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Interferon-induced transmembrane protein 1 (Dispanin subfamily A member 2a) (DSPA2a) (Interferon-induced protein 17) (Interferon-inducible protein 9-27) (Leu-13 antigen) (CD antigen CD225)

 IFM1_HUMAN              Reviewed;         125 AA.
P13164; Q15322; Q53XZ0;
01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
25-NOV-2008, sequence version 3.
12-SEP-2018, entry version 157.
RecName: Full=Interferon-induced transmembrane protein 1;
AltName: Full=Dispanin subfamily A member 2a;
Short=DSPA2a;
AltName: Full=Interferon-induced protein 17;
AltName: Full=Interferon-inducible protein 9-27;
AltName: Full=Leu-13 antigen;
AltName: CD_antigen=CD225;
Name=IFITM1; Synonyms=CD225, IFI17;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-13.
PubMed=2492664; DOI=10.1073/pnas.86.3.840;
Reid L.E., Brasnett A.H., Gilbert C.S., Porter A.C.G., Gewert D.R.,
Stark G.R., Kerr I.M.;
"A single DNA response element can confer inducibility by both
alpha- and gamma-interferons.";
Proc. Natl. Acad. Sci. U.S.A. 86:840-844(1989).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ALA-13.
PubMed=7559564; DOI=10.1074/jbc.270.40.23860;
Deblandre G.A., Marinx O.P., Evans S.S., Majjaj S., Leo O., Caput D.,
Huez G.A., Wathelet M.G.;
"Expression cloning of an interferon-inducible 17-kDa membrane protein
implicated in the control of cell growth.";
J. Biol. Chem. 270:23860-23866(1995).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13.
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 MRNA], AND VARIANT ALA-13.
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16554811; DOI=10.1038/nature04632;
Taylor T.D., Noguchi H., Totoki Y., Toyoda A., Kuroki Y., Dewar K.,
Lloyd C., Itoh T., Takeda T., Kim D.-W., She X., Barlow K.F.,
Bloom T., Bruford E., Chang J.L., Cuomo C.A., Eichler E.,
FitzGerald M.G., Jaffe D.B., LaButti K., Nicol R., Park H.-S.,
Seaman C., Sougnez C., Yang X., Zimmer A.R., Zody M.C., Birren B.W.,
Nusbaum C., Fujiyama A., Hattori M., Rogers J., Lander E.S.,
Sakaki Y.;
"Human chromosome 11 DNA sequence and analysis including novel gene
identification.";
Nature 440:497-500(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ALA-13.
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ALA-13.
TISSUE=Cervix;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
INTERACTION WITH CD81.
PubMed=2398277;
Takahashi S., Doss C., Levy S., Levy R.;
"TAPA-1, the target of an antiproliferative antibody, is associated on
the cell surface with the Leu-13 antigen.";
J. Immunol. 145:2207-2213(1990).
[9]
FUNCTION.
PubMed=16847454; DOI=10.1038/sj.onc.1209807;
Yang G., Xu Y., Chen X., Hu G.;
"IFITM1 plays an essential role in the antiproliferative action of
interferon-gamma.";
Oncogene 26:594-603(2007).
[10]
SUBCELLULAR LOCATION, AND INTERACTION WITH CAV1.
PubMed=19499152; DOI=10.1093/abbs/gmp034;
Xu Y., Yang G., Hu G.;
"Binding of IFITM1 enhances the inhibiting effect of caveolin-1 on ERK
activation.";
Acta Biochim. Biophys. Sin. 41:488-494(2009).
[11]
FUNCTION IN VIRAL RESISTANCE.
PubMed=20064371; DOI=10.1016/j.cell.2009.12.017;
Brass A.L., Huang I.C., Benita Y., John S.P., Krishnan M.N.,
Feeley E.M., Ryan B.J., Weyer J.L., van der Weyden L., Fikrig E.,
Adams D.J., Xavier R.J., Farzan M., Elledge S.J.;
"The IFITM proteins mediate cellular resistance to influenza A H1N1
virus, West Nile virus, and dengue virus.";
Cell 139:1243-1254(2009).
[12]
REVIEW.
PubMed=21166591; DOI=10.1089/jir.2010.0112;
Siegrist F., Ebeling M., Certa U.;
"The small interferon-induced transmembrane genes and proteins.";
J. Interferon Cytokine Res. 31:183-197(2011).
[13]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=20838853; DOI=10.1007/s11060-010-0377-4;
Yu F., Ng S.S., Chow B.K., Sze J., Lu G., Poon W.S., Kung H.F.,
Lin M.C.;
"Knockdown of interferon-induced transmembrane protein 1 (IFITM1)
inhibits proliferation, migration, and invasion of glioma cells.";
J. Neurooncol. 103:187-195(2011).
[14]
FUNCTION.
PubMed=21177806; DOI=10.1128/JVI.01531-10;
Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.;
"The IFITM proteins inhibit HIV-1 infection.";
J. Virol. 85:2126-2137(2011).
[15]
ERRATUM.
Lu J., Pan Q., Rong L., He W., Liu S.L., Liang C.;
J. Virol. 85:4043-4043(2011).
[16]
FUNCTION.
PubMed=21976647; DOI=10.1128/JVI.05633-11;
Raychoudhuri A., Shrivastava S., Steele R., Kim H., Ray R., Ray R.B.;
"ISG56 and IFITM1 proteins inhibit hepatitis C virus replication.";
J. Virol. 85:12881-12889(2011).
[17]
FUNCTION.
PubMed=21253575; DOI=10.1371/journal.ppat.1001258;
Huang I.C., Bailey C.C., Weyer J.L., Radoshitzky S.R., Becker M.M.,
Chiang J.J., Brass A.L., Ahmed A.A., Chi X., Dong L., Longobardi L.E.,
Boltz D., Kuhn J.H., Elledge S.J., Bavari S., Denison M.R., Choe H.,
Farzan M.;
"Distinct patterns of IFITM-mediated restriction of filoviruses, SARS
coronavirus, and influenza A virus.";
PLoS Pathog. 7:E1001258-E1001258(2011).
[18]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22634173; DOI=10.1016/j.bone.2012.05.012;
Kim B.S., Kim H.J., Kim J.S., You Y.O., Zadeh H., Shin H.I., Lee S.J.,
Park Y.J., Takata T., Pi S.H., Lee J., You H.K.;
"IFITM1 increases osteogenesis through Runx2 in human alveolar-derived
bone marrow stromal cells.";
Bone 51:506-514(2012).
[19]
FUNCTION.
PubMed=22479637; DOI=10.1371/journal.pone.0034508;
Chan Y.K., Huang I.C., Farzan M.;
"IFITM proteins restrict antibody-dependent enhancement of dengue
virus infection.";
PLoS ONE 7:E34508-E34508(2012).
[20]
GENE FAMILY.
PubMed=22363774; DOI=10.1371/journal.pone.0031961;
Sallman Almen M., Bringeland N., Fredriksson R., Schioth H.B.;
"The dispanins: a novel gene family of ancient origin that contains 14
human members.";
PLoS ONE 7:E31961-E31961(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, VARIANT [LARGE SCALE
ANALYSIS] ALA-13, 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).
[22]
SUBCELLULAR LOCATION, AND TOPOLOGY.
PubMed=25105503; DOI=10.1371/journal.pone.0104341;
Weston S., Czieso S., White I.J., Smith S.E., Kellam P., Marsh M.;
"A membrane topology model for human interferon inducible
transmembrane protein 1.";
PLoS ONE 9:E104341-E104341(2014).
[23]
VARIANT [LARGE SCALE ANALYSIS] ALA-13, AND 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).
-!- FUNCTION: IFN-induced antiviral protein which inhibits the entry
of viruses to the host cell cytoplasm, permitting endocytosis, but
preventing subsequent viral fusion and release of viral contents
into the cytosol. Active against multiple viruses, including
influenza A virus, SARS coronavirus (SARS-CoV), Marburg virus
(MARV), Ebola virus (EBOV), Dengue virus (DNV), West Nile virus
(WNV), human immunodeficiency virus type 1 (HIV-1) and hepatitis C
virus (HCV). Can inhibit: influenza virus hemagglutinin protein-
mediated viral entry, MARV and EBOV GP1,2-mediated viral entry and
SARS-CoV S protein-mediated viral entry. Also implicated in cell
adhesion and control of cell growth and migration. Plays a key
role in the antiproliferative action of IFN-gamma either by
inhibiting the ERK activation or by arresting cell growth in G1
phase in a p53-dependent manner. Acts as a positive regulator of
osteoblast differentiation. {ECO:0000269|PubMed:16847454,
ECO:0000269|PubMed:20064371, ECO:0000269|PubMed:20838853,
ECO:0000269|PubMed:21177806, ECO:0000269|PubMed:21253575,
ECO:0000269|PubMed:21976647, ECO:0000269|PubMed:22479637,
ECO:0000269|PubMed:22634173}.
-!- SUBUNIT: Interacts with CAV1; this interaction enhances the
ability of CAV1 in inhibiting ERK activation. Interacts with CD81.
{ECO:0000269|PubMed:19499152, ECO:0000269|PubMed:2398277}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19499152,
ECO:0000269|PubMed:25105503}; Single-pass membrane protein
{ECO:0000269|PubMed:19499152}.
-!- TISSUE SPECIFICITY: Bone (at protein level). Levels greatly
elevated in colon cancer, cervical cancer, esophageal cancer and
ovarian cancer. Expressed in glioma cell lines.
{ECO:0000269|PubMed:20838853, ECO:0000269|PubMed:22634173}.
-!- INDUCTION: By IFN-alpha and IFNG/IFN-gamma.
-!- PTM: Palmitoylation on membrane-proximal cysteines controls
clustering in membrane compartments and antiviral activity against
influenza virus. {ECO:0000250}.
-!- SIMILARITY: Belongs to the CD225/Dispanin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; J04164; AAA35494.1; -; mRNA.
EMBL; X84958; CAA59337.1; -; mRNA.
EMBL; BT007173; AAP35837.1; -; mRNA.
EMBL; AK290480; BAF83169.1; -; mRNA.
EMBL; AC136475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471278; EAW61218.1; -; Genomic_DNA.
EMBL; BC000897; AAH00897.1; -; mRNA.
CCDS; CCDS41584.1; -.
PIR; A31454; A31454.
RefSeq; NP_003632.3; NM_003641.3.
UniGene; Hs.458414; -.
ProteinModelPortal; P13164; -.
BioGrid; 114091; 4.
DIP; DIP-32672N; -.
IntAct; P13164; 4.
MINT; P13164; -.
STRING; 9606.ENSP00000330825; -.
TCDB; 8.A.58.1.1; the dispanin (dispanin) family.
iPTMnet; P13164; -.
PhosphoSitePlus; P13164; -.
SwissPalm; P13164; -.
BioMuta; IFITM1; -.
DMDM; 215274118; -.
EPD; P13164; -.
MaxQB; P13164; -.
PaxDb; P13164; -.
PeptideAtlas; P13164; -.
PRIDE; P13164; -.
ProteomicsDB; 52897; -.
TopDownProteomics; P13164; -.
DNASU; 8519; -.
Ensembl; ENST00000328221; ENSP00000330825; ENSG00000185885.
Ensembl; ENST00000408968; ENSP00000386187; ENSG00000185885.
Ensembl; ENST00000528780; ENSP00000437057; ENSG00000185885.
GeneID; 8519; -.
KEGG; hsa:8519; -.
UCSC; uc001loy.5; human.
CTD; 8519; -.
DisGeNET; 8519; -.
EuPathDB; HostDB:ENSG00000185885.15; -.
GeneCards; IFITM1; -.
HGNC; HGNC:5412; IFITM1.
HPA; CAB017615; -.
HPA; HPA004810; -.
MIM; 604456; gene.
neXtProt; NX_P13164; -.
OpenTargets; ENSG00000185885; -.
PharmGKB; PA29653; -.
eggNOG; ENOG410J2DU; Eukaryota.
eggNOG; ENOG4112C1U; LUCA.
GeneTree; ENSGT00390000003476; -.
HOGENOM; HOG000115781; -.
HOVERGEN; HBG001182; -.
InParanoid; P13164; -.
KO; K19831; -.
OMA; MINIQSE; -.
OrthoDB; EOG091G1143; -.
PhylomeDB; P13164; -.
TreeFam; TF334894; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
Reactome; R-HSA-909733; Interferon alpha/beta signaling.
ChiTaRS; IFITM1; human.
GeneWiki; IFITM1; -.
GenomeRNAi; 8519; -.
PRO; PR:P13164; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000185885; Expressed in 223 organ(s), highest expression level in blood.
CleanEx; HS_IFITM1; -.
Genevisible; P13164; HS.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:ProtInc.
GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0008285; P:negative regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0046597; P:negative regulation of viral entry into host cell; IDA:UniProtKB.
GO; GO:0045071; P:negative regulation of viral genome replication; IDA:UniProtKB.
GO; GO:0001503; P:ossification; IEA:UniProtKB-KW.
GO; GO:0045669; P:positive regulation of osteoblast differentiation; IMP:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
GO; GO:0035455; P:response to interferon-alpha; IDA:UniProtKB.
GO; GO:0035456; P:response to interferon-beta; IDA:UniProtKB.
GO; GO:0034341; P:response to interferon-gamma; IDA:UniProtKB.
GO; GO:0009615; P:response to virus; IDA:UniProtKB.
GO; GO:0060337; P:type I interferon signaling pathway; TAS:Reactome.
InterPro; IPR007593; CD225/Dispanin_fam.
Pfam; PF04505; CD225; 1.
1: Evidence at protein level;
Antiviral defense; Cell membrane; Complete proteome; Immunity;
Innate immunity; Lipoprotein; Membrane; Osteogenesis; Palmitate;
Phosphoprotein; Polymorphism; Reference proteome; Transmembrane;
Transmembrane helix.
CHAIN 1 125 Interferon-induced transmembrane protein
1.
/FTId=PRO_0000153727.
TOPO_DOM 1 36 Cytoplasmic. {ECO:0000255}.
INTRAMEM 37 57 Helical. {ECO:0000303|PubMed:25105503}.
TOPO_DOM 58 86 Cytoplasmic. {ECO:0000255}.
TRANSMEM 87 107 Helical. {ECO:0000255}.
TOPO_DOM 108 125 Extracellular. {ECO:0000255}.
REGION 84 125 Interaction with CAV1.
{ECO:0000269|PubMed:19499152}.
MOD_RES 16 16 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
LIPID 50 50 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 51 51 S-palmitoyl cysteine. {ECO:0000250}.
LIPID 84 84 S-palmitoyl cysteine. {ECO:0000250}.
VARIANT 13 13 P -> A (in dbSNP:rs9667990).
{ECO:0000244|PubMed:21269460,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:2492664,
ECO:0000269|PubMed:7559564,
ECO:0000269|Ref.3, ECO:0000269|Ref.6}.
/FTId=VAR_047422.
CONFLICT 103 103 L -> S (in Ref. 1; AAA35494).
{ECO:0000305}.
SEQUENCE 125 AA; 13964 MW; 10EE5B64894838ED CRC64;
MHKEEHEVAV LGPPPSTILP RSTVINIHSE TSVPDHVVWS LFNTLFLNWC CLGFIAFAYS
VKSRDRKMVG DVTGAQAYAS TAKCLNIWAL ILGILMTIGF ILLLVFGSVT VYHIMLQIIQ
EKRGY


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E0371r ELISA kit 10 kDa interferon gamma-induced protein,C-X-C motif chemokine 10,Cxcl10,Gamma-IP10,Inp10,Interferon-inducible protein 10,IP-10,Mob1,Protein Mob-1,Rat,Rattus norvegicus,Scyb10,Small-inducibl 96T
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EIAAB12244 eIF-2A protein kinase 2,Eif2ak2,Eukaryotic translation initiation factor 2-alpha kinase 2,Interferon-induced, double-stranded RNA-activated protein kinase,Interferon-inducible RNA-dependent protein ki
EIAAB12245 eIF-2A protein kinase 2,EIF2AK2,Eukaryotic translation initiation factor 2-alpha kinase 2,Homo sapiens,Human,Interferon-induced, double-stranded RNA-activated protein kinase,Interferon-inducible RNA-d
EIAAB25872 Chicken,Gallus gallus,Interferon-induced GTP-binding protein Mx,Interferon-inducible Mx protein,MX
EIAAB32393 Interferon-inducible double stranded RNA-dependent protein kinase activator A,Prkra,Protein activator of the interferon-induced protein kinase,Protein kinase, interferon-inducible double stranded RNA-
18-003-42929 Interferon-induced. double-stranded RNA-activated protein kinase - EC 2.7.11.1; Interferon-inducible RNA-dependent protein kinase; Protein kinase RNA-activated; PKR; p68 kinase; P1_eIF-2A protein kina 0.05 mg Aff Pur
E1928h ELISA CMK,C-X-C motif chemokine 9,CXCL9,Gamma-interferon-induced monokine,Homo sapiens,Human,HuMIG,MIG,MIG,Monokine induced by interferon-gamma,SCYB9,Small-inducible cytokine B9 96T
U1928h CLIA kit CMK,C-X-C motif chemokine 9,CXCL9,Gamma-interferon-induced monokine,Homo sapiens,Human,HuMIG,MIG,MIG,Monokine induced by interferon-gamma,SCYB9,Small-inducible cytokine B9 96T
E1928h ELISA kit CMK,C-X-C motif chemokine 9,CXCL9,Gamma-interferon-induced monokine,Homo sapiens,Human,HuMIG,MIG,MIG,Monokine induced by interferon-gamma,SCYB9,Small-inducible cytokine B9 96T
U1928h CLIA CMK,C-X-C motif chemokine 9,CXCL9,Gamma-interferon-induced monokine,Homo sapiens,Human,HuMIG,MIG,MIG,Monokine induced by interferon-gamma,SCYB9,Small-inducible cytokine B9 96T


 

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