OF 1-19, DISULFIDE BOND, PHOSPHORYLATION AT THR-10,
FUNCTION, AND SUBCELLULAR LOCATION.
PubMed=18618420; DOI=10.1002/psc.1050;
Kouno T., Mizuguchi M., Sakaguchi M., Makino E., Mori Y., Shinoda H.,
Aizawa T., Demura M., Huh N.H., Kawano K.;
"The structure of S100A11 fragment explains a local structural change
induced by phosphorylation.";
J. Pept. Sci. 14:1129-1138(2008).
-!- FUNCTION: Facilitates the differentiation and the cornification of
keratinocytes. {ECO:0000269|PubMed:18618420}.
-!- SUBUNIT: Homodimer; disulfide-linked.
{ECO:0000269|PubMed:18618420}.
-!- INTERACTION:
P04271:S100B; NbExp=5; IntAct=EBI-701862, EBI-458391;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18618420}.
Nucleus {ECO:0000269|PubMed:18618420}.
-!- PTM: Phosphorylation at Thr-10 by PRKCA significantly suppresses
homodimerization and promotes association with NCL/nucleolin which
induces nuclear translocation. {ECO:0000269|PubMed:18618420}.
-!- MISCELLANEOUS: Binds two calcium ions per molecule with an
affinity similar to that of the S-100 proteins. {ECO:0000250}.
-!- SIMILARITY: Belongs to the S-100 family. {ECO:0000305}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
Distributed under the Creative Commons Attribution (CC BY 4.0) License
-----------------------------------------------------------------------
EMBL; D38583; BAA07597.1; -; mRNA.
EMBL; X80201; CAA56492.1; -; mRNA.
EMBL; D49355; BAA08354.1; -; mRNA.
EMBL; D50374; BAA23325.1; -; mRNA.
EMBL; BT009912; AAP88914.1; -; mRNA.
EMBL; AL591893; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001410; AAH01410.1; -; mRNA.
EMBL; BC014354; AAH14354.1; -; mRNA.
CCDS; CCDS1009.1; -.
PIR; I37080; I37080.
RefSeq; NP_005611.1; NM_005620.1.
UniGene; Hs.417004; -.
PDB; 1V4Z; NMR; -; A=1-19.
PDB; 1V50; NMR; -; A=1-19.
PDB; 2LUC; NMR; -; A/B=1-105.
PDBsum; 1V4Z; -.
PDBsum; 1V50; -.
PDBsum; 2LUC; -.
ProteinModelPortal; P31949; -.
SMR; P31949; -.
BioGrid; 112190; 22.
IntAct; P31949; 13.
STRING; 9606.ENSP00000271638; -.
DrugBank; DB02482; Phosphonothreonine.
iPTMnet; P31949; -.
PhosphoSitePlus; P31949; -.
SwissPalm; P31949; -.
BioMuta; S100A11; -.
DMDM; 1710818; -.
DOSAC-COBS-2DPAGE; P31949; -.
SWISS-2DPAGE; P31949; -.
EPD; P31949; -.
PaxDb; P31949; -.
PeptideAtlas; P31949; -.
PRIDE; P31949; -.
ProteomicsDB; 54821; -.
TopDownProteomics; P31949; -.
DNASU; 6282; -.
Ensembl; ENST00000271638; ENSP00000271638; ENSG00000163191.
GeneID; 6282; -.
KEGG; hsa:6282; -.
CTD; 6282; -.
DisGeNET; 6282; -.
EuPathDB; HostDB:ENSG00000163191.5; -.
GeneCards; S100A11; -.
HGNC; HGNC:10488; S100A11.
HPA; CAB034320; -.
HPA; HPA042745; -.
MIM; 603114; gene.
neXtProt; NX_P31949; -.
OpenTargets; ENSG00000163191; -.
PharmGKB; PA34900; -.
eggNOG; ENOG410J1U7; Eukaryota.
eggNOG; ENOG410YYVE; LUCA.
GeneTree; ENSGT00760000119034; -.
HOGENOM; HOG000246968; -.
HOVERGEN; HBG001479; -.
InParanoid; P31949; -.
OMA; AQACHDS; -.
OrthoDB; EOG091G10QT; -.
PhylomeDB; P31949; -.
TreeFam; TF332727; -.
Reactome; R-HSA-6798695; Neutrophil degranulation.
ChiTaRS; S100A11; human.
EvolutionaryTrace; P31949; -.
GeneWiki; S100A11; -.
GenomeRNAi; 6282; -.
PRO; PR:P31949; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000163191; -.
CleanEx; HS_S100A11; -.
ExpressionAtlas; P31949; baseline and differential.
Genevisible; P31949; HS.
GO; GO:0005913; C:cell-cell adherens junction; HDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005576; C:extracellular region; HDA:BHF-UCL.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0001726; C:ruffle; IDA:UniProtKB.
GO; GO:0034774; C:secretory granule lumen; TAS:Reactome.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; HDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; TAS:ProtInc.
GO; GO:0008156; P:negative regulation of DNA replication; TAS:ProtInc.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
InterPro; IPR011992; EF-hand-dom_pair.
InterPro; IPR018247; EF_Hand_1_Ca_BS.
InterPro; IPR002048; EF_hand_dom.
InterPro; IPR001751; S100/CaBP-9k_CS.
InterPro; IPR013787; S100_Ca-bd_sub.
InterPro; IPR028482; S100A11.
PANTHER; PTHR11639:SF60; PTHR11639:SF60; 1.
Pfam; PF00036; EF-hand_1; 1.
Pfam; PF01023; S_100; 1.
SMART; SM00054; EFh; 1.
SMART; SM01394; S_100; 1.
SUPFAM; SSF47473; SSF47473; 1.
PROSITE; PS00018; EF_HAND_1; 1.
PROSITE; PS50222; EF_HAND_2; 1.
PROSITE; PS00303; S100_CABP; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Calcium; Complete proteome; Cytoplasm;
Direct protein sequencing; Disulfide bond; Metal-binding; Nucleus;
Phosphoprotein; Reference proteome; Repeat.
CHAIN 1 105 Protein S100-A11.
/FTId=PRO_0000424465.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:22814378}.
CHAIN 2 105 Protein S100-A11, N-terminally processed.
/FTId=PRO_0000144009.
DOMAIN 13 49 EF-hand 1. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
DOMAIN 55 90 EF-hand 2. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 25 38 1; low affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
CA_BIND 68 79 2; high affinity. {ECO:0000255|PROSITE-
ProRule:PRU00448}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:22814378}.
MOD_RES 2 2 N-acetylalanine; in Protein S100-A11, N-
terminally processed.
{ECO:0000244|PubMed:22814378}.
MOD_RES 3 3 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 5 5 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 6 6 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 10 10 Phosphothreonine.
{ECO:0000269|PubMed:18618420}.
MOD_RES 27 27 N6-acetyllysine.
{ECO:0000250|UniProtKB:P50543}.
DISULFID 13 13 Interchain.
{ECO:0000269|PubMed:18618420}.
HELIX 7 18 {ECO:0000244|PDB:1V4Z}.
STRAND 30 32 {ECO:0000244|PDB:2LUC}.
HELIX 36 45 {ECO:0000244|PDB:2LUC}.
HELIX 48 54 {ECO:0000244|PDB:2LUC}.
HELIX 58 67 {ECO:0000244|PDB:2LUC}.
STRAND 70 75 {ECO:0000244|PDB:2LUC}.
HELIX 77 96 {ECO:0000244|PDB:2LUC}.
SEQUENCE 105 AA; 11740 MW; 1729ED680290CFE4 CRC64;
MAKISSPTET ERCIESLIAV FQKYAGKDGY NYTLSKTEFL SFMNTELAAF TKNQKDPGVL
DRMMKKLDTN SDGQLDFSEF LNLIGGLAMA CHDSFLKAVP SQKRT


Related products :

Catalog number Product name Quantity
EIAAB36554 Calgizzarin,Homo sapiens,Human,Metastatic lymph node gene 70 protein,MLN 70,MLN70,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100A11,S100C
EIAAB36558 Calgizzarin,EMAP,Endothelial monocyte-activating polypeptide,Mouse,Mus musculus,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100a11,S100c
EIAAB36557 Calgizzarin,Oryctolagus cuniculus,PCALG,Protein S100-A11,Protein S100-C,Rabbit,S100 calcium-binding protein A11,S100A11,S100C
EIAAB36556 Calgizzarin,Pig,Protein S100-A11,Protein S100-C,S100 calcium-binding protein A11,S100A11,S100C,Sus scrofa
EIAAB36571 AAG13,Aging-associated gene 13 protein,Homo sapiens,Human,Protein S100-A16,Protein S100-F,S100 calcium-binding protein A16,S100A16,S100F
32-213 S100 calcium binding protein A1 (S100-alpha_ S100A1), The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localiz 0.1 mL
EIAAB36663 Homo sapiens,Human,Protein S100-A7A,S100 calcium-binding protein A15,S100 calcium-binding protein A7A,S100 calcium-binding protein A7-like 1,S100A15,S100A7A,S100A7L1
EIAAB36572 Mouse,Mus musculus,Protein S100-A15A,Protein S100-A7A,S100 calcium-binding protein A15A,S100 calcium-binding protein A7A,S100a15,S100a15a,S100a7,S100a7a
EIAAB36537 Capl,Metastasin,Metastatic cell protein,Mouse,Mts1,Mus musculus,PEL98,Placental calcium-binding protein,Protein 18A2,Protein Mts1,Protein S100-A4,S100 calcium-binding protein A4,S100a4
EIAAB36555 Calgizzarin,Protein S100-A11,Rat,Rattus norvegicus,S100 calcium-binding protein A11,S100a11
E2054h ELISA Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
U2054h CLIA kit Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
U2054h CLIA Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
E2054h ELISA kit Homo sapiens,Human,Protein S100-E,Protein S100-P,S100 calcium-binding protein P,S100E,S100P 96T
20-272-190393 S100 alpha 6 - Mouse monoclonal [CACY - 100] to S100 alpha 6; S100 calcium-binding protein A6; Calcyclin; Prolactin receptor-associated protein; PRA; Growth factor-inducible protein 2A9; MLN 4 Monoclo 0.1 ml
32-201 S100 calcium binding protein A10 (S100A10_P11), The protein encoded by this gene is a member of the S100 family of proteins containing 2 EF-hand calcium-binding motifs. S100 proteins are localized in 0.1 mL
EIAAB36559 Calgizzarin,Chicken,Gallus gallus,Protein S100-A11,S100 calcium-binding protein A11,S100A11
15-288-22597F Protein S100-A6 - S100 calcium-binding protein A6; Calcyclin; Prolactin receptor-associated protein; PRA; Growth factor-inducible protein 2A9; MLN 4 Polyclonal 0.05 mg
15-288-22597F Protein S100-A6 - S100 calcium-binding protein A6; Calcyclin; Prolactin receptor-associated protein; PRA; Growth factor-inducible protein 2A9; MLN 4 Polyclonal 0.1 mg
EIAAB36540 Metastasin,Nerve growth factor-induced protein 42A,P9K,Placental calcium-binding protein,Protein S100-A4,Rat,Rattus norvegicus,S100 calcium-binding protein A4,S100a4
E1769h ELISA kit CACY,Calcyclin,Growth factor-inducible protein 2A9,Homo sapiens,Human,MLN 4,PRA,Prolactin receptor-associated protein,Protein S100-A6,S100 calcium-binding protein A6,S100A6 96T
E1769h ELISA CACY,Calcyclin,Growth factor-inducible protein 2A9,Homo sapiens,Human,MLN 4,PRA,Prolactin receptor-associated protein,Protein S100-A6,S100 calcium-binding protein A6,S100A6 96T
U1769h CLIA CACY,Calcyclin,Growth factor-inducible protein 2A9,Homo sapiens,Human,MLN 4,PRA,Prolactin receptor-associated protein,Protein S100-A6,S100 calcium-binding protein A6,S100A6 96T
DL-S100-Hu Human S100 Calcium Binding Protein (S100) ELISA Kit 96T
DL-S100-b Bovine S100 Calcium Binding Protein (S100) ELISA Kit 96T


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur