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Epithelial membrane protein 2 (EMP-2) (Protein XMP)

 EMP2_HUMAN              Reviewed;         167 AA.
P54851; B2R7V6; D3DUF8;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
01-OCT-1996, sequence version 1.
05-DEC-2018, entry version 148.
RecName: Full=Epithelial membrane protein 2;
Short=EMP-2;
AltName: Full=Protein XMP;
Name=EMP2; Synonyms=XMP;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Spleen;
PubMed=8917086; DOI=10.1016/0378-1119(96)00134-5;
Taylor V., Suter U.;
"Epithelial membrane protein-2 and epithelial membrane protein-3: two
novel members of the peripheral myelin protein 22 gene family.";
Gene 175:115-120(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=8996089; DOI=10.1016/S0378-1119(96)00475-1;
Ben-Porath I., Benvenisty N.;
"Characterization of a tumor-associated gene, a member of a novel
family of genes encoding membrane glycoproteins.";
Gene 183:69-75(1996).
[3]
SEQUENCE REVISION.
Ben-Porath I., Benvenisty N.;
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Kim Y.-S., Ueda E., Borok Z., Kim S.-Y., Jetten A.M.;
"Genomic structure of the human epithelial membrane protein 2 (EMP2)
gene; regulation by two alternative promoters.";
Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Tongue;
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).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
FUNCTION, INTERACTION WITH P2RX7, AND SUBCELLULAR LOCATION.
PubMed=12107182; DOI=10.1074/jbc.M205120200;
Wilson H.L., Wilson S.A., Surprenant A., North R.A.;
"Epithelial membrane proteins induce membrane blebbing and interact
with the P2X7 receptor C terminus.";
J. Biol. Chem. 277:34017-34023(2002).
[9]
TISSUE SPECIFICITY.
PubMed=12710941; DOI=10.1016/S0014-4800(03)00009-1;
Wadehra M., Sulur G.G., Braun J., Gordon L.K., Goodglick L.;
"Epithelial membrane protein-2 is expressed in discrete anatomical
regions of the eye.";
Exp. Mol. Pathol. 74:106-112(2003).
[10]
FUNCTION, AND INTERACTION WITH ITGB3.
PubMed=16216233; DOI=10.1016/j.ydbio.2005.09.003;
Wadehra M., Forbes A., Pushkarna N., Goodglick L., Gordon L.K.,
Williams C.J., Braun J.;
"Epithelial membrane protein-2 regulates surface expression of
alphavbeta3 integrin in the endometrium.";
Dev. Biol. 287:336-345(2005).
[11]
FUNCTION.
PubMed=16487956; DOI=10.1016/j.ydbio.2006.01.015;
Wadehra M., Dayal M., Mainigi M., Ord T., Iyer R., Braun J.,
Williams C.J.;
"Knockdown of the tetraspan protein epithelial membrane protein-2
inhibits implantation in the mouse.";
Dev. Biol. 292:430-441(2006).
[12]
INDUCTION.
PubMed=18400107; DOI=10.1186/1477-7827-6-15;
Wadehra M., Mainigi M., Morales S.A., Rao R.G., Gordon L.K.,
Williams C.J., Braun J.;
"Steroid hormone regulation of EMP2 expression and localization in the
endometrium.";
Reprod. Biol. Endocrinol. 6:15-15(2008).
[13]
INTERACTION WITH PTK2, AND FUNCTION.
PubMed=19494199; DOI=10.1167/iovs.08-3315;
Morales S.A., Mareninov S., Coulam P., Wadehra M., Goodglick L.,
Braun J., Gordon L.K.;
"Functional consequences of interactions between FAK and epithelial
membrane protein 2 (EMP2).";
Invest. Ophthalmol. Vis. Sci. 50:4949-4956(2009).
[14]
FUNCTION, INTERACTION WITH PTK2, AND SUBCELLULAR LOCATION.
PubMed=21637765; DOI=10.1371/journal.pone.0019945;
Fu M., Rao R., Sudhakar D., Hogue C.P., Rutta Z., Morales S.,
Gordon L.K., Braun J., Goodglick L., Wadehra M.;
"Epithelial membrane protein-2 promotes endometrial tumor formation
through activation of FAK and Src.";
PLoS ONE 6:E19945-E19945(2011).
[15]
FUNCTION.
PubMed=22728127; DOI=10.1016/j.exer.2012.06.002;
Morales S.A., Telander D.G., Mareninov S., Nagy A., Wadehra M.,
Braun J., Gordon L.K.;
"Anti-EMP2 diabody blocks epithelial membrane protein 2 (EMP2) and FAK
mediated collagen gel contraction in ARPE-19 cells.";
Exp. Eye Res. 102:10-16(2012).
[16]
FUNCTION.
PubMed=23439602; DOI=10.1167/iovs.12-11013;
Morales S.A., Telander D.G., Leon D., Forward K., Braun J.,
Wadehra M., Gordon L.K.;
"Epithelial membrane protein 2 controls VEGF expression in ARPE-19
cells.";
Invest. Ophthalmol. Vis. Sci. 54:2367-2372(2013).
[17]
FUNCTION.
PubMed=23334331; DOI=10.1038/onc.2012.622;
Gordon L.K., Kiyohara M., Fu M., Braun J., Dhawan P., Chan A.,
Goodglick L., Wadehra M.;
"EMP2 regulates angiogenesis in endometrial cancer cells through
induction of VEGF.";
Oncogene 32:5369-5376(2013).
[18]
FUNCTION, INVOLVEMENT IN NPHS10, VARIANTS NPHS10 LEU-7 AND THR-10, AND
CHARACTERIZATION OF VARIANTS NPHS10 LEU-7 AND THR-10.
PubMed=24814193; DOI=10.1016/j.ajhg.2014.04.010;
Gee H.Y., Ashraf S., Wan X., Vega-Warner V., Esteve-Rudd J.,
Lovric S., Fang H., Hurd T.W., Sadowski C.E., Allen S.J., Otto E.A.,
Korkmaz E., Washburn J., Levy S., Williams D.S., Bakkaloglu S.A.,
Zolotnitskaya A., Ozaltin F., Zhou W., Hildebrandt F.;
"Mutations in EMP2 cause childhood-onset nephrotic syndrome.";
Am. J. Hum. Genet. 94:884-890(2014).
-!- FUNCTION: Functions as a key regulator of cell membrane
composition by regulating proteins surface expression. Also, plays
a role in regulation of processes including cell migration, cell
proliferation, cell contraction and cell adhesion. Negatively
regulates caveolae formation by reducing CAV1 expression and CAV1
amount by increasing lysosomal degradation (PubMed:24814193).
Facilitates surface trafficking and formation of lipid rafts
bearing GPI-anchor proteins (By similarity). Regulates surface
expression of MHC1 and ICAM1 proteins increasing susceptibility to
T-cell mediated cytotoxicity (By similarity). Regulates the plasma
membrane expression of the integrin heterodimers ITGA6-ITGB1,
ITGA5-ITGB3 and ITGA5-ITGB1 resulting in modulation of cell-matrix
adhesion (PubMed:16216233). Also regulates many processes through
PTK2. Regulates blood vessel endothelial cell migration and
angiogenesis by regulating VEGF protein expression through PTK2
activation (PubMed:23439602). Regulates cell migration and cell
contraction through PTK2 and SRC activation (PubMed:21637765,
PubMed:22728127). Regulates focal adhesion density, F-actin
conformation and cell adhesion capacity through interaction with
PTK2 (PubMed:19494199). Positively regulates cell proliferation
(PubMed:24814193). Plays a role during cell death and cell
blebbing (PubMed:12107182). Promotes angiogenesis and
vasculogenesis through induction of VEGFA via a HIF1A-dependent
pathway (PubMed:23334331). Also plays a role in embryo
implantation by regulating surface trafficking of integrin
heterodimer ITGA5-ITGB3 (PubMed:16487956). May play a role in
glomerular filtration (By similarity).
{ECO:0000250|UniProtKB:F1QIK8, ECO:0000250|UniProtKB:O88662,
ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233,
ECO:0000269|PubMed:16487956, ECO:0000269|PubMed:19494199,
ECO:0000269|PubMed:21637765, ECO:0000269|PubMed:22728127,
ECO:0000269|PubMed:23334331, ECO:0000269|PubMed:23439602,
ECO:0000269|PubMed:24814193}.
-!- SUBUNIT: Interacts with PTK2; regulates PTK2 activation and
localization (PubMed:19494199, PubMed:21637765). Interacts with
ITGB3; regulates the levels of the heterodimer ITGA5-ITGB3
integrin surface expression (PubMed:16216233). Interacts with
P2RX7 (via C-terminus) (PubMed:12107182). Interacts with ITGB1;
the interaction may be direct or indirect and ITGB1 has a
heterodimer form (By similarity). {ECO:0000250|UniProtKB:O88662,
ECO:0000269|PubMed:12107182, ECO:0000269|PubMed:16216233,
ECO:0000269|PubMed:19494199, ECO:0000269|PubMed:21637765}.
-!- SUBCELLULAR LOCATION: Golgi apparatus membrane
{ECO:0000250|UniProtKB:O88662}; Multi-pass membrane protein
{ECO:0000255}. Cell membrane {ECO:0000269|PubMed:12107182,
ECO:0000269|PubMed:21637765}. Apical cell membrane
{ECO:0000250|UniProtKB:O88662}. Membrane raft
{ECO:0000269|PubMed:21637765}. Cytoplasm
{ECO:0000269|PubMed:21637765}. Nucleus
{ECO:0000250|UniProtKB:Q66HH2}. Note=Localizes in cytoplasm, foot
processes and cell bodies of podocytes and nucleus of endothelial
cells of kidney. Localizes to the apical cell surface in the
luminal epithelium and glandular epithelium. Colocalized with
ITGB1 and GPI-anchor proteins on plasma membrane.
{ECO:0000250|UniProtKB:O88662, ECO:0000250|UniProtKB:Q66HH2}.
-!- TISSUE SPECIFICITY: Expressed in ciliary body epithelia, sclera,
cornea, and retinal pigment epithelium (at protein level)
(PubMed:12710941). {ECO:0000269|PubMed:12710941}.
-!- INDUCTION: Up-regulated by progesterone, increasing plasma
membrane expression. {ECO:0000269|PubMed:18400107}.
-!- DISEASE: Nephrotic syndrome 10 (NPHS10) [MIM:615861]: A form of
nephrotic syndrome, a renal disease clinically characterized by
focal segmental glomerulosclerosis, progressive renal failure,
severe proteinuria, hypoalbuminemia, hyperlipidemia and edema.
NPHS10 is a steroid-sensitive form characterized by onset in
childhood and remission without end-stage kidney disease.
{ECO:0000269|PubMed:24814193}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the PMP-22/EMP/MP20 family. {ECO:0000305}.
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EMBL; U52100; AAC51779.1; -; mRNA.
EMBL; X94770; CAA64393.1; -; mRNA.
EMBL; AY057060; AAL27085.1; -; Genomic_DNA.
EMBL; AK313134; BAG35953.1; -; mRNA.
EMBL; CH471112; EAW85180.1; -; Genomic_DNA.
EMBL; CH471112; EAW85181.1; -; Genomic_DNA.
EMBL; CH471112; EAW85182.1; -; Genomic_DNA.
EMBL; BC009687; AAH09687.1; -; mRNA.
CCDS; CCDS10541.1; -.
PIR; JC5044; JC5044.
PIR; JC5732; JC5732.
RefSeq; NP_001415.1; NM_001424.5.
RefSeq; XP_006720927.1; XM_006720864.3.
UniGene; Hs.531561; -.
ProteinModelPortal; P54851; -.
SMR; P54851; -.
BioGrid; 108328; 2.
IntAct; P54851; 2.
STRING; 9606.ENSP00000352540; -.
iPTMnet; P54851; -.
PhosphoSitePlus; P54851; -.
BioMuta; EMP2; -.
DMDM; 1706643; -.
PaxDb; P54851; -.
PeptideAtlas; P54851; -.
PRIDE; P54851; -.
ProteomicsDB; 56740; -.
DNASU; 2013; -.
Ensembl; ENST00000359543; ENSP00000352540; ENSG00000213853.
Ensembl; ENST00000536829; ENSP00000445712; ENSG00000213853.
GeneID; 2013; -.
KEGG; hsa:2013; -.
UCSC; uc002czx.4; human.
CTD; 2013; -.
DisGeNET; 2013; -.
EuPathDB; HostDB:ENSG00000213853.9; -.
GeneCards; EMP2; -.
HGNC; HGNC:3334; EMP2.
HPA; HPA014711; -.
MalaCards; EMP2; -.
MIM; 602334; gene.
MIM; 615861; phenotype.
neXtProt; NX_P54851; -.
OpenTargets; ENSG00000213853; -.
Orphanet; 93216; Familial idiopathic steroid-resistant nephrotic syndrome with minimal changes.
Orphanet; 93209; Idiopathic steroid-sensitive nephrotic syndrome with diffuse mesangial proliferation.
Orphanet; 93206; Idiopathic steroid-sensitive nephrotic syndrome with focal segmental hyalinosis.
Orphanet; 93207; Idiopathic steroid-sensitive nephrotic syndrome with minimal change.
PharmGKB; PA27771; -.
eggNOG; ENOG410IH06; Eukaryota.
eggNOG; ENOG4111QXD; LUCA.
GeneTree; ENSGT00940000153917; -.
HOGENOM; HOG000059542; -.
HOVERGEN; HBG001690; -.
InParanoid; P54851; -.
OMA; NNTNCTE; -.
OrthoDB; EOG091G0RF4; -.
PhylomeDB; P54851; -.
TreeFam; TF330414; -.
ChiTaRS; EMP2; human.
GeneWiki; EMP2; -.
GenomeRNAi; 2013; -.
PRO; PR:P54851; -.
Proteomes; UP000005640; Chromosome 16.
Bgee; ENSG00000213853; Expressed in 213 organ(s), highest expression level in visceral pleura.
CleanEx; HS_EMP2; -.
Genevisible; P54851; HS.
GO; GO:0045177; C:apical part of cell; ISS:UniProtKB.
GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; ISS:UniProtKB.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0031410; C:cytoplasmic vesicle; IEA:Ensembl.
GO; GO:0005829; C:cytosol; IEA:GOC.
GO; GO:0005794; C:Golgi apparatus; ISS:UniProtKB.
GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
GO; GO:0045121; C:membrane raft; IDA:UniProtKB.
GO; GO:0005634; C:nucleus; ISS:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0005178; F:integrin binding; IPI:MGI.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0019901; F:protein kinase binding; IPI:UniProtKB.
GO; GO:0007015; P:actin filament organization; IDA:UniProtKB.
GO; GO:0070252; P:actin-mediated cell contraction; IDA:UniProtKB.
GO; GO:0032147; P:activation of protein kinase activity; IDA:UniProtKB.
GO; GO:0032060; P:bleb assembly; IDA:UniProtKB.
GO; GO:0043534; P:blood vessel endothelial cell migration; IDA:UniProtKB.
GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
GO; GO:0008219; P:cell death; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0008283; P:cell proliferation; TAS:ProtInc.
GO; GO:0007160; P:cell-matrix adhesion; IDA:UniProtKB.
GO; GO:0045022; P:early endosome to late endosome transport; ISS:UniProtKB.
GO; GO:0007566; P:embryo implantation; IMP:UniProtKB.
GO; GO:0001765; P:membrane raft assembly; ISS:UniProtKB.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:UniProtKB.
GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IDA:MGI.
GO; GO:2001046; P:positive regulation of integrin-mediated signaling pathway; IDA:MGI.
GO; GO:0034394; P:protein localization to cell surface; IMP:UniProtKB.
GO; GO:0072659; P:protein localization to plasma membrane; ISS:UniProtKB.
GO; GO:0045765; P:regulation of angiogenesis; IDA:UniProtKB.
GO; GO:0001952; P:regulation of cell-matrix adhesion; IBA:GO_Central.
GO; GO:0010594; P:regulation of endothelial cell migration; IDA:UniProtKB.
GO; GO:0003093; P:regulation of glomerular filtration; IDA:UniProtKB.
GO; GO:0043549; P:regulation of kinase activity; IDA:UniProtKB.
GO; GO:2001212; P:regulation of vasculogenesis; IDA:UniProtKB.
GO; GO:0001913; P:T cell mediated cytotoxicity; ISS:UniProtKB.
InterPro; IPR003933; EMP-2.
InterPro; IPR004031; PMP22/EMP/MP20/Claudin.
InterPro; IPR004032; PMP22_EMP_MP20.
PANTHER; PTHR10671:SF32; PTHR10671:SF32; 1.
Pfam; PF00822; PMP22_Claudin; 1.
PRINTS; PR01453; EPMEMFAMILY.
PRINTS; PR01455; EPMEMPROT2.
PROSITE; PS01221; PMP22_1; 1.
PROSITE; PS01222; PMP22_2; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Cytoplasm; Disease mutation;
Glycoprotein; Golgi apparatus; Membrane; Nucleus; Reference proteome;
Transmembrane; Transmembrane helix.
CHAIN 1 167 Epithelial membrane protein 2.
/FTId=PRO_0000164658.
TRANSMEM 1 21 Helical. {ECO:0000255}.
TRANSMEM 67 87 Helical. {ECO:0000255}.
TRANSMEM 95 115 Helical. {ECO:0000255}.
TRANSMEM 143 163 Helical. {ECO:0000255}.
CARBOHYD 44 44 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 47 47 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 52 52 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VARIANT 7 7 F -> L (in NPHS10; decreased amount of
CAV1; dbSNP:rs730882194).
{ECO:0000269|PubMed:24814193}.
/FTId=VAR_071478.
VARIANT 10 10 A -> T (in NPHS10; decreased amount of
CAV1; dbSNP:rs587777482).
{ECO:0000269|PubMed:24814193}.
/FTId=VAR_071479.
CONFLICT 20 20 F -> L (in Ref. 3; CAA64393).
{ECO:0000305}.
CONFLICT 64 64 V -> F (in Ref. 3; CAA64393).
{ECO:0000305}.
SEQUENCE 167 AA; 19199 MW; 3E341DF3581EBCBF CRC64;
MLVLLAFIIA FHITSAALLF IATVDNAWWV GDEFFADVWR ICTNNTNCTV INDSFQEYST
LQAVQATMIL STILCCIAFF IFVLQLFRLK QGERFVLTSI IQLMSCLCVM IAASIYTDRR
EDIHDKNAKF YPVTREGSYG YSYILAWVAF ACTFISGMMY LILRKRK


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ARP41470_T100 Epithelial membrane protein 2 (EMP2) 100 µg
SP-88512-1 EMP-1 (Epithelial Membrane Protein) (AA: Gly-Gly-Thr-Tyr-Ser-Cys-His-Phe-Gly-Pro-Leu-Thr-Trp-Val-Cys-Lys-Pro-Gln-Gly-Gly) (MW: 2093.39) 1 mg
EB07249 Epithelial membrane protein 3 (EMP3) 0.1 mg
EB07249 Epithelial membrane protein 3 (EMP3) 0.1 mg
CENPS_MOUSE Rat ELISA Kit FOR Epithelial membrane protein 1 96T


 

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