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Keratin, type I cytoskeletal 14 (Cytokeratin-14) (CK-14) (Keratin-14) (K14)

 K1C14_HUMAN             Reviewed;         472 AA.
P02533; Q14715; Q53XY3; Q9BUE3; Q9UBN2; Q9UBN3; Q9UCY4;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
05-MAY-2009, sequence version 4.
27-SEP-2017, entry version 196.
RecName: Full=Keratin, type I cytoskeletal 14;
AltName: Full=Cytokeratin-14;
Short=CK-14;
AltName: Full=Keratin-14;
Short=K14;
Name=KRT14;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6210150; DOI=10.1016/0092-8674(84)90456-2;
Marchuk D., McCrohon S., Fuchs E.;
"Remarkable conservation of structure among intermediate filament
genes.";
Cell 39:491-498(1984).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANT TYR-63.
PubMed=2580298; DOI=10.1073/pnas.82.6.1609;
Marchuk D., McCrohon S., Fuchs E.;
"Complete sequence of a gene encoding a human type I keratin:
sequences homologous to enhancer elements in the regulatory region of
the gene.";
Proc. Natl. Acad. Sci. U.S.A. 82:1609-1613(1985).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-63 AND
THR-94.
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 (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS TYR-63 AND
THR-94.
TISSUE=Brain, Pancreas, and Skin;
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 [MRNA] OF 64-472.
TISSUE=Epidermis;
PubMed=6186381; DOI=10.1016/0092-8674(82)90424-X;
Hanukoglu I., Fuchs E.;
"The cDNA sequence of a human epidermal keratin: divergence of
sequence but conservation of structure among intermediate filament
proteins.";
Cell 31:243-252(1982).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 117-132, AND VARIANT DM-EBS
ASP-129.
PubMed=8601736; DOI=10.1111/1523-1747.ep12342985;
Chan Y.-M., Cheng J., Gedde-Dahl T. Jr., Niemi K.M., Fuchs E.;
"Genetic analysis of a severe case of Dowling-Meara epidermolysis
bullosa simplex.";
J. Invest. Dermatol. 106:327-334(1996).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, AND VARIANTS DM-EBS
PHE-122; CYS-125 AND HIS-125.
PubMed=1717157; DOI=10.1016/0092-8674(91)90051-Y;
Coulombe P.A., Hutton M.E., Letai A., Hebert A., Paller A.S.,
Fuchs E.;
"Point mutations in human keratin 14 genes of epidermolysis bullosa
simplex patients: genetic and functional analyses.";
Cell 66:1301-1311(1991).
[9]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 118-126, AND VARIANT K-EBS
PHE-122.
PubMed=7526926; DOI=10.1093/hmg/3.7.1171;
Yamanishi K., Matsuki M., Konishi K., Yasuno H.;
"A novel mutation of Leu122 to Phe at a highly conserved hydrophobic
residue in the helix initiation motif of keratin 14 in epidermolysis
bullosa simplex.";
Hum. Mol. Genet. 3:1171-1172(1994).
[10]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 352-424, AND VARIANT K-EBS
THR-413.
Fujiwara H.;
"A novel mutation of cytokeratin 14 in a Japanese epidermolysis
bullosa simplex family.";
Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
[11]
TISSUE SPECIFICITY.
PubMed=9457912; DOI=10.1046/j.1523-1747.1998.00097.x;
Bowden P.E., Hainey S.D., Parker G., Jones D.O., Zimonjic D.,
Popescu N., Hodgins M.B.;
"Characterization and chromosomal localization of human hair-specific
keratin genes and comparative expression during the hair growth
cycle.";
J. Invest. Dermatol. 110:158-164(1998).
[12]
INTERACTION WITH TRADD.
PubMed=11684708; DOI=10.1083/jcb.200103078;
Inada H., Izawa I., Nishizawa M., Fujita E., Kiyono T., Takahashi T.,
Momoi T., Inagaki M.;
"Keratin attenuates tumor necrosis factor-induced cytotoxicity through
association with TRADD.";
J. Cell Biol. 155:415-426(2001).
[13]
FUNCTION, INTERACTION WITH KERATIN FILAMENTS, AND SUBCELLULAR
LOCATION.
PubMed=11724817; DOI=10.1083/jcb.200104063;
Bousquet O., Ma L., Yamada S., Gu C., Idei T., Takahashi K., Wirtz D.,
Coulombe P.A.;
"The nonhelical tail domain of keratin 14 promotes filament bundling
and enhances the mechanical properties of keratin intermediate
filaments in vitro.";
J. Cell Biol. 155:747-754(2001).
[14]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of
the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[15]
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).
[16]
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).
[17]
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).
[18]
UBIQUITINATION BY THE BCR(KLHL24) COMPLEX, AND INTERACTION WITH
KLHL24.
PubMed=27798626; DOI=10.1038/ng.3701;
Lin Z., Li S., Feng C., Yang S., Wang H., Ma D., Zhang J., Gou M.,
Bu D., Zhang T., Kong X., Wang X., Sarig O., Ren Y., Dai L., Liu H.,
Zhang J., Li F., Hu Y., Padalon-Brauch G., Vodo D., Zhou F., Chen T.,
Deng H., Sprecher E., Yang Y., Tan X.;
"Stabilizing mutations of KLHL24 ubiquitin ligase cause loss of
keratin 14 and human skin fragility.";
Nat. Genet. 48:1508-1516(2016).
[19]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 295-422 IN COMPLEX WITH KRT5,
DISULFIDE BOND, AND SUBCELLULAR LOCATION.
PubMed=22705788; DOI=10.1038/nsmb.2330;
Lee C.H., Kim M.S., Chung B.M., Leahy D.J., Coulombe P.A.;
"Structural basis for heteromeric assembly and perinuclear
organization of keratin filaments.";
Nat. Struct. Mol. Biol. 19:707-715(2012).
[20]
VARIANT K-EBS PRO-384.
PubMed=1720261; DOI=10.1126/science.1720261;
Bonifas J.M., Rothman A.L., Epstein E.H. Jr.;
"Epidermolysis bullosa simplex: evidence in two families for keratin
gene abnormalities.";
Science 254:1202-1205(1991).
[21]
VARIANT WC-EBS GLU-375 DEL.
PubMed=7506606; DOI=10.1093/hmg/2.11.1971;
Chen M.A., Bonifas J.M., Matsumura K., Blumenfeld A.,
Epstein E.H. Jr.;
"A novel three-nucleotide deletion in the helix 2B region of keratin
14 in epidermolysis bullosa simplex: delta E375.";
Hum. Mol. Genet. 2:1971-1972(1993).
[22]
VARIANT K-EBS ARG-272.
PubMed=7682883; DOI=10.1002/humu.1380020107;
Humphries M.M., Sheils D.M., Farrar G.J., Kumar-Singh R., Kenna P.F.,
Mansergh F.C., Jordan S.A., Young M.M., Humphries P.;
"A mutation (Met-->Arg) in the type I keratin (K14) gene responsible
for autosomal dominant epidermolysis bullosa simplex.";
Hum. Mutat. 2:37-42(1993).
[23]
VARIANT DM-EBS HIS-125.
PubMed=7688405; DOI=10.1111/1523-1747.ep12365079;
Stephens K., Sybert V.P., Wijsman E.M., Ehrlich P., Spencer A.;
"A keratin 14 mutational hot spot for epidermolysis bullosa simplex,
Dowling-Meara: implications for diagnosis.";
J. Invest. Dermatol. 101:240-243(1993).
[24]
VARIANT EBSB1 ALA-144.
PubMed=7526933; DOI=10.1038/ng0493-327;
Hovnanian A., Pollack E., Hilal L., Rochat A., Prost C., Barrandon Y.,
Goossens M.;
"A missense mutation in the rod domain of keratin 14 associated with
recessive epidermolysis bullosa simplex.";
Nat. Genet. 3:327-331(1993).
[25]
VARIANT WC-EBS MET-270.
PubMed=7506097; DOI=10.1038/ng1193-294;
Rugg E.L., Morley S.M., Smith F.J.D., Boxer M., Tidman M.J.,
Navsaria H.A., Leigh I.M., Lane E.B.;
"Missing links: Weber-Cockayne keratin mutations implicate the L12
linker domain in effective cytoskeleton function.";
Nat. Genet. 5:294-300(1993).
[26]
VARIANTS WC-EBS ILE-119; ASP-274; ASN-377 AND CYS-388, AND VARIANTS
DM-EBS ARG-120; CYS-125 AND SER-125.
PubMed=7561171; DOI=10.1111/1523-1747.ep12323846;
Chen H., Bonifas J.M., Matsumura K., Ikeda S., Leyden W.A.,
Epstein E.H. Jr.;
"Keratin 14 gene mutations in patients with epidermolysis bullosa
simplex.";
J. Invest. Dermatol. 105:629-632(1995).
[27]
VARIANT WC-EBS ILE-119.
PubMed=9284105; DOI=10.1111/1523-1747.ep12336051;
Hu Z.L., Smith L., Martins S., Bonifas J.M., Chen H.,
Epstein E.H. Jr.;
"Partial dominance of a keratin 14 mutation in epidermolysis bullosa
simplex: increased severity of disease in a homozygote.";
J. Invest. Dermatol. 109:360-364(1997).
[28]
VARIANT DM-EBS THR-119.
PubMed=9804355; DOI=10.1046/j.1523-1747.1998.00388.x;
Shemanko C.S., Mellerio J.E., Tidman M.J., Lane E.B., Eady R.A.J.;
"Severe palmo-plantar hyperkeratosis in Dowling-Meara epidermolysis
bullosa simplex caused by a mutation in the keratin 14 gene (KRT14).";
J. Invest. Dermatol. 111:893-895(1998).
[29]
VARIANT WC-EBS GLY-273.
PubMed=9804357; DOI=10.1046/j.1523-1747.1998.00374.x;
Mueller F.B., Kuester W., Bruckner-Tuderman L., Korge B.P.;
"Novel K5 and K14 mutations in German patients with the Weber-Cockayne
variant of epidermolysis bullosa simplex.";
J. Invest. Dermatol. 111:900-902(1998).
[30]
VARIANT DM-EBS CYS-125.
PubMed=10583131; DOI=10.1046/j.1365-2133.1999.03124.x;
Sasaki Y., Shimizu H., Akiyama M., Hiraoka Y., Takizawa Y., Yamada S.,
Morishima Y., Yamanishi K., Aiso S., Nishikawa T.;
"A recurrent keratin 14 mutation in Dowling-Meara epidermolysis
bullosa simplex.";
Br. J. Dermatol. 141:747-748(1999).
[31]
VARIANT K-EBS HIS-415, AND VARIANT DM-EBS GLN-419.
Hut P.H.L., van der Vlies P., Jonkman M.F., Shimizu H., Buys C.H.C.M.,
Scheffer H.;
"Genomic keratin 14 mutation detection in epidermolysis bullosa
simplex.";
Eur. J. Hum. Genet. Suppl. 7:121-121(1999).
[32]
VARIANT WC-EBS ASN-116, VARIANT DM-EBS SER-123, VARIANT K-EBS PRO-143,
VARIANT THR-94, AND SEQUENCE REVISION TO 25 AND 43.
PubMed=9989794; DOI=10.1046/j.1523-1747.1999.00495.x;
Soerensen C.B., Ladekjaer-Mikkelsen A.-S., Andresen B.S., Brandrup F.,
Veien N.K., Buus S.K., Anton-Lamprecht I., Kruse T.A., Jensen P.K.A.,
Eiberg H., Bolund L., Gregersen N.;
"Identification of novel and known mutations in the genes for keratin
5 and 14 in Danish patients with epidermolysis bullosa simplex:
correlation between genotype and phenotype.";
J. Invest. Dermatol. 112:184-190(1999).
[33]
VARIANT DM-EBS HIS-125.
PubMed=10730767; DOI=10.1046/j.1365-2133.2000.03304.x;
Shemanko C.S., Horn H.M., Keohane S.G., Hepburn N., Kerr A.I.G.,
Atherton D.J., Tidman M.J., Lane E.B.;
"Laryngeal involvement in the Dowling-Meara variant of epidermolysis
bullosa simplex with keratin mutations of severely disruptive
potential.";
Br. J. Dermatol. 142:315-320(2000).
[34]
VARIANTS DM-EBS CYS-125; HIS-125 AND GLN-419, VARIANTS K-EBS ASP-247
AND HIS-415, AND VARIANT WC-EBS LYS-422.
PubMed=10733662; DOI=10.1046/j.1523-1747.2000.00928.x;
Hut P.H.L., van der Vlies P., Jonkman M.F., Verlind E., Shimizu H.,
Buys C.H.C.M., Scheffer H.;
"Exempting homologous pseudogene sequences from polymerase chain
reaction amplification allows genomic keratin 14 hotspot analysis.";
J. Invest. Dermatol. 114:616-619(2000).
[35]
VARIANTS DM-EBS CYS-125 AND HIS-415, AND VARIANT K-EBS PRO-134.
PubMed=10820403;
DOI=10.1002/(SICI)1097-0223(200005)20:5<371::AID-PD818>3.0.CO;2-5;
Rugg E.L., Baty D., Shemanko C.S., Magee G., Polak S., Bergman R.,
Kadar T., Boxer M., Falik-Zaccai T., Borochowitz Z., Lane E.B.;
"DNA based prenatal testing for the skin blistering disorder
epidermolysis bullosa simplex.";
Prenat. Diagn. 20:371-377(2000).
[36]
VARIANT DM-EBS THR-119, AND VARIANT K-EBS VAL-119.
PubMed=11710919; DOI=10.1046/j.0022-202x.2001.01508.x;
Cummins R.E., Klingberg S., Wesley J., Rogers M., Zhao Y.,
Murrell D.F.;
"Keratin 14 point mutations at codon 119 of helix 1A resulting in
different epidermolysis bullosa simplex phenotypes.";
J. Invest. Dermatol. 117:1103-1107(2001).
[37]
VARIANTS WC-EBS HIS-388 AND CYS-415, AND VARIANT DM-EBS HIS-125.
PubMed=12707098; DOI=10.1001/archderm.139.4.498;
Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E.,
Petronius D., Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I.,
Uitto J., Sprecher E.;
"Epidermolysis bullosa simplex in Israel: clinical and genetic
features.";
Arch. Dermatol. 139:498-505(2003).
[38]
ERRATUM.
Ciubotaru D., Bergman R., Baty D., Indelman M., Pfendner E.,
Petronius D., Moualem H., Kanaan M., Ben Amitai D., McLean W.H.I.,
Uitto J., Sprecher E.;
Arch. Dermatol. 139:1084-1084(2003).
[39]
VARIANTS DM-EBS PRO-130 AND GLN-419, AND VARIANT WC-EBS MET-408.
PubMed=12655565; DOI=10.1002/humu.9124;
Schuilenga-Hut P.H.L., Vlies P., Jonkman M.F., Waanders E.,
Buys C.H.C.M., Scheffer H.;
"Mutation analysis of the entire keratin 5 and 14 genes in patients
with epidermolysis bullosa simplex and identification of novel
mutations.";
Hum. Mutat. 21:447-447(2003).
[40]
VARIANTS DM-EBS SER-128 DEL AND PRO-416, AND VARIANT WC-EBS CYS-148.
PubMed=12603865; DOI=10.1046/j.1523-1747.2003.12052.x;
Wood P., Baty D.U., Lane E.B., McLean W.H.I.;
"Long-range polymerase chain reaction for specific full-length
amplification of the human keratin 14 gene and novel keratin 14
mutations in epidermolysis bullosa simplex patients.";
J. Invest. Dermatol. 120:495-497(2003).
[41]
VARIANTS DM-EBS LYS-123 AND GLY-125, AND VARIANT WC-EBS LEU-133.
PubMed=14987259; DOI=10.1111/j.0906-6705.2004.0120.x;
Csikos M., Szalai Z., Becker K., Sebok B., Schneider I., Horvath A.,
Karpati S.;
"Novel keratin 14 gene mutations in patients from Hungary with
epidermolysis bullosa simplex.";
Exp. Dermatol. 13:185-191(2004).
[42]
INVOLVEMENT IN NFJS, AND INVOLVEMENT IN DPR.
PubMed=16960809; DOI=10.1086/507792;
Lugassy J., Itin P., Ishida-Yamamoto A., Holland K., Huson S.,
Geiger D., Hennies H.C., Indelman M., Bercovich D., Uitto J.,
Bergman R., McGrath J.A., Richard G., Sprecher E.;
"Naegeli-Franceschetti-Jadassohn syndrome and dermatopathia pigmentosa
reticularis: two allelic ectodermal dysplasias caused by dominant
mutations in KRT14.";
Am. J. Hum. Genet. 79:724-730(2006).
[43]
VARIANT WC-EBS VAL-119, AND VARIANTS DM-EBS HIS-125 AND CYS-125.
PubMed=16882168; DOI=10.1111/j.1365-2133.2006.07285.x;
Yasukawa K., Sawamura D., Goto M., Nakamura H., Jung S.-Y., Kim S.-C.,
Shimizu H.;
"Epidermolysis bullosa simplex in Japanese and Korean patients:
genetic studies in 19 cases.";
Br. J. Dermatol. 155:313-317(2006).
[44]
VARIANTS DM-EBS LYS-123; CYS-125; HIS-125 AND PRO-417, VARIANTS K-EBS
LEU-133; THR-272 AND PRO-384, AND VARIANTS WC-EBS PRO-211 AND GLU-411
DEL.
PubMed=16786515; DOI=10.1002/humu.9437;
Mueller F.B., Kuester W., Wodecki K., Almeida H. Jr.,
Bruckner-Tuderman L., Krieg T., Korge B.P., Arin M.J.;
"Novel and recurrent mutations in keratin KRT5 and KRT14 genes in
epidermolysis bullosa simplex: implications for disease phenotype and
keratin filament assembly.";
Hum. Mutat. 27:719-720(2006).
[45]
VARIANT GLN-418.
PubMed=24981776; DOI=10.1111/exd.12478;
Jankowski M., Wertheim-Tysarowska K., Jakubowski R., Sota J.,
Nowak W., Czajkowski R.;
"Novel KRT14 mutation causing epidermolysis bullosa simplex with
variable phenotype.";
Exp. Dermatol. 23:684-687(2014).
-!- FUNCTION: The nonhelical tail domain is involved in promoting
KRT5-KRT14 filaments to self-organize into large bundles and
enhances the mechanical properties involved in resilience of
keratin intermediate filaments in vitro.
{ECO:0000269|PubMed:11724817}.
-!- SUBUNIT: Heterotetramer of two type I and two type II keratins.
disulfide-linked keratin-14 associates with keratin-5. Interacts
with TRADD and with keratin filaments. Associates with other type
I keratins. Interacts with EPPK1 (By similarity). Interacts with
KLHL24 (PubMed:27798626). {ECO:0000250|UniProtKB:Q61781,
ECO:0000269|PubMed:11684708, ECO:0000269|PubMed:11724817,
ECO:0000269|PubMed:22705788, ECO:0000269|PubMed:27798626}.
-!- INTERACTION:
Q13835-2:PKP1; NbExp=2; IntAct=EBI-702178, EBI-9087684;
P41219:PRPH; NbExp=4; IntAct=EBI-702178, EBI-752074;
-!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Expressed in both
as a filamentous pattern.
-!- TISSUE SPECIFICITY: Detected in the basal layer, lowered within
the more apically located layers specifically in the stratum
spinosum, stratum granulosum but is not detected in stratum
corneum. Strongly expressed in the outer root sheath of anagen
follicles but not in the germinative matrix, inner root sheath or
hair. Found in keratinocytes surrounding the club hair during
telogen. {ECO:0000269|PubMed:9457912}.
-!- PTM: A disulfide bond is formed between rather than within
filaments and promotes the formation of a keratin filament cage
around the nucleus.
-!- PTM: Ubiquitinated by the BCR(KLHL24) E3 ubiquitin ligase complex.
{ECO:0000269|PubMed:27798626}.
-!- DISEASE: Epidermolysis bullosa simplex, Dowling-Meara type (DM-
EBS) [MIM:131760]: A severe form of intraepidermal epidermolysis
bullosa characterized by generalized herpetiform blistering, milia
formation, dystrophic nails, and mucous membrane involvement.
{ECO:0000269|PubMed:10583131, ECO:0000269|PubMed:10730767,
ECO:0000269|PubMed:10733662, ECO:0000269|PubMed:10820403,
ECO:0000269|PubMed:11710919, ECO:0000269|PubMed:12603865,
ECO:0000269|PubMed:12655565, ECO:0000269|PubMed:12707098,
ECO:0000269|PubMed:14987259, ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:16882168, ECO:0000269|PubMed:1717157,
ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:7688405,
ECO:0000269|PubMed:8601736, ECO:0000269|PubMed:9804355,
ECO:0000269|PubMed:9989794, ECO:0000269|Ref.31}. Note=The disease
is caused by mutations affecting the gene represented in this
entry.
-!- DISEASE: Epidermolysis bullosa simplex, Weber-Cockayne type (WC-
EBS) [MIM:131800]: A form of intraepidermal epidermolysis bullosa
characterized by blistering limited to palmar and plantar areas of
the skin. {ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:12603865, ECO:0000269|PubMed:12655565,
ECO:0000269|PubMed:12707098, ECO:0000269|PubMed:14987259,
ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:7506097, ECO:0000269|PubMed:7506606,
ECO:0000269|PubMed:7561171, ECO:0000269|PubMed:9284105,
ECO:0000269|PubMed:9804357, ECO:0000269|PubMed:9989794}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Epidermolysis bullosa simplex, Koebner type (K-EBS)
[MIM:131900]: A form of intraepidermal epidermolysis bullosa
characterized by generalized skin blistering. The phenotype is not
fundamentally distinct from the Dowling-Meara type, although it is
less severe. {ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:10820403, ECO:0000269|PubMed:11710919,
ECO:0000269|PubMed:16786515, ECO:0000269|PubMed:1720261,
ECO:0000269|PubMed:7526926, ECO:0000269|PubMed:7682883,
ECO:0000269|PubMed:9989794, ECO:0000269|Ref.10,
ECO:0000269|Ref.31}. Note=The disease is caused by mutations
affecting the gene represented in this entry.
-!- DISEASE: Epidermolysis bullosa simplex, autosomal recessive 1
(EBSB1) [MIM:601001]: An intraepidermal epidermolysis bullosa
characterized by localized blistering on the dorsal, lateral and
plantar surfaces of the feet. {ECO:0000269|PubMed:7526933}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Naegeli-Franceschetti-Jadassohn syndrome (NFJS)
[MIM:161000]: A rare autosomal dominant form of ectodermal
dysplasia. The cardinal features are absence of dermatoglyphics
(fingerprints), reticular cutaneous hyperpigmentation (starting at
about the age of 2 years without a preceding inflammatory stage),
palmoplantar keratoderma, hypohidrosis with diminished sweat gland
function and discomfort provoked by heat, nail dystrophy, and
tooth enamel defects. {ECO:0000269|PubMed:16960809}. Note=The
disease is caused by mutations affecting the gene represented in
this entry.
-!- DISEASE: Dermatopathia pigmentosa reticularis (DPR) [MIM:125595]:
A rare ectodermal dysplasia characterized by lifelong persistent
reticulate hyperpigmentation, non-cicatricial alopecia, and nail
dystrophy. Variable features include adermatoglyphia, hypohidrosis
or hyperhidrosis, and palmoplantar hyperkeratosis.
{ECO:0000269|PubMed:16960809}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- 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}.
-!- WEB RESOURCE: Name=Human Intermediate Filament Mutation Database;
URL="http://www.interfil.org";
-----------------------------------------------------------------------
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Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; J00124; AAB59562.1; -; Genomic_DNA.
EMBL; BT007186; AAP35850.1; -; mRNA.
EMBL; AC019349; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC002690; AAH02690.1; -; mRNA.
EMBL; BC019097; AAH19097.1; -; mRNA.
EMBL; BC042437; AAH42437.1; -; mRNA.
EMBL; BC094830; AAH94830.1; -; mRNA.
EMBL; D28807; BAA05967.1; -; Genomic_DNA.
EMBL; AF186085; AAF04034.1; -; Genomic_DNA.
EMBL; AF186086; AAF04035.1; -; Genomic_DNA.
EMBL; AF186087; AAF04036.1; -; Genomic_DNA.
EMBL; AF186088; AAF04037.1; -; Genomic_DNA.
EMBL; AF186089; AAF04038.1; -; Genomic_DNA.
EMBL; AF186090; AAF04039.1; -; Genomic_DNA.
CCDS; CCDS11400.1; -.
PIR; A26763; KRHUE.
RefSeq; NP_000517.2; NM_000526.4.
UniGene; Hs.654380; -.
PDB; 3TNU; X-ray; 3.00 A; A=295-422.
PDBsum; 3TNU; -.
ProteinModelPortal; P02533; -.
SMR; P02533; -.
BioGrid; 110059; 43.
DIP; DIP-33874N; -.
IntAct; P02533; 44.
STRING; 9606.ENSP00000167586; -.
iPTMnet; P02533; -.
PhosphoSitePlus; P02533; -.
SwissPalm; P02533; -.
BioMuta; KRT14; -.
DMDM; 229463044; -.
PaxDb; P02533; -.
PeptideAtlas; P02533; -.
PRIDE; P02533; -.
DNASU; 3861; -.
Ensembl; ENST00000167586; ENSP00000167586; ENSG00000186847.
GeneID; 3861; -.
KEGG; hsa:3861; -.
UCSC; uc002hxf.3; human.
CTD; 3861; -.
DisGeNET; 3861; -.
EuPathDB; HostDB:ENSG00000186847.5; -.
GeneCards; KRT14; -.
GeneReviews; KRT14; -.
HGNC; HGNC:6416; KRT14.
HPA; CAB000134; -.
HPA; HPA000452; -.
HPA; HPA000539; -.
HPA; HPA023040; -.
MalaCards; KRT14; -.
MIM; 125595; phenotype.
MIM; 131760; phenotype.
MIM; 131800; phenotype.
MIM; 131900; phenotype.
MIM; 148066; gene.
MIM; 161000; phenotype.
MIM; 601001; phenotype.
neXtProt; NX_P02533; -.
OpenTargets; ENSG00000186847; -.
Orphanet; 86920; Dermatopathia pigmentosa reticularis.
Orphanet; 79397; Epidermolysis bullosa simplex with mottled pigmentation.
Orphanet; 79396; Epidermolysis bullosa simplex, Dowling-Meara type.
Orphanet; 79399; Generalized epidermolysis bullosa simplex, non-Dowling-Meara type.
Orphanet; 89838; KRT14-related epidermolysis bullosa simplex.
Orphanet; 79400; Localized epidermolysis bullosa simplex.
Orphanet; 69087; Naegeli-Franceschetti-Jadassohn syndrome.
PharmGKB; PA30203; -.
eggNOG; ENOG410IFTF; Eukaryota.
eggNOG; ENOG410Y9IV; LUCA.
GeneTree; ENSGT00760000118808; -.
HOVERGEN; HBG013015; -.
InParanoid; P02533; -.
KO; K07604; -.
OMA; SYASNGL; -.
OrthoDB; EOG091G087I; -.
PhylomeDB; P02533; -.
TreeFam; TF332742; -.
Reactome; R-HSA-446107; Type I hemidesmosome assembly.
Reactome; R-HSA-6805567; Keratinization.
Reactome; R-HSA-6809371; Formation of the cornified envelope.
SIGNOR; P02533; -.
GeneWiki; Keratin_14; -.
GenomeRNAi; 3861; -.
PRO; PR:P02533; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000186847; -.
CleanEx; HS_KRT14; -.
Genevisible; P02533; HS.
GO; GO:0045178; C:basal part of cell; IEA:Ensembl.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005882; C:intermediate filament; IDA:BHF-UCL.
GO; GO:0045095; C:keratin filament; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990254; F:keratin filament binding; IPI:UniProtKB.
GO; GO:0005200; F:structural constituent of cytoskeleton; TAS:ProtInc.
GO; GO:0007568; P:aging; IDA:UniProtKB.
GO; GO:0070268; P:cornification; TAS:Reactome.
GO; GO:0008544; P:epidermis development; TAS:ProtInc.
GO; GO:0042633; P:hair cycle; IDA:UniProtKB.
GO; GO:0031581; P:hemidesmosome assembly; TAS:Reactome.
GO; GO:0045110; P:intermediate filament bundle assembly; IMP:UniProtKB.
GO; GO:0031424; P:keratinization; TAS:Reactome.
GO; GO:0010212; P:response to ionizing radiation; IEA:Ensembl.
GO; GO:0010043; P:response to zinc ion; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF; 1.
1: Evidence at protein level;
3D-structure; Coiled coil; Complete proteome; Cytoplasm;
Disease mutation; Disulfide bond; Ectodermal dysplasia;
Epidermolysis bullosa; Intermediate filament; Keratin; Nucleus;
Palmoplantar keratoderma; Phosphoprotein; Polymorphism;
Reference proteome; Ubl conjugation.
CHAIN 1 472 Keratin, type I cytoskeletal 14.
/FTId=PRO_0000063653.
REGION 1 114 Head.
REGION 115 422 Rod.
REGION 115 150 Coil 1A.
REGION 151 168 Linker 1.
REGION 169 260 Coil 1B.
REGION 261 283 Linker 12.
REGION 284 422 Coil 2.
REGION 423 472 Tail.
REGION 425 472 Interaction with Type I keratins and
keratin filaments.
SITE 364 364 Stutter.
MOD_RES 435 435 Phosphoserine.
{ECO:0000250|UniProtKB:Q61781}.
DISULFID 367 367 Interchain.
{ECO:0000269|PubMed:22705788}.
VARIANT 63 63 C -> Y (in dbSNP:rs6503640).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2580298,
ECO:0000269|Ref.3}.
/FTId=VAR_055347.
VARIANT 94 94 A -> T (in dbSNP:rs3826550).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:9989794,
ECO:0000269|Ref.3}.
/FTId=VAR_010437.
VARIANT 116 116 K -> N (in WC-EBS; dbSNP:rs59271739).
{ECO:0000269|PubMed:9989794}.
/FTId=VAR_010438.
VARIANT 119 119 M -> I (in WC-EBS at heterozygosity; more
severe phenotype is associated with
homozygosity; dbSNP:rs57358989).
{ECO:0000269|PubMed:7561171,
ECO:0000269|PubMed:9284105}.
/FTId=VAR_010439.
VARIANT 119 119 M -> T (in DM-EBS; dbSNP:rs28928893).
{ECO:0000269|PubMed:11710919,
ECO:0000269|PubMed:9804355}.
/FTId=VAR_010440.
VARIANT 119 119 M -> V (in K-EBS and WC-EBS;
dbSNP:rs61263401).
{ECO:0000269|PubMed:11710919,
ECO:0000269|PubMed:16882168}.
/FTId=VAR_023719.
VARIANT 120 120 Q -> R (in DM-EBS; dbSNP:rs60993843).
{ECO:0000269|PubMed:7561171}.
/FTId=VAR_010441.
VARIANT 122 122 L -> F (in DM-EBS and K-EBS;
dbSNP:rs59110575).
{ECO:0000269|PubMed:1717157,
ECO:0000269|PubMed:7526926}.
/FTId=VAR_010442.
VARIANT 123 123 N -> K (in DM-EBS; dbSNP:rs3826549).
{ECO:0000269|PubMed:14987259,
ECO:0000269|PubMed:16786515}.
/FTId=VAR_023720.
VARIANT 123 123 N -> S (in DM-EBS; dbSNP:rs60171927).
{ECO:0000269|PubMed:9989794}.
/FTId=VAR_010443.
VARIANT 125 125 R -> C (in DM-EBS; dbSNP:rs60399023).
{ECO:0000269|PubMed:10583131,
ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:10820403,
ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:1717157,
ECO:0000269|PubMed:7561171}.
/FTId=VAR_003837.
VARIANT 125 125 R -> G (in DM-EBS; dbSNP:rs60399023).
{ECO:0000269|PubMed:14987259}.
/FTId=VAR_023721.
VARIANT 125 125 R -> H (in DM-EBS; dbSNP:rs58330629).
{ECO:0000269|PubMed:10730767,
ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:12707098,
ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:16882168,
ECO:0000269|PubMed:1717157,
ECO:0000269|PubMed:7688405}.
/FTId=VAR_003838.
VARIANT 125 125 R -> S (in DM-EBS).
{ECO:0000269|PubMed:7561171}.
/FTId=VAR_010444.
VARIANT 128 128 Missing (in DM-EBS).
{ECO:0000269|PubMed:12603865}.
/FTId=VAR_031634.
VARIANT 129 129 Y -> D (in DM-EBS; dbSNP:rs60470268).
{ECO:0000269|PubMed:8601736}.
/FTId=VAR_010445.
VARIANT 130 130 L -> P (in DM-EBS; dbSNP:rs57522245).
{ECO:0000269|PubMed:12655565}.
/FTId=VAR_023722.
VARIANT 133 133 V -> A (in dbSNP:rs56798071).
/FTId=VAR_033496.
VARIANT 133 133 V -> L (in WC-EBS and K-EBS;
dbSNP:rs61027685).
{ECO:0000269|PubMed:14987259,
ECO:0000269|PubMed:16786515}.
/FTId=VAR_023723.
VARIANT 134 134 R -> P (in K-EBS; dbSNP:rs61540016).
{ECO:0000269|PubMed:10820403}.
/FTId=VAR_031635.
VARIANT 143 143 L -> P (in K-EBS; dbSNP:rs61326242).
{ECO:0000269|PubMed:9989794}.
/FTId=VAR_010446.
VARIANT 144 144 E -> A (in EBSB1; dbSNP:rs57121345).
{ECO:0000269|PubMed:7526933}.
/FTId=VAR_003839.
VARIANT 148 148 R -> C (in WC-EBS; dbSNP:rs58378809).
{ECO:0000269|PubMed:12603865}.
/FTId=VAR_031636.
VARIANT 211 211 R -> P (in WC-EBS; dbSNP:rs60589227).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027718.
VARIANT 215 215 E -> K (in dbSNP:rs11551755).
/FTId=VAR_049784.
VARIANT 247 247 A -> D (in K-EBS; dbSNP:rs147611635).
{ECO:0000269|PubMed:10733662}.
/FTId=VAR_010447.
VARIANT 270 270 V -> M (in WC-EBS; dbSNP:rs58560979).
{ECO:0000269|PubMed:7506097}.
/FTId=VAR_003840.
VARIANT 272 272 M -> R (in K-EBS; dbSNP:rs61371557).
{ECO:0000269|PubMed:7682883}.
/FTId=VAR_003841.
VARIANT 272 272 M -> T (in K-EBS; dbSNP:rs61371557).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027719.
VARIANT 273 273 D -> G (in WC-EBS; dbSNP:rs59375065).
{ECO:0000269|PubMed:9804357}.
/FTId=VAR_010448.
VARIANT 274 274 A -> D (in WC-EBS; dbSNP:rs58785777).
{ECO:0000269|PubMed:7561171}.
/FTId=VAR_010449.
VARIANT 375 375 Missing (in WC-EBS).
{ECO:0000269|PubMed:7506606}.
/FTId=VAR_003842.
VARIANT 377 377 I -> N (in WC-EBS; dbSNP:rs61536893).
{ECO:0000269|PubMed:7561171}.
/FTId=VAR_010450.
VARIANT 384 384 L -> P (in K-EBS; dbSNP:rs59629244).
{ECO:0000269|PubMed:16786515,
ECO:0000269|PubMed:1720261}.
/FTId=VAR_003843.
VARIANT 388 388 R -> C (in WC-EBS; dbSNP:rs59966597).
{ECO:0000269|PubMed:7561171}.
/FTId=VAR_010451.
VARIANT 388 388 R -> H (in WC-EBS; dbSNP:rs58645163).
{ECO:0000269|PubMed:12707098}.
/FTId=VAR_031637.
VARIANT 408 408 L -> M (in WC-EBS; dbSNP:rs57200223).
{ECO:0000269|PubMed:12655565}.
/FTId=VAR_023724.
VARIANT 411 411 Missing (in WC-EBS).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027720.
VARIANT 413 413 A -> T (in K-EBS; dbSNP:rs59780231).
{ECO:0000269|Ref.10}.
/FTId=VAR_023725.
VARIANT 415 415 Y -> C (in WC-EBS; dbSNP:rs59442925).
{ECO:0000269|PubMed:12707098}.
/FTId=VAR_031638.
VARIANT 415 415 Y -> H (in K-EBS; dbSNP:rs58380626).
{ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:10820403,
ECO:0000269|Ref.31}.
/FTId=VAR_003844.
VARIANT 416 416 R -> P (in DM-EBS; dbSNP:rs60622724).
{ECO:0000269|PubMed:12603865}.
/FTId=VAR_031639.
VARIANT 417 417 R -> P (in DM-EBS; dbSNP:rs61085704).
{ECO:0000269|PubMed:16786515}.
/FTId=VAR_027721.
VARIANT 418 418 L -> Q (probable disease-associated
mutation found in epidermolysis bullosa
simplex with variable phenotype).
{ECO:0000269|PubMed:24981776}.
/FTId=VAR_071705.
VARIANT 419 419 L -> Q (in DM-EBS; dbSNP:rs57364972).
{ECO:0000269|PubMed:10733662,
ECO:0000269|PubMed:12655565,
ECO:0000269|Ref.31}.
/FTId=VAR_003845.
VARIANT 422 422 E -> K (in WC-EBS; dbSNP:rs58762773).
{ECO:0000269|PubMed:10733662}.
/FTId=VAR_010452.
CONFLICT 26 26 G -> A (in Ref. 1 and 2; AAB59562).
{ECO:0000305}.
CONFLICT 44 44 S -> N (in Ref. 1 and 2; AAB59562).
{ECO:0000305}.
HELIX 333 418 {ECO:0000244|PDB:3TNU}.
SEQUENCE 472 AA; 51561 MW; 120BA30BA2F8E397 CRC64;
MTTCSRQFTS SSSMKGSCGI GGGIGGGSSR ISSVLAGGSC RAPSTYGGGL SVSSSRFSSG
GACGLGGGYG GGFSSSSSSF GSGFGGGYGG GLGAGLGGGF GGGFAGGDGL LVGSEKVTMQ
NLNDRLASYL DKVRALEEAN ADLEVKIRDW YQRQRPAEIK DYSPYFKTIE DLRNKILTAT
VDNANVLLQI DNARLAADDF RTKYETELNL RMSVEADING LRRVLDELTL ARADLEMQIE
SLKEELAYLK KNHEEEMNAL RGQVGGDVNV EMDAAPGVDL SRILNEMRDQ YEKMAEKNRK
DAEEWFFTKT EELNREVATN SELVQSGKSE ISELRRTMQN LEIELQSQLS MKASLENSLE
ETKGRYCMQL AQIQEMIGSV EEQLAQLRCE MEQQNQEYKI LLDVKTRLEQ EIATYRRLLE
GEDAHLSSSQ FSSGSQSSRD VTSSSRQIRT KVMDVHDGKV VSTHEQVLRT KN


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E2282h 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
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
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
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


 

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