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

 K1C18_RAT               Reviewed;         423 AA.
Q5BJY9; Q63278;
16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 109.
RecName: Full=Keratin, type I cytoskeletal 18;
AltName: Full=Cytokeratin-18;
Short=CK-18;
AltName: Full=Keratin-18;
Short=K18;
Name=Krt18 {ECO:0000250|UniProtKB:P05783};
Synonyms=Krt1-18 {ECO:0000312|RGD:619935};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1] {ECO:0000305, ECO:0000312|EMBL:AAH91275.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus {ECO:0000312|EMBL:AAH91275.1};
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).
[2] {ECO:0000305, ECO:0000312|EMBL:CAA57204.1}
NUCLEOTIDE SEQUENCE [MRNA] OF 124-270, AND DEVELOPMENTAL STAGE.
STRAIN=Wistar {ECO:0000312|EMBL:CAA57204.1};
TISSUE=Fetal gonad {ECO:0000269|PubMed:8541209};
PubMed=8541209; DOI=10.1016/0925-4773(95)00401-L;
Fridmacher V., le Bert M., Guillou F., Magre S.;
"Switch in the expression of the K19/K18 keratin genes as a very early
evidence of testicular differentiation in the rat.";
Mech. Dev. 52:199-207(1995).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 131-140, AND SUBCELLULAR LOCATION.
TISSUE=Liver {ECO:0000269|PubMed:16128803};
PubMed=16128803; DOI=10.1111/j.1742-4658.2005.04847.x;
Segawa M., Niino K., Mineki R., Kaga N., Murayama K., Sugimoto K.,
Watanabe Y., Furukawa K., Horigome T.;
"Proteome analysis of a rat liver nuclear insoluble protein fraction
and localization of a novel protein, ISP36, to compartments in the
interchromatin space.";
FEBS J. 272:4327-4338(2005).
[4] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=7507868; DOI=10.1111/j.1432-0436.1993.tb00032.x;
Frojdman K., Paranko J., Virtanen I., Pelliniemi L.J.;
"Intermediate filament proteins and epithelial differentiation in the
embryonic ovary of the rat.";
Differentiation 55:47-55(1993).
[5] {ECO:0000305}
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=7514933;
Flint N., Pemberton P.W., Lobley R.W., Evans G.S.;
"Cytokeratin expression in epithelial cells isolated from the crypt
and villus regions of the rodent small intestine.";
Epithelial Cell Biol. 3:16-23(1994).
[6] {ECO:0000305}
TISSUE SPECIFICITY.
PubMed=7517927; DOI=10.1007/BF00315832;
Kasper M., Hofer D., Woodcock-Mitchell J., Migheli A., Attanasio A.,
Rudolf T., Muller M., Drenckhahn D.;
"Colocalization of cytokeratin 18 and villin in type III alveolar
cells (brush cells) of the rat lung.";
Histochemistry 101:57-62(1994).
[7] {ECO:0000305}
DEVELOPMENTAL STAGE.
PubMed=7589899; DOI=10.1046/j.1432-0436.1995.5930155.x;
Zhang C., Cotter M., Lawton A., Oakley B., Wong L., Zeng Q.;
"Keratin 18 is associated with a subset of older taste cells in the
rat.";
Differentiation 59:155-162(1995).
[8] {ECO:0000305}
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=8789401; DOI=10.1007/BF02389690;
Zeng Q., Lawton A., Oakley B.;
"Glycoconjugates and keratin 18 define subsets of taste cells.";
Histochem. J. 27:997-1006(1995).
[9] {ECO:0000305}
DEPHOSPHORYLATION BY ETHANOL.
PubMed=8824732;
DOI=10.1002/(SICI)1097-0169(1996)33:1<30::AID-CM4>3.0.CO;2-M;
Eckert B.S., Yeagle P.L.;
"Site-specificity of ethanol-induced dephosphorylation of rat
hepatocyte keratins 8 and 18: a 31P NMR study.";
Cell Motil. Cytoskeleton 33:30-37(1996).
[10] {ECO:0000305}
FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH
THROMBIN-ANTITHROMBIN COMPLEX.
PubMed=9353322; DOI=10.1074/jbc.272.45.28574;
Wells M.J., Hatton M.W., Hewlett B., Podor T.J., Sheffield W.P.,
Blajchman M.A.;
"Cytokeratin 18 is expressed on the hepatocyte plasma membrane surface
and interacts with thrombin-antithrombin complexes.";
J. Biol. Chem. 272:28574-28581(1997).
[11] {ECO:0000305}
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=10707864; DOI=10.1016/S0168-8278(00)80069-0;
Sanchez A., Alvarez A.M., Pagan R., Roncero C., Vilaro S., Benito M.,
Fabregat I.;
"Fibronectin regulates morphology, cell organization and gene
expression of rat fetal hepatocytes in primary culture.";
J. Hepatol. 32:242-250(2000).
[12] {ECO:0000305}
SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=11428046; DOI=10.1023/A:1026548020851;
Hofer D., Shin D.W., Drenckhahn D.;
"Identification of cytoskeletal markers for the different microvilli
and cell types of the rat vomeronasal sensory epithelium.";
J. Neurocytol. 29:147-156(2000).
[13] {ECO:0000305}
TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
PubMed=14630065; DOI=10.1016/S0887-2333(03)00132-2;
Ridd K., Alexander D.J., Reed C.J.;
"Foetal rat lung epithelial (FRLE) cells: partial characterisation and
response to pneumotoxins.";
Toxicol. in Vitro 18:79-88(2004).
[14] {ECO:0000305}
SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
PubMed=16998620; DOI=10.1007/s10266-005-0059-4;
Iwasaki S., Aoyagi H., Asami T.;
"Expression of keratin 18 in the periderm cells of the lingual
epithelium of fetal rats: visualization by fluorescence
immunohistochemistry and differential interference contrast
microscopy.";
Odontology 94:64-68(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-19 AND SER-35, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=16641100; DOI=10.1073/pnas.0600895103;
Hoffert J.D., Pisitkun T., Wang G., Shen R.-F., Knepper M.A.;
"Quantitative phosphoproteomics of vasopressin-sensitive renal cells:
regulation of aquaporin-2 phosphorylation at two sites.";
Proc. Natl. Acad. Sci. U.S.A. 103:7159-7164(2006).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31; SER-35 AND SER-57,
AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22673903; DOI=10.1038/ncomms1871;
Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A.,
Lundby C., Olsen J.V.;
"Quantitative maps of protein phosphorylation sites across 14
different rat organs and tissues.";
Nat. Commun. 3:876-876(2012).
-!- FUNCTION: When phosphorylated, plays a role in filament
reorganization. Involved in the delivery of mutated CFTR to the
plasma membrane. Together with KRT8, is involved in interleukin-6
(IL-6)-mediated barrier protection (By similarity). Involved in
the uptake of thrombin-antithrombin complexes by hepatic cells.
{ECO:0000250|UniProtKB:P05783, ECO:0000269|PubMed:9353322}.
-!- 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 DNAJB6, TCHP and TRADD (By
similarity). Interacts with the thrombin-antithrombin complex.
Interacts with FAM83H (By similarity). Interacts with EPPK1 (By
similarity). {ECO:0000250, ECO:0000250|UniProtKB:P05783,
ECO:0000250|UniProtKB:P05784, ECO:0000269|PubMed:9353322}.
-!- SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000269|PubMed:16128803,
ECO:0000269|PubMed:16998620}. Nucleus, nucleolus {ECO:0000250}.
Cytoplasm {ECO:0000269|PubMed:16128803,
ECO:0000269|PubMed:16998620}.
-!- TISSUE SPECIFICITY: Expressed on the plasma membrane of
hepatocytes and in the narrow apical portions of supporting cells
in the vomeronasal sensory epithelium. Detected in the type III
alveolar cells of the lung, in the proliferative crypt epithelium
of the small intestine and in the older intragemmal cells of the
tongue. {ECO:0000269|PubMed:10707864, ECO:0000269|PubMed:11428046,
ECO:0000269|PubMed:14630065, ECO:0000269|PubMed:7514933,
ECO:0000269|PubMed:7517927, ECO:0000269|PubMed:8789401,
ECO:0000269|PubMed:9353322}.
-!- DEVELOPMENTAL STAGE: Expression first detected in the male gonad
at 13.5 dpc, at the onset of testicular differentiation, and at 17
dpc in cell aggregates of the early ovary; then only in some cord
cells of the older ovary. Expressed in fetal lung epithelium at 20
dpc. Detected at 13 dpc, sparsely distributed throughout the
cytoplasm in the single layer of periderm cells covering the
dorsal epithelium of the fetal tongue. Expression increases in the
lingual periderm cells at 17 dpc and then disappears at 19 dpc
coinciding with the disappearance of the periderm cells at the
onset of squamous stratification of the lingual epithelium.
Expressed at day 2-3 postnatally in older, elongated taste bud
cells and at day 5, uniformly distributed throughout the
epithelium of villi, intervillus epithelium and developing crypt
buds of the small intestine. {ECO:0000269|PubMed:14630065,
ECO:0000269|PubMed:16998620, ECO:0000269|PubMed:7507868,
ECO:0000269|PubMed:7514933, ECO:0000269|PubMed:7589899,
ECO:0000269|PubMed:8541209, ECO:0000269|PubMed:8789401}.
-!- INDUCTION: By IL-6 (By similarity). By fibronectin.
{ECO:0000250|UniProtKB:P05783, ECO:0000269|PubMed:10707864}.
-!- PTM: Phosphorylation increases by IL-6.
{ECO:0000250|UniProtKB:P05783}.
-!- PTM: Proteolytically cleaved by caspases during epithelial cell
apoptosis. Cleavage occurs at Asp-231 by either caspase-3,
caspase-6 or caspase-7 (By similarity). {ECO:0000250}.
-!- PTM: Dephosphorylated by ethanol. {ECO:0000269|PubMed:8824732}.
-!- 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:0000255|PROSITE-ProRule:PRU01188}.
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EMBL; BC091275; AAH91275.1; -; mRNA.
EMBL; X81448; CAA57204.1; -; mRNA.
RefSeq; NP_446428.1; NM_053976.1.
UniGene; Rn.103924; -.
ProteinModelPortal; Q5BJY9; -.
SMR; Q5BJY9; -.
IntAct; Q5BJY9; 2.
STRING; 10116.ENSRNOP00000067234; -.
iPTMnet; Q5BJY9; -.
PhosphoSitePlus; Q5BJY9; -.
PaxDb; Q5BJY9; -.
PRIDE; Q5BJY9; -.
Ensembl; ENSRNOT00000073951; ENSRNOP00000067234; ENSRNOG00000047393.
GeneID; 294853; -.
KEGG; rno:294853; -.
CTD; 3875; -.
RGD; 619935; Krt18.
eggNOG; ENOG410IEYR; Eukaryota.
eggNOG; ENOG4111DJ8; LUCA.
GeneTree; ENSGT00900000140814; -.
HOGENOM; HOG000230975; -.
HOVERGEN; HBG013015; -.
InParanoid; Q5BJY9; -.
KO; K07604; -.
OMA; RAKYEKM; -.
OrthoDB; EOG091G0A3U; -.
PhylomeDB; Q5BJY9; -.
Reactome; R-RNO-6805567; Keratinization.
Reactome; R-RNO-6809371; Formation of the cornified envelope.
PRO; PR:Q5BJY9; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000047393; -.
Genevisible; Q5BJY9; RN.
GO; GO:0071944; C:cell periphery; IEA:Ensembl.
GO; GO:0005913; C:cell-cell adherens junction; IEA:Ensembl.
GO; GO:0034451; C:centriolar satellite; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
GO; GO:0045095; C:keratin filament; IDA:RGD.
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; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0097110; F:scaffold protein binding; IEA:Ensembl.
GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
GO; GO:0043000; P:Golgi to plasma membrane CFTR protein transport; IEA:Ensembl.
GO; GO:0097284; P:hepatocyte apoptotic process; IEA:Ensembl.
GO; GO:0045104; P:intermediate filament cytoskeleton organization; IEA:Ensembl.
GO; GO:0043066; P:negative regulation of apoptotic process; IEA:Ensembl.
GO; GO:0033209; P:tumor necrosis factor-mediated signaling pathway; IEA:Ensembl.
InterPro; IPR001664; IF.
InterPro; IPR018039; Intermediate_filament_CS.
InterPro; IPR027695; Keratin-18.
InterPro; IPR002957; Keratin_I.
PANTHER; PTHR23239; PTHR23239; 1.
PANTHER; PTHR23239:SF35; PTHR23239:SF35; 1.
Pfam; PF00038; Filament; 1.
PRINTS; PR01248; TYPE1KERATIN.
SMART; SM01391; Filament; 1.
PROSITE; PS00226; IF_ROD_1; 1.
PROSITE; PS51842; IF_ROD_2; 1.
1: Evidence at protein level;
Acetylation; Coiled coil; Complete proteome; Cytoplasm;
Direct protein sequencing; 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_0000063668.
DOMAIN 72 384 IF rod. {ECO:0000255|PROSITE-
ProRule:PRU01188}.
REGION 2 71 Head. {ECO:0000255}.
REGION 62 366 Necessary for interaction with PNN.
{ECO:0000250|UniProtKB:P05783}.
REGION 69 121 Interaction with TRADD.
{ECO:0000250|UniProtKB:P05783}.
REGION 72 107 Coil 1A. {ECO:0000255}.
REGION 108 125 Linker 1. {ECO:0000255}.
REGION 126 217 Coil 1B. {ECO:0000255}.
REGION 218 241 Linker 12. {ECO:0000255}.
REGION 236 384 Interaction with DNAJB6.
{ECO:0000250|UniProtKB:P05783}.
REGION 242 380 Coil 2. {ECO:0000255}.
REGION 381 423 Tail. {ECO:0000255}.
SITE 231 232 Cleavage; by caspase-3, caspase-6 or
caspase-7. {ECO:0000250}.
SITE 264 264 Stutter. {ECO:0000255}.
SITE 324 324 Stutter. {ECO:0000255}.
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:0000244|PubMed:16641100}.
MOD_RES 31 31 Phosphoserine; alternate.
{ECO:0000244|PubMed:22673903}.
MOD_RES 32 32 Phosphoserine; alternate.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 35 35 Phosphoserine.
{ECO:0000244|PubMed:16641100,
ECO:0000244|PubMed:22673903}.
MOD_RES 37 37 Phosphotyrosine.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 43 43 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
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:0000250|UniProtKB:P05784}.
MOD_RES 57 57 Phosphoserine.
{ECO:0000244|PubMed:22673903}.
MOD_RES 60 60 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 85 85 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 124 124 N6-acetyllysine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 137 137 Phosphoserine.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 170 170 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 295 295 Phosphothreonine.
{ECO:0000250|UniProtKB:P05783}.
MOD_RES 384 384 Phosphoserine.
{ECO:0000250|UniProtKB:P05784}.
MOD_RES 391 391 Phosphoserine.
{ECO:0000250|UniProtKB:P05783}.
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|UniProtKB:P05783}.
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}.
CROSSLNK 410 410 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P05783}.
CONFLICT 125 125 T -> I (in Ref. 2; CAA57204).
{ECO:0000305}.
SEQUENCE 423 AA; 47761 MW; 793F0BAA275CCA4E CRC64;
MSFTTRSTTF STNYRSLGSV RTPSQRVRPA SSAASVYAGA GGSGSRISVS RSVWGGSVGS
AGLAGMGGVQ TEKETMQDLN DRLASYLDKV KNLETENRRL ESKIREYLEK RGPQGVRDWG
HYFKTIEDLR AQIFANSVDN ARIVLQIDNA RLAADDFRVK YETELAMRQS VESDIHGLRK
VVDDTNITRL QLETEIEALK EELLFMKKNH EEEVQGLEAQ IASSGLTVEV DAPKSQDLSK
IMADIRAQYE QLAQKNREEL DKYWSQQIEE STTVVTTKSA EIRDAETTLL ELRRTLQTLE
IDLDSMKNQN INLENNLGEV EARYRVQMEQ LNGVLLHLES ELAQTRAEGQ RQTQEYEALL
NIKVKLEAEI ATYRRLLEDG DDFSLNDALD SSNSMQTVQR TTTRKVVDGK VVSETNDTRV
LRH


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E1231m ELISA kit CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 96T
E1231m ELISA CK-18,Cytokeratin endo B,Cytokeratin-18,K18,Keratin D,Keratin, type I cytoskeletal 18,Keratin-18,Kerd,Krt1-18,Krt18,Mouse,Mus musculus 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
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
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
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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