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Keratin, type I cytoskeletal 18 (Cytokeratin endo B) (Keratin D) (Cytokeratin-18) (CK-18) (Keratin-18) (K18)

 K1C18_MOUSE             Reviewed;         423 AA.
P05784; Q3TIX1; Q3TJH6; Q3TJW7; Q61766;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
29-MAY-2007, sequence version 5.
30-AUG-2017, entry version 154.
RecName: Full=Keratin, type I cytoskeletal 18;
AltName: Full=Cytokeratin endo B;
Short=Keratin D;
AltName: Full=Cytokeratin-18;
Short=CK-18;
AltName: Full=Keratin-18;
Short=K18;
Name=Krt18; Synonyms=Kerd, Krt1-18;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND INDUCTION.
TISSUE=Endoderm;
PubMed=2416755;
Singer P.A., Trevor K., Oshima R.G.;
"Molecular cloning and characterization of the Endo B cytokeratin
expressed in preimplantation mouse embryos.";
J. Biol. Chem. 261:538-547(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Teratocarcinoma;
Alonso A., Weber T., Jorcano J.L.;
"Cloning and characterization of keratin D, a murine endodermal
cytoskeletal protein induced during in vitro differentiation of F9
teratocarcinoma cells.";
Roux's Arch. Dev. Biol. 196:16-21(1987).
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/SvJ; TISSUE=Liver;
PubMed=2467843; DOI=10.1016/0378-1119(88)90107-2;
Ichinose Y., Morita T., Zhang F., Srimahasongcram S., Tondella M.L.C.,
Matsumoto M., Nozaki M., Matsushiro A.;
"Nucleotide sequence and structure of the mouse cytokeratin endoB
gene.";
Gene 70:85-95(1988).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Blastocyst, Embryo, and Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Eye;
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).
[6]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-132, AND TISSUE SPECIFICITY.
PubMed=2454868; DOI=10.1101/gad.2.5.505;
Oshima R.G., Trevor K., Shevinsky L.H., Ryder O.A., Cecena G.;
"Identification of the gene coding for the Endo B murine cytokeratin
and its methylated, stable inactive state in mouse nonepithelial
cells.";
Genes Dev. 2:505-516(1988).
[7]
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=7504637; DOI=10.1006/dbio.1993.1326;
Thorey I.S., Meneses J.J., Neznanov N., Kulesh D.A., Pedersen R.A.,
Oshima R.G.;
"Embryonic expression of human keratin 18 and K18-beta-galactosidase
fusion genes in transgenic mice.";
Dev. Biol. 160:519-534(1993).
[8]
DEVELOPMENTAL STAGE.
PubMed=7507912;
Dixon M.J., Robinson V., White A., Ferguson M.W.;
"Monoclonal antibodies recognising stage and region specific epitopes
in embryonic mouse palatal epithelial cells.";
J. Anat. 183:423-438(1993).
[9]
CLEAVAGE BY CASPASES.
PubMed=9298992; DOI=10.1083/jcb.138.6.1379;
Caulin C., Salvesen G.S., Oshima R.G.;
"Caspase cleavage of keratin 18 and reorganization of intermediate
filaments during epithelial cell apoptosis.";
J. Cell Biol. 138:1379-1394(1997).
[10]
DEVELOPMENTAL STAGE.
PubMed=16973199; DOI=10.1016/j.tice.2006.07.001;
Erman A., Veranic P., Psenicnik M., Jezernik K.;
"Superficial cell differentiation during embryonic and postnatal
development of mouse urothelium.";
Tissue Cell 38:293-301(2006).
[11]
FUNCTION, TISSUE SPECIFICITY, PHOSPHORYLATION, AND INDUCTION.
PubMed=17213200; DOI=10.1074/jbc.M604068200;
Wang L., Srinivasan S., Theiss A.L., Merlin D., Sitaraman S.V.;
"Interleukin-6 induces keratin expression in intestinal epithelial
cells: potential role of keratin-8 in interleukin-6-induced barrier
function alterations.";
J. Biol. Chem. 282:8219-8227(2007).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35 AND
SER-316, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-32; SER-35;
TYR-37; SER-43; SER-57; SER-137; SER-316; SER-384 AND SER-391, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, Liver, Lung, and Pancreas;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[14]
PHOSPHORYLATION AT SER-52 BY MAPKAPK2 AND MAPKAPK3.
PubMed=20724476; DOI=10.1074/jbc.M110.132357;
Menon M.B., Schwermann J., Singh A.K., Franz-Wachtel M., Pabst O.,
Seidler U., Omary M.B., Kotlyarov A., Gaestel M.;
"p38 MAP kinase and MAPKAP kinases MK2/3 cooperatively phosphorylate
epithelial keratins.";
J. Biol. Chem. 285:33242-33251(2010).
[15]
INTERACTION WITH EPPK1.
PubMed=25617501; DOI=10.1016/j.jhep.2015.01.007;
Szabo S., Woegenstein K.L., Oesterreicher C.H., Guldiken N., Chen Y.,
Doler C., Wiche G., Boor P., Haybaeck J., Strnad P., Fuchs P.;
"Epiplakin attenuates experimental mouse liver injury by chaperoning
keratin reorganization.";
J. Hepatol. 62:1357-1366(2015).
-!- FUNCTION: When phosphorylated, plays a role in filament
reorganization. Involved in the delivery of mutated CFTR to the
plasma membrane. Involved in the uptake of thrombin-antithrombin
complexes by hepatic cells (By similarity). Together with KRT8, is
involved in interleukin-6 (IL-6)-mediated barrier protection.
{ECO:0000250, ECO:0000269|PubMed:17213200}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
KRT18 associates with KRT8. Interacts with PNN, HCV core protein
and mutated CFTR. Interacts with YWHAE, YWHAH and YWHAZ only when
phosphorylated. Interacts with the thrombin-antithrombin complex.
Interacts with DNAJB6, TCHP and TRADD (By similarity). Interacts
with FAM83H (By similarity). Interacts with EPPK1
(PubMed:25617501). {ECO:0000250, ECO:0000250|UniProtKB:P05783,
ECO:0000269|PubMed:25617501}.
-!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250}. Nucleus,
nucleolus {ECO:0000250}. Cytoplasm {ECO:0000250}.
-!- TISSUE SPECIFICITY: Expressed in endoderm, intestinal epithelial
cells and in most extraembryonic tissues.
{ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:2416755,
ECO:0000269|PubMed:2454868, ECO:0000269|PubMed:7504637}.
-!- DEVELOPMENTAL STAGE: During embryogenesis, expressed in a complex
spatial and temporal pattern in various embryonic epithelia. In
7.5 and 13.5 day old embryo, expressed in most endodermal
epithelia, ectodermal and nascent mesodermal tissues. When the
neural plate forms, expression begins in the cells of skin
ectoderm, head process/notochord, periderm, whisker buds, choroid
plexus and the epithelia of auditory duct and inner ear. High
expression in the lining endodermal cells when the foregut and
hindgut invaginations form. Expression in all three layers of the
urothelium starts at day 15 in the embryo and is not visible after
day 18. By day 11 and 12, the entire embryonic palatal epithelium
shows expression as well as the nasal passages and the roof of the
mouth; which disappears progresively from day 13 to 15.
{ECO:0000269|PubMed:16973199, ECO:0000269|PubMed:7504637,
ECO:0000269|PubMed:7507912}.
-!- INDUCTION: By retinoic acid and IL-6.
{ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:2416755}.
-!- PTM: Phosphorylation increases by IL-6.
{ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:20724476}.
-!- PTM: Proteolytically cleaved by caspases during epithelial cell
apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-
6 or caspase-7. {ECO:0000269|PubMed:9298992}.
-!- PTM: O-GlcNAcylation increases solubility, and decreases stability
by inducing proteasomal degradation. {ECO:0000250}.
-!- MISCELLANEOUS: There are two types of cytoskeletal and
microfibrillar keratin: I (acidic; 40-55 kDa) and II (neutral to
basic; 56-70 kDa).
-!- SIMILARITY: Belongs to the intermediate filament family.
{ECO:0000305}.
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EMBL; M11686; AAA39390.1; -; mRNA.
EMBL; M36376; AAA39373.1; -; mRNA.
EMBL; M22832; AAA37552.1; -; Genomic_DNA.
EMBL; AK145413; BAE26424.1; -; mRNA.
EMBL; AK167072; BAE39232.1; -; mRNA.
EMBL; AK167265; BAE39378.1; -; mRNA.
EMBL; AK167432; BAE39519.1; -; mRNA.
EMBL; AK167469; BAE39553.1; -; mRNA.
EMBL; AK167676; BAE39725.1; -; mRNA.
EMBL; BC089022; AAH89022.1; -; mRNA.
EMBL; Y00217; CAA68365.1; -; Genomic_DNA.
CCDS; CCDS27869.1; -.
PIR; I59463; I59463.
RefSeq; NP_034794.2; NM_010664.2.
UniGene; Mm.22479; -.
ProteinModelPortal; P05784; -.
SMR; P05784; -.
BioGrid; 201023; 1.
IntAct; P05784; 5.
MINT; MINT-1866927; -.
STRING; 10090.ENSMUSP00000023803; -.
iPTMnet; P05784; -.
PhosphoSitePlus; P05784; -.
SWISS-2DPAGE; P05784; -.
EPD; P05784; -.
PaxDb; P05784; -.
PeptideAtlas; P05784; -.
PRIDE; P05784; -.
Ensembl; ENSMUST00000023803; ENSMUSP00000023803; ENSMUSG00000023043.
GeneID; 16668; -.
KEGG; mmu:16668; -.
UCSC; uc007xuj.2; mouse.
CTD; 3875; -.
MGI; MGI:96692; Krt18.
eggNOG; ENOG410IEYR; Eukaryota.
eggNOG; ENOG4111DJ8; LUCA.
GeneTree; ENSGT00760000119046; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; P05784; -.
KO; K07604; -.
OMA; RAKYEKM; -.
OrthoDB; EOG091G0A3U; -.
PhylomeDB; P05784; -.
TreeFam; TF332742; -.
Reactome; R-MMU-6805567; Keratinization.
Reactome; R-MMU-6809371; Formation of the cornified envelope.
ChiTaRS; Krt18; mouse.
PRO; PR:P05784; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000023043; -.
CleanEx; MM_KRT18; -.
Genevisible; P05784; MM.
GO; GO:0071944; C:cell periphery; IDA:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISO:MGI.
GO; GO:0034451; C:centriolar satellite; ISO:MGI.
GO; GO:0005737; C:cytoplasm; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005882; C:intermediate filament; IDA:MGI.
GO; GO:0045095; C:keratin filament; IDA:MGI.
GO; GO:0005815; C:microtubule organizing center; ISO:MGI.
GO; GO:0016363; C:nuclear matrix; IEA:UniProtKB-SubCell.
GO; GO:0005730; C:nucleolus; IEA:UniProtKB-SubCell.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; ISO:MGI.
GO; GO:0003723; F:RNA binding; ISO:MGI.
GO; GO:0097110; F:scaffold protein binding; ISO:MGI.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IMP:MGI.
GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; ISO:MGI.
GO; GO:0097284; P:hepatocyte apoptotic process; IMP:MGI.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; ISO:MGI.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IGI:MGI.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR027695; Keratin-18.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF225; PTHR23239:SF225; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm; Glycoprotein;
Intermediate filament; Isopeptide bond; Keratin; Methylation; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:P05783}.
CHAIN 2 423 Keratin, type I cytoskeletal 18.
/FTId=PRO_0000063667.
REGION 2 71 Head.
REGION 62 366 Necessary for interaction with PNN.
{ECO:0000250}.
REGION 69 121 Interaction with TRADD. {ECO:0000250}.
REGION 72 380 Rod.
REGION 72 107 Coil 1A.
REGION 108 125 Linker 1.
REGION 126 217 Coil 1B.
REGION 218 241 Linker 12.
REGION 236 384 Interaction with DNAJB6. {ECO:0000250}.
REGION 242 380 Coil 2.
REGION 381 423 Tail.
SITE 231 232 Cleavage; by caspase-3, caspase-6 or
caspase-7.
SITE 264 264 Stutter.
SITE 324 324 Stutter.
MOD_RES 2 2 N-acetylserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 7 7 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 11 11 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 19 19 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 31 31 Phosphoserine; alternate.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 32 32 Phosphoserine; alternate.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 37 37 Phosphotyrosine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 46 46 Omega-N-methylarginine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 50 50 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 52 52 Phosphoserine; by MAPKAPK2 and MAPKAPK3.
{ECO:0000269|PubMed:20724476}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 92 92 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 124 124 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 295 295 Phosphothreonine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 316 316 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 392 392 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 394 394 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 397 397 Phosphothreonine.
{ECO:0000250|UniProtKB:P05783}.
CARBOHYD 31 31 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 32 32 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CARBOHYD 50 50 O-linked (GlcNAc) serine; alternate.
{ECO:0000250}.
CROSSLNK 73 73 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05783}.
CROSSLNK 240 240 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05783}.
CROSSLNK 363 363 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05783}.
CROSSLNK 365 365 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05783}.
CONFLICT 134 134 F -> L (in Ref. 1; AAA39390 and 2;
AAA39373). {ECO:0000305}.
CONFLICT 214 214 V -> A (in Ref. 4; BAE26424/BAE39378).
{ECO:0000305}.
CONFLICT 244 244 D -> N (in Ref. 2; AAA39373).
{ECO:0000305}.
CONFLICT 253 253 A -> G (in Ref. 2; AAA39373).
{ECO:0000305}.
CONFLICT 300 300 E -> G (in Ref. 4; BAE39725).
{ECO:0000305}.
SEQUENCE 423 AA; 47538 MW; A67ACD6814A02118 CRC64;
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS
AGLAGMGGIQ TEKETMQDLN DRLASYLDKV KSLETENRRL ESKIREHLEK KGPQGVRDWG
HYFKIIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK
IMADIRAQYE ALAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLT ELRRTLQTLE
IDLDSMKNQN INLENSLGDV EARYKAQMEQ LNGVLLHLES ELAQTRAEGQ RQAQEYEALL
NIKVKLEAEI ATYRRLLEDG EDFSLNDALD SSNSMQTVQK TTTRKIVDGR VVSETNDTRV
LRH


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E2287m ELISA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
E2287m ELISA kit CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
E2287r ELISA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T
U2287r CLIA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T
U2287m CLIA kit CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
U2287m CLIA CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8 96T
U2287r CLIA kit CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8 96T
E2287m CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Mouse,Mus musculus,Type-II keratin Kb8
E2287r CK-8,Cytokeratin endo A,Cytokeratin-8,K8,Keratin, type II cytoskeletal 8,Keratin-8,Krt2-8,Krt8,Rat,Rattus norvegicus,Type-II keratin Kb8
E1427h ELISA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
E1427h ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
U1427h CLIA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,Homo sapiens,Human,K2e,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,KRT2,KRT2A,KRT2E,Type-II keratin Kb2 96T
E1427r ELISA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
E1427r ELISA kit CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
U1427r CLIA CK-2e,Cytokeratin-2e,Epithelial keratin-2e,K2e,Kb2,Keratin, type II cytoskeletal 2 epidermal,Keratin-2 epidermis,Keratin-2e,Krt2,Krt2a,Rat,Rattus norvegicus,Type-II keratin Kb2 96T
E2282h ELISA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
E2282h ELISA kit 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2282h CLIA 67 kDa cytokeratin,CK-1,Cytokeratin-1,Hair alpha protein,Homo sapiens,Human,K1,Keratin, type II cytoskeletal 1,Keratin-1,KRT1,KRTA,Type-II keratin Kb1 96T
U2288m CLIA 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T
U2288m CLIA kit 56 kDa cytokeratin,CK-10,Cytokeratin-10,K10,Keratin, type I cytoskeletal 10,Keratin, type I cytoskeletal 59 kDa,Keratin-10,Krt10,Krt1-10,Mouse,Mus musculus 96T


 

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