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Disintegrin and metalloproteinase domain-containing protein 9 (ADAM 9) (EC 3.4.24.-) (Meltrin-gamma) (Metalloprotease/disintegrin/cysteine-rich protein 9) (Myeloma cell metalloproteinase)

 ADAM9_MOUSE             Reviewed;         845 AA.
Q61072; E9QPP2; Q60618; Q61853; Q80U94;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
27-SEP-2017, entry version 146.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
Short=ADAM 9;
EC=3.4.24.-;
AltName: Full=Meltrin-gamma;
AltName: Full=Metalloprotease/disintegrin/cysteine-rich protein 9;
AltName: Full=Myeloma cell metalloproteinase;
Flags: Precursor;
Name=Adam9 {ECO:0000312|MGI:MGI:105376};
Synonyms=Kiaa0021 {ECO:0000312|EMBL:BAC65470.1}, Mdc9, Mltng;
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=Lung;
PubMed=8647900; DOI=10.1083/jcb.132.4.717;
Weskamp G., Kraetzschmar J., Reid M.S., Blobel C.P.;
"MDC9, a widely expressed cellular disintegrin containing cytoplasmic
SH3 ligand domains.";
J. Cell Biol. 132:717-726(1996).
[2] {ECO:0000312|EMBL:BAC65470.1}
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain {ECO:0000312|EMBL:BAC65470.1};
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=FVB/N-3; TISSUE=Mammary gland;
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 426-575.
PubMed=7566181; DOI=10.1038/377652a0;
Yagami-Hiromasa T., Sato T., Kurisaki T., Kamijo K., Nabeshima Y.,
Fujisawa-Sehara A.;
"A metalloprotease-disintegrin participating in myoblast fusion.";
Nature 377:652-656(1995).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 432-478.
STRAIN=BALB/cJ;
PubMed=8146185; DOI=10.1073/pnas.91.7.2748;
Weskamp G., Blobel C.P.;
"A family of cellular proteins related to snake venom disintegrins.";
Proc. Natl. Acad. Sci. U.S.A. 91:2748-2751(1994).
[7]
FUNCTION, PHOSPHORYLATION, ENZYME REGULATION, AND PROTEIN SEQUENCE OF
206-212.
PubMed=9920899; DOI=10.1074/jbc.274.6.3531;
Roghani M., Becherer J.D., Moss M.L., Atherton R.E.,
Erdjument-Bromage H., Arribas J., Blackburn R.K., Weskamp G.,
Tempst P., Blobel C.P.;
"Metalloprotease-disintegrin MDC9: intracellular maturation and
catalytic activity.";
J. Biol. Chem. 274:3531-3540(1999).
[8]
INTERACTION WITH SH3GL2 AND SNX9.
PubMed=10531379; DOI=10.1074/jbc.274.44.31693;
Howard L., Nelson K.K., Maciewicz R.A., Blobel C.P.;
"Interaction of the metalloprotease disintegrins MDC9 and MDC15 with
two SH3 domain-containing proteins, endophilin I and SH3PX1.";
J. Biol. Chem. 274:31693-31699(1999).
[9]
FUNCTION, AND INTERACTION WITH ITGA6.
PubMed=10825303;
Nath D., Slocombe P.M., Webster A., Stephens P.E., Docherty A.J.,
Murphy G.;
"Meltrin gamma(ADAM-9) mediates cellular adhesion through
alpha(6)beta(1)integrin, leading to a marked induction of fibroblast
cell motility.";
J. Cell Sci. 113:2319-2328(2000).
[10]
DISRUPTION PHENOTYPE.
PubMed=11839819; DOI=10.1128/MCB.22.5.1537-1544.2002;
Weskamp G., Cai H., Brodie T.A., Higashyama S., Manova K., Ludwig T.,
Blobel C.P.;
"Mice lacking the metalloprotease-disintegrin MDC9 (ADAM9) have no
evident major abnormalities during development or adult life.";
Mol. Cell. Biol. 22:1537-1544(2002).
[11]
DISRUPTION PHENOTYPE.
PubMed=19409519; DOI=10.1016/j.ajhg.2009.04.005;
Parry D.A., Toomes C., Bida L., Danciger M., Towns K.V., McKibbin M.,
Jacobson S.G., Logan C.V., Ali M., Bond J., Chance R., Swendeman S.,
Daniele L.L., Springell K., Adams M., Johnson C.A., Booth A.P.,
Jafri H., Rashid Y., Banin E., Strom T.M., Farber D.B., Sharon D.,
Blobel C.P., Pugh E.N. Jr., Pierce E.A., Inglehearn C.F.;
"Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in
humans and retinal degeneration in mice.";
Am. J. Hum. Genet. 84:683-691(2009).
[12]
FUNCTION, AND MUTAGENESIS OF GLU-348.
PubMed=19273593; DOI=10.1128/MCB.01460-08;
Guaiquil V., Swendeman S., Yoshida T., Chavala S., Campochiaro P.A.,
Blobel C.P.;
"ADAM9 is involved in pathological retinal neovascularization.";
Mol. Cell. Biol. 29:2694-2703(2009).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Kidney, and Testis;
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]
MUTAGENESIS OF ARG-53; ARG-56; ARG-202 AND ARG-205, SUBCELLULAR
LOCATION, AND ENZYME REGULATION.
PubMed=25795784; DOI=10.1074/jbc.M114.624072;
Wong E., Maretzky T., Peleg Y., Blobel C.P., Sagi I.;
"The functional maturation of a disintegrin and metalloproteinase
(ADAM) 9, 10, and 17 requires processing at a newly identified
proprotein convertase (PC) cleavage site.";
J. Biol. Chem. 290:12135-12146(2015).
-!- FUNCTION: Cleaves and releases a number of molecules with
important roles in tumorigenesis and angiogenesis, such as TEK,
KDR, EPHB4, CD40, VCAM1 and CDH5 (PubMed:19273593). May mediate
cell-cell, cell-matrix interactions and regulate the motility of
cells via interactions with integrins (PubMed:10825303).
{ECO:0000269|PubMed:10825303, ECO:0000269|PubMed:19273593}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- ENZYME REGULATION: Synthesized as an inactive form which is
proteolytically cleaved to generate an active enzyme. Processing
at the upstream site is particularly important for activation of
the proenzyme, whereas processing at the boundary between the pro-
domain and the catalytic domain does not appear to be essential
(PubMed:25795784). Inhibited by hydroxamic acid-based inhibitors
(PubMed:9920899). {ECO:0000269|PubMed:25795784,
ECO:0000269|PubMed:9920899}.
-!- SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic
tail (PubMed:10531379). Interacts with ITGA6 (PubMed:10825303).
{ECO:0000269|PubMed:10531379, ECO:0000269|PubMed:10825303}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25795784,
ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}.
-!- PTM: Proteolytically cleaved in the trans-Golgi network before it
reaches the plasma membrane to generate a mature protein. The
removal of the pro-domain occurs via cleavage at two different
sites. Processed most likely by a pro-protein convertase such as
furin, at the boundary between the pro-domain and the catalytic
domain. An additional upstream cleavage pro-protein convertase
site (Arg-56/Glu-57) has an important role in the activation of
ADAM9. {ECO:0000269|PubMed:25795784, ECO:0000269|PubMed:9920899}.
-!- PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-
13-acetate (PMA) (PubMed:9920899). {ECO:0000269|PubMed:9920899}.
-!- DISRUPTION PHENOTYPE: Deficient mice appear to develop normally,
are viable and fertile, and do not have any major pathological
phenotypes (PubMed:11839819). In adulthood, 20 months after birth,
mice display progressive retinal degeneration, disorganized
retinal layers and a degenerate retinal pigment epithelium
(PubMed:19409519). {ECO:0000269|PubMed:11839819,
ECO:0000269|PubMed:19409519}.
-!- SEQUENCE CAUTION:
Sequence=BAC65470.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
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EMBL; U41765; AAC52446.1; -; mRNA.
EMBL; AK122188; BAC65470.1; ALT_INIT; mRNA.
EMBL; AC156553; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC047156; AAH47156.1; -; mRNA.
EMBL; D50412; BAA08913.1; -; mRNA.
EMBL; U06145; AAA18424.1; -; mRNA.
PIR; I48943; I48943.
PIR; S60259; S60259.
RefSeq; NP_031430.2; NM_007404.2.
UniGene; Mm.28908; -.
ProteinModelPortal; Q61072; -.
SMR; Q61072; -.
BioGrid; 197973; 1.
IntAct; Q61072; 2.
MINT; MINT-252904; -.
STRING; 10090.ENSMUSP00000081048; -.
MEROPS; M12.209; -.
iPTMnet; Q61072; -.
PhosphoSitePlus; Q61072; -.
EPD; Q61072; -.
MaxQB; Q61072; -.
PaxDb; Q61072; -.
PRIDE; Q61072; -.
Ensembl; ENSMUST00000084035; ENSMUSP00000081048; ENSMUSG00000031555.
GeneID; 11502; -.
KEGG; mmu:11502; -.
UCSC; uc009lfk.2; mouse.
CTD; 8754; -.
MGI; MGI:105376; Adam9.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00760000118888; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q61072; -.
KO; K06834; -.
OrthoDB; EOG091G01NX; -.
TreeFam; TF314733; -.
BRENDA; 3.4.24.B9; 3474.
PRO; PR:Q61072; -.
Proteomes; UP000000589; Chromosome 8.
Bgee; ENSMUSG00000031555; -.
ExpressionAtlas; Q61072; baseline and differential.
Genevisible; Q61072; MM.
GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:MGI.
GO; GO:0070062; C:extracellular exosome; ISO:MGI.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031233; C:intrinsic component of external side of plasma membrane; IDA:BHF-UCL.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005518; F:collagen binding; ISO:MGI.
GO; GO:0005178; F:integrin binding; ISO:MGI.
GO; GO:0043236; F:laminin binding; ISO:MGI.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:BHF-UCL.
GO; GO:0008237; F:metallopeptidase activity; ISO:MGI.
GO; GO:0005080; F:protein kinase C binding; IPI:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IDA:BHF-UCL.
GO; GO:0000186; P:activation of MAPKK activity; ISO:MGI.
GO; GO:0007155; P:cell adhesion; ISO:MGI.
GO; GO:0033627; P:cell adhesion mediated by integrin; IDA:UniProtKB.
GO; GO:0016477; P:cell migration; IDA:UniProtKB.
GO; GO:0007160; P:cell-matrix adhesion; ISO:MGI.
GO; GO:0071222; P:cellular response to lipopolysaccharide; ISO:MGI.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:UniProtKB.
GO; GO:0042117; P:monocyte activation; ISO:MGI.
GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; ISO:MGI.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; ISO:MGI.
GO; GO:0051549; P:positive regulation of keratinocyte migration; ISO:MGI.
GO; GO:0034241; P:positive regulation of macrophage fusion; ISO:MGI.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; ISO:MGI.
GO; GO:0051592; P:response to calcium ion; ISO:MGI.
GO; GO:0051384; P:response to glucocorticoid; IMP:BHF-UCL.
GO; GO:0042542; P:response to hydrogen peroxide; ISO:MGI.
GO; GO:0010042; P:response to manganese ion; ISO:MGI.
GO; GO:0034612; P:response to tumor necrosis factor; ISO:MGI.
GO; GO:0007179; P:transforming growth factor beta receptor signaling pathway; IMP:BHF-UCL.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 2.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR001590; Peptidase_M12B.
InterPro; IPR002870; Peptidase_M12B_N.
InterPro; IPR034027; Reprolysin_adamalysin.
Pfam; PF08516; ADAM_CR; 1.
Pfam; PF00200; Disintegrin; 1.
Pfam; PF01562; Pep_M12B_propep; 1.
Pfam; PF01421; Reprolysin; 1.
PRINTS; PR00289; DISINTEGRIN.
SMART; SM00608; ACR; 1.
SMART; SM00050; DISIN; 1.
SUPFAM; SSF57552; SSF57552; 1.
PROSITE; PS50215; ADAM_MEPRO; 1.
PROSITE; PS00427; DISINTEGRIN_1; 1.
PROSITE; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Cell membrane; Complete proteome; Direct protein sequencing;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; Signal; Transmembrane; Transmembrane helix; Zinc;
Zymogen.
SIGNAL 1 29 {ECO:0000255}.
CHAIN 30 845 Disintegrin and metalloproteinase domain-
containing protein 9.
/FTId=PRO_0000029063.
TOPO_DOM 30 697 Extracellular. {ECO:0000255}.
TRANSMEM 698 718 Helical. {ECO:0000255}.
TOPO_DOM 719 845 Cytoplasmic. {ECO:0000255}.
DOMAIN 212 406 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 414 501 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 644 698 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
COMPBIAS 505 634 Cys-rich.
ACT_SITE 348 348 {ECO:0000250|UniProtKB:P78536,
ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 347 347 Zinc; catalytic. {ECO:0000250}.
METAL 351 351 Zinc; catalytic. {ECO:0000250}.
METAL 357 357 Zinc; catalytic. {ECO:0000250}.
SITE 56 57 Cleavage. {ECO:0000305|PubMed:25795784}.
SITE 205 206 Cleavage; by furin-like protease.
{ECO:0000269|PubMed:9920899}.
CARBOHYD 144 144 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 154 154 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 231 231 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 381 381 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 487 487 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 636 636 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 322 401 {ECO:0000250}.
DISULFID 363 385 {ECO:0000250|UniProtKB:P78536}.
DISULFID 365 370 {ECO:0000250}.
DISULFID 473 493 {ECO:0000250}.
DISULFID 644 656 {ECO:0000250}.
DISULFID 650 662 {ECO:0000250}.
DISULFID 664 673 {ECO:0000250}.
MUTAGEN 53 53 R->A: Reduces the shedding activity; when
associated with A-56. Does not prevent
pro-domain processing between the
pro- and metalloprotease domain; when
associated with A-56.
{ECO:0000269|PubMed:25795784}.
MUTAGEN 56 56 R->A: Reduces the shedding activity; when
associated with A-56. Does not prevent
pro-domain processing between the
pro- and metalloprotease domain; when
associated with A-56.
{ECO:0000269|PubMed:25795784}.
MUTAGEN 202 202 R->A: Does not affect shedding activity;
when associated with A-205.
{ECO:0000269|PubMed:25795784}.
MUTAGEN 205 205 R->A: Does not affect shedding activity;
when associated with A-203.
{ECO:0000269|PubMed:25795784}.
MUTAGEN 348 348 E->A: Abolishes catalytic activity.
{ECO:0000269|PubMed:19273593}.
CONFLICT 296 296 W -> R (in Ref. 1; AAC52446, 2; BAC65470
and 4; AAH47156). {ECO:0000305}.
SEQUENCE 845 AA; 92079 MW; 38C40F89D4A77725 CRC64;
MGPRALSPLA SLRLRWLLAC GLLGPVLEAG RPDLEQTVHL SSYEIITPWR LTRERREALG
PSSQQISYVI QAQGKQHIIH LERNTDLLPN DFVVYTYDKE GSLLSDHPNV QSHCHYRGYV
EGVQNSAVAV SACFGLRGLL HLENASFGIE PLHNSSHFEH IFYPMDGIHQ EPLRCGVSNR
DTEKEGTQGD EEEHPSVTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
RLANYLDSMY IMLNIRIVLV GLEIWTDRNP INIIGGAGDV LGNFVQWREK FLITRWRHDS
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
RECFCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGS CLLNIPKPDE AYSAPSCGNK
LVDPGEECDC GTAKECEVDP CCEGSTCKLK SFAECAYGDC CKDCQFLPGG SMCRGKTSEC
DVPEYCNGSS QFCPPDVFIQ NGYPCQNSKA YCYNGMCQYY DAQCQVIFGS KAKAAPRDCF
IEVNSKGDRF GNCGFSGSEY KKCATGNALC GKLQCENVQD MPVFGIVPAI IQTPSRGTKC
WGVDFQLGSD VPDPGMVNEG TKCDAGKICR NFQCVNASVL NYDCDIQGKC HGHGVCNSNK
NCHCEDGWAP PHCDTKGYGG SVDSGPTYNA KSTALRDGLL VFFFLIVPLV AAAIFLFIKR
DELRKTFRKK RSQMSDGRNQ ANVSRQPGDP SISRPPGGPN VSRPPGGPGV SRPPGGPGVS
RPPGGPGVSR PPPGHGNRFP VPTYAAKQPA QFPSRPPPPQ PKISSQGNLI PARPAPAPPL
YSSLT


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U0766p CLIA ADAM 10,ADAM10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Mammalian disintegrin-metalloprotease,Pig,Sus scrofa 96T
E0766p ELISA ADAM 10,ADAM10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Mammalian disintegrin-metalloprotease,Pig,Sus scrofa 96T
18-661-15039 ADAM 10 - EC 3.4.24.81; A disintegrin and metalloproteinase domain 10; Mammalian disintegrin-metalloprotease; Kuzbanian protein homolog; CDw156c antigen Polyclonal 0.1 mg
U0620m CLIA ADAM 8,Adam8,Cell surface antigen MS2,Disintegrin and metalloproteinase domain-containing protein 8,Macrophage cysteine-rich glycoprotein,Mouse,Ms2,Mus musculus 96T
E0620m ELISA kit ADAM 8,Adam8,Cell surface antigen MS2,Disintegrin and metalloproteinase domain-containing protein 8,Macrophage cysteine-rich glycoprotein,Mouse,Ms2,Mus musculus 96T
E0620m ELISA ADAM 8,Adam8,Cell surface antigen MS2,Disintegrin and metalloproteinase domain-containing protein 8,Macrophage cysteine-rich glycoprotein,Mouse,Ms2,Mus musculus 96T
U0766m CLIA ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuz,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Mouse,Mus musculus 96T
E0766m ELISA kit ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuz,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Mouse,Mus musculus 96T
E0766r ELISA ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Rat,Rattus norvegicus 96T
E0766r ELISA kit ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Rat,Rattus norvegicus 96T
U0766r CLIA ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Rat,Rattus norvegicus 96T
E0766m ELISA ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuz,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Mouse,Mus musculus 96T


 

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