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Protein Red (Cytokine IK) (IK factor) (Protein RER)

 RED_HUMAN               Reviewed;         557 AA.
Q13123; Q6IPD8;
15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
18-MAY-2010, sequence version 3.
22-NOV-2017, entry version 137.
RecName: Full=Protein Red {ECO:0000303|PubMed:10216252};
AltName: Full=Cytokine IK {ECO:0000303|PubMed:7970704};
AltName: Full=IK factor {ECO:0000303|PubMed:7970704};
AltName: Full=Protein RER;
Name=IK; Synonyms=RED {ECO:0000303|PubMed:10216252}, RER;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
TISSUE=Leukemia;
PubMed=10216252; DOI=10.1016/S0378-1119(99)00066-9;
Assier E., Bouzinba-Segard H., Stolzenberg M.-C., Stephens R.,
Bardos J., Freemont P., Charron D., Trowsdale J., Rich T.;
"Isolation, sequencing and expression of RED, a novel human gene
encoding an acidic-basic dipeptide repeat.";
Gene 230:145-154(1999).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 316-477.
TISSUE=Leukemia;
PubMed=7970704;
Krief P., Augery-Bourget Y., Plaisance S., Merck M.F., Assier E.,
Tanchou V., Billard M., Boucheix C., Jasmin C., Azzarone B.;
"A new cytokine (IK) down-regulating HLA class II: monoclonal
antibodies, cloning and chromosome localization.";
Oncogene 9:3449-3456(1994).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-485, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460, 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).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-98, 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).
[9]
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).
[10]
FUNCTION, INTERACTION WITH MAD1L1, SUBCELLULAR LOCATION, AND
INDUCTION.
PubMed=22351768; DOI=10.1074/jbc.M111.299131;
Yeh P.C., Yeh C.C., Chen Y.C., Juang Y.L.;
"RED, a spindle pole-associated protein, is required for kinetochore
localization of MAD1, mitotic progression, and activation of the
spindle assembly checkpoint.";
J. Biol. Chem. 287:11704-11716(2012).
[11]
SUBUNIT, AND INTERACTION WITH SMU1.
PubMed=22365833; DOI=10.1016/j.molcel.2011.12.034;
Hegele A., Kamburov A., Grossmann A., Sourlis C., Wowro S.,
Weimann M., Will C.L., Pena V., Luehrmann R., Stelzl U.;
"Dynamic protein-protein interaction wiring of the human
spliceosome.";
Mol. Cell 45:567-580(2012).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-287; SER-417 AND
SER-536, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Erythroleukemia;
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).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH DHX15.
PubMed=24252166; DOI=10.1186/2050-7771-1-11;
Hu L., Yang F., Liu X., Xu D., Dai W.;
"Nuclear protein IK undergoes dynamic subcellular translocation and
forms unique nuclear bodies during the cell cycle.";
Biomark. Res. 1:11-11(2013).
[14]
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).
[15]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-544, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[16]
FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SMU1, INTERACTION
(MICROBIAL INFECTION) WITH INFLUENZA A VIRUS RNA POLYMERASE SUBUNITS
PB1 AND PB2, AND SUBCELLULAR LOCATION.
PubMed=24945353; DOI=10.1371/journal.ppat.1004164;
Fournier G., Chiang C., Munier S., Tomoiu A., Demeret C.,
Vidalain P.O., Jacob Y., Naffakh N.;
"Recruitment of RED-SMU1 complex by Influenza A Virus RNA polymerase
to control Viral mRNA splicing.";
PLoS Pathog. 10:E1004164-E1004164(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-151; LYS-310; LYS-331;
LYS-386; LYS-388; LYS-404; LYS-408; LYS-496; LYS-501; LYS-509;
LYS-541; LYS-543; LYS-544 AND LYS-553, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Auxiliary spliceosomal protein that regulates selection
of alternative splice sites in a small set of target pre-mRNA
species (Probable). Required for normal mitotic cell cycle
progression (PubMed:22351768, PubMed:24252166). Recruits MAD1L1
and MAD2L1 to kinetochores, and is required to trigger the spindle
assembly checkpoint (PubMed:22351768). Required for normal
accumulation of SMU1 (PubMed:24945353).
{ECO:0000269|PubMed:22351768, ECO:0000269|PubMed:24252166,
ECO:0000269|PubMed:24945353, ECO:0000305}.
-!- FUNCTION: (Microbial infection) Required, together with SMU1, for
normal splicing of influenza A virus NS1 pre-mRNA, which is
required for the production of the exportin NS2 and for the
production of influenza A virus particles. Not required for the
production of VSV virus particles. {ECO:0000269|PubMed:24945353}.
-!- SUBUNIT: (Microbial infection) Identified in a complex with SMU1
and influenza A virus RNA polymerase subunits PB1 and PB2.
Directly interacts with SMU1 and with influenza A virus RNA
polymerase subunits PB1 and PB2. {ECO:0000269|PubMed:22365833}.
-!- SUBUNIT: Interacts with SMU1 (PubMed:22365833, PubMed:24945353).
Probable component of the spliceosome B complex (PubMed:22365833).
Interacts with MAD1L1 (PubMed:22351768). May interact with DHX15
(PubMed:24252166). {ECO:0000269|PubMed:22351768,
ECO:0000269|PubMed:24945353, ECO:0000305|PubMed:22365833,
ECO:0000305|PubMed:24252166}.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-713456, EBI-713456;
O14965:AURKA; NbExp=3; IntAct=EBI-713456, EBI-448680;
Q8NHQ1:CEP70; NbExp=3; IntAct=EBI-713456, EBI-739624;
Q15029:EFTUD2; NbExp=2; IntAct=EBI-713456, EBI-357897;
Q70Z53:FRA10AC1; NbExp=2; IntAct=EBI-713456, EBI-710176;
P55081:MFAP1; NbExp=2; IntAct=EBI-713456, EBI-1048159;
O94906:PRPF6; NbExp=2; IntAct=EBI-713456, EBI-536755;
P98175:RBM10; NbExp=2; IntAct=EBI-713456, EBI-721525;
P04618:rev (xeno); NbExp=3; IntAct=EBI-713456, EBI-6164309;
O15541:RNF113A; NbExp=2; IntAct=EBI-713456, EBI-2130294;
Q2TAY7:SMU1; NbExp=6; IntAct=EBI-713456, EBI-298027;
Q8TAD8:SNIP1; NbExp=2; IntAct=EBI-713456, EBI-749336;
Q9HCS7:XAB2; NbExp=2; IntAct=EBI-713456, EBI-295232;
Q96NB3:ZNF830; NbExp=2; IntAct=EBI-713456, EBI-3920997;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24945353}.
Nucleus, nucleoplasm {ECO:0000269|PubMed:24252166,
ECO:0000269|PubMed:24945353}. Chromosome
{ECO:0000269|PubMed:24252166}. Cytoplasm, cytoskeleton, spindle
pole {ECO:0000269|PubMed:22351768}. Note=Predominantly present
throughout the nucleoplasm during prometaphase, metaphase and
anaphase. Is also detected in nuclear foci that are not identical
with Cajal bodies. Starts to accumulate at chromosomes during
telophase, and is nearly exclusively associated with chromosomes
in newly divided cells (PubMed:24252166). Colocalizes with MAD1L1
at mitotic spindle poles during metaphase and anaphase
(PubMed:22351768). {ECO:0000269|PubMed:24252166}.
-!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:10216252}.
-!- DEVELOPMENTAL STAGE: Expressed at similar levels in fetal and
adult tissues. {ECO:0000269|PubMed:10216252}.
-!- INDUCTION: Up-regulated during mitosis (at protein level).
{ECO:0000269|PubMed:22351768}.
-!- SIMILARITY: Belongs to the RED family. {ECO:0000305}.
-!- CAUTION: Was originally thought to be the IK factor, a cytokine
involved in the negative regulatory pathway of constitutive MHC
class II antigens expression. {ECO:0000305|PubMed:7970704}.
-----------------------------------------------------------------------
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EMBL; AJ005579; CAA06607.1; -; mRNA.
EMBL; AC116353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC071964; AAH71964.1; -; mRNA.
EMBL; S74221; AAB32531.1; -; mRNA.
CCDS; CCDS47280.1; -.
PIR; I58408; I58408.
RefSeq; NP_006074.2; NM_006083.3.
UniGene; Hs.421245; -.
PDB; 5O9Z; EM; 4.50 A; R=1-557.
PDBsum; 5O9Z; -.
ProteinModelPortal; Q13123; -.
SMR; Q13123; -.
BioGrid; 109766; 86.
CORUM; Q13123; -.
IntAct; Q13123; 41.
MINT; MINT-1371308; -.
STRING; 9606.ENSP00000396301; -.
BindingDB; Q13123; -.
ChEMBL; CHEMBL2321616; -.
iPTMnet; Q13123; -.
PhosphoSitePlus; Q13123; -.
BioMuta; IK; -.
DMDM; 296452987; -.
EPD; Q13123; -.
MaxQB; Q13123; -.
PaxDb; Q13123; -.
PeptideAtlas; Q13123; -.
PRIDE; Q13123; -.
Ensembl; ENST00000417647; ENSP00000396301; ENSG00000113141.
GeneID; 3550; -.
KEGG; hsa:3550; -.
UCSC; uc003lgq.4; human.
CTD; 3550; -.
DisGeNET; 3550; -.
EuPathDB; HostDB:ENSG00000113141.15; -.
GeneCards; IK; -.
HGNC; HGNC:5958; IK.
HPA; HPA048798; -.
MIM; 600549; gene.
neXtProt; NX_Q13123; -.
OpenTargets; ENSG00000113141; -.
PharmGKB; PA29774; -.
eggNOG; KOG2498; Eukaryota.
eggNOG; ENOG410YR3Z; LUCA.
GeneTree; ENSGT00630000089902; -.
HOGENOM; HOG000007717; -.
HOVERGEN; HBG017223; -.
InParanoid; Q13123; -.
KO; K13109; -.
OMA; LEEMNDA; -.
OrthoDB; EOG091G0BYA; -.
PhylomeDB; Q13123; -.
TreeFam; TF321907; -.
ChiTaRS; IK; human.
GeneWiki; IK_(gene); -.
GenomeRNAi; 3550; -.
PMAP-CutDB; Q13123; -.
PRO; PR:Q13123; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000113141; -.
CleanEx; HS_IK; -.
ExpressionAtlas; Q13123; baseline and differential.
Genevisible; Q13123; HS.
GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
GO; GO:0000922; C:spindle pole; IEA:UniProtKB-SubCell.
GO; GO:0005681; C:spliceosomal complex; IEA:UniProtKB-KW.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0000278; P:mitotic cell cycle; IMP:UniProtKB.
GO; GO:0007094; P:mitotic spindle assembly checkpoint; IMP:UniProtKB.
GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
GO; GO:0034501; P:protein localization to kinetochore; IMP:UniProtKB.
GO; GO:0008380; P:RNA splicing; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR012492; RED_C.
InterPro; IPR012916; RED_N.
Pfam; PF07807; RED_C; 1.
Pfam; PF07808; RED_N; 1.
ProDom; PD311621; RED_C; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Complete proteome; Cytoplasm;
Cytoskeleton; Host-virus interaction; Isopeptide bond;
mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
Reference proteome; Repeat; Spliceosome; Ubl conjugation.
CHAIN 1 557 Protein Red.
/FTId=PRO_0000097235.
REPEAT 342 343 1.
REPEAT 344 345 2.
REPEAT 346 347 3.
REPEAT 348 349 4.
REPEAT 350 351 5.
REPEAT 352 353 6.
REPEAT 354 355 7.
REPEAT 356 357 8.
REPEAT 358 359 9.
REPEAT 360 361 10.
REPEAT 362 363 11.
REPEAT 364 365 12.
REPEAT 366 367 13.
REPEAT 368 369 14.
REPEAT 370 371 15.
REPEAT 372 373 16.
REPEAT 374 375 17.
REGION 342 375 17 X 2 AA tandem repeats of R-[ED].
COMPBIAS 182 187 Poly-Glu. {ECO:0000255}.
COMPBIAS 334 374 Arg-rich. {ECO:0000255|PROSITE-
ProRule:PRU00002}.
MOD_RES 98 98 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 137 137 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q9Z1M8}.
MOD_RES 287 287 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 417 417 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 460 460 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 485 485 Phosphothreonine.
{ECO:0000244|PubMed:17525332}.
MOD_RES 536 536 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
CROSSLNK 151 151 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 310 310 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 331 331 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 386 386 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 388 388 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 404 404 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 408 408 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 496 496 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 501 501 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 509 509 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 541 541 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 543 543 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 544 544 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
CROSSLNK 553 553 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CONFLICT 176 176 A -> L (in Ref. 1; CAA06607).
{ECO:0000305}.
CONFLICT 182 182 E -> D (in Ref. 1; CAA06607).
{ECO:0000305}.
SEQUENCE 557 AA; 65602 MW; BE7B332985D5F4CA CRC64;
MPERDSEPFS NPLAPDGHDV DDPHSFHQSK LTNEDFRKLL MTPRAAPTSA PPSKSRHHEM
PREYNEDEDP AARRRKKKSY YAKLRQQEIE RERELAEKYR DRAKERRDGV NKDYEETELI
STTANYRAVG PTAEADKSAA EKRRQLIQES KFLGGDMEHT HLVKGLDFAL LQKVRAEIAS
KEKEEEELME KPQKETKKDE DPENKIEFKT RLGRNVYRML FKSKAYERNE LFLPGRMAYV
VDLDDEYADT DIPTTLIRSK ADCPTMEAQT TLTTNDIVIS KLTQILSYLR QGTRNKKLKK
KDKGKLEEKK PPEADMNIFE DIGDYVPSTT KTPRDKERER YRERERDRER DRDRDRERER
ERDRERERER DREREEEKKR HSYFEKPKVD DEPMDVDKGP GSTKELIKSI NEKFAGSAGW
EGTESLKKPE DKKQLGDFFG MSNSYAECYP ATMDDMAVDS DEEVDYSKMD QGNKKGPLGR
WDFDTQEEYS EYMNNKEALP KAAFQYGIKM SEGRKTRRFK ETNDKAELDR QWKKISAIIE
KRKKMEADGV EVKRPKY


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31-142 TNFSF12 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is a ligand for the FN14_TWEAKR receptor. This cytokine has overlapping signaling functions with TNF, 0.05 mg
25-364 TNFSF12 is a cytokine that belongs to the tumor necrosis factor (TNF) ligand family. This protein is a ligand for the FN14_TWEAKR receptor. This cytokine has overlapping signaling functions with TNF, 0.05 mg
E1792m ELISA Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine,Prote 96T
U1792m CLIA Caga,Calgranulin-A,Chemotactic cytokine CP-10,Leukocyte L1 complex light chain,Migration inhibitory factor-related protein 8,Mouse,Mrp8,MRP-8,Mus musculus,p8,Pro-inflammatory S100 cytokine,Protei 96T
EIAAB34192 Cytokine IK,Homo sapiens,Human,IK,IK factor,Protein Red,Protein RER,RED,RER
EIAAB07441 CIS,CIS-1,CISH,Cytokine-inducible SH2-containing protein,G18,Homo sapiens,Human,Protein G18,SOCS,Suppressor of cytokine signaling
EIAAB09417 CLF-1,Crlf1,Crlm3,CRLM-3,Cytokine receptor-like factor 1,Cytokine receptor-like molecule 3,Cytokine-like factor 1,Mouse,Mus musculus,Novel cytokine receptor 6,NR6
EIAAB34194 Cytokine IK,Ik,IK factor,Mouse,Mus musculus,Protein Red,Protein RER,Red,Rer
E1684m ELISA Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
E1684m ELISA kit Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
U1684m CLIA Cis3,CIS-3,Cish3,Cytokine-inducible SH2 protein 3,Mouse,Mus musculus,Protein EF-10,Socs3,SOCS-3,Suppressor of cytokine signaling 3 96T
U2103m CLIA Cytokine CX1,Cytokine-like protein ZCYTO7,Il17b,IL-17B,Interleukin-17B,Mouse,Mus musculus,Neuronal interleukin-17-related factor,Nirf,Zcyto7 96T
E2103m ELISA Cytokine CX1,Cytokine-like protein ZCYTO7,Il17b,IL-17B,Interleukin-17B,Mouse,Mus musculus,Neuronal interleukin-17-related factor,Nirf,Zcyto7 96T
U2103m CLIA kit Cytokine CX1,Cytokine-like protein ZCYTO7,Il17b,IL-17B,Interleukin-17B,Mouse,Mus musculus,Neuronal interleukin-17-related factor,Nirf,Zcyto7 96T
E2103m ELISA kit Cytokine CX1,Cytokine-like protein ZCYTO7,Il17b,IL-17B,Interleukin-17B,Mouse,Mus musculus,Neuronal interleukin-17-related factor,Nirf,Zcyto7 96T
EIAAB09419 CRL2,CRLF2,Cytokine receptor-like 2,Cytokine receptor-like factor 2,Homo sapiens,Human,ILXR,IL-XR,Thymic stromal lymphopoietin protein receptor,TSLP receptor,TSLPR
EIAAB09421 Creme9,CREME-9,Crlf3,Cytokine receptor-like factor 3,Cytokine receptor-like molecule 9,Cytokine receptor-related factor 4,Cytor4,Mouse,Mus musculus
EIAAB14391 Cytokine-like protein 2-21,Fam3b,Mouse,Mus musculus,ORF9,Pancreatic-derived factor,PANDER,Protein FAM3B
EIAAB14390 C21orf11,C21orf76,Cytokine-like protein 2-21,FAM3B,Homo sapiens,Human,Pancreatic-derived factor,PANDER,PRED44,Protein FAM3B,UNQ320_PRO365


 

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