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

 ADAM9_HUMAN             Reviewed;         819 AA.
Q13443; B7ZLN7; Q10718; Q8NFM6;
19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
01-NOV-1996, sequence version 1.
07-NOV-2018, entry version 190.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 9;
Short=ADAM 9;
EC=3.4.24.-;
AltName: Full=Cellular disintegrin-related protein;
AltName: Full=Meltrin-gamma;
AltName: Full=Metalloprotease/disintegrin/cysteine-rich protein 9;
AltName: Full=Myeloma cell metalloproteinase;
Flags: Precursor;
Name=ADAM9; Synonyms=KIAA0021, MCMP, MDC9, MLTNG;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
SUBCELLULAR LOCATION.
TISSUE=Mammary carcinoma;
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]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=8809033; DOI=10.1042/bj3180459;
McKie N., Dallas D.J., Edwards T., Apperley J.F., Russell R.G.G.,
Croucher P.I.;
"Cloning of a novel membrane-linked metalloproteinase from human
myeloma cells.";
Biochem. J. 318:459-462(1996).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=12054541; DOI=10.1016/S0006-291X(02)00302-9;
Hotoda N., Koike H., Sasagawa N., Ishiura S.;
"A secreted form of human ADAM9 has an alpha-secretase activity for
APP.";
Biochem. Biophys. Res. Commun. 293:800-805(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Bone marrow;
PubMed=7584026; DOI=10.1093/dnares/1.1.27;
Nomura N., Miyajima N., Sazuka T., Tanaka A., Kawarabayasi Y.,
Sato S., Nagase T., Seki N., Ishikawa K., Tabata S.;
"Prediction of the coding sequences of unidentified human genes. I.
The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by
analysis of randomly sampled cDNA clones from human immature myeloid
cell line KG-1.";
DNA Res. 1:27-35(1994).
[5]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
[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] (ISOFORM 2).
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]
TISSUE SPECIFICITY.
PubMed=9016778; DOI=10.1006/bbrc.1996.5957;
McKie N., Edwards T., Dallas D.J., Houghton A., Stringer B.,
Graham R., Russell G., Croucher P.I.;
"Expression of members of a novel membrane linked metalloproteinase
family (ADAM) in human articular chondrocytes.";
Biochem. Biophys. Res. Commun. 230:335-339(1997).
[9]
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).
[10]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
INVOLVEMENT IN CORD9.
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]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND THR-761, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and 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).
[13]
3D-STRUCTURE MODELING OF 208-404.
Manzetti S., McCulloch D.R., Herington A.C.;
"Exploring the substrate affinities of MMP-3, ADAM-9 and ADAM-10 using
molecular modelling and dynamics simulations.";
Submitted (JUN-2002) to the PDB data bank.
-!- FUNCTION: Cleaves and releases a number of molecules with
important roles in tumorigenesis and angiogenesis, such as TEK,
KDR, EPHB4, CD40, VCAM1 and CDH5. May mediate cell-cell, cell-
matrix interactions and regulate the motility of cells via
interactions with integrins. {ECO:0000250|UniProtKB:Q61072}.
-!- FUNCTION: Isoform 2: May act as alpha-secretase for amyloid
precursor protein (APP). {ECO:0000269|PubMed:12054541}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
Note=Binds 1 zinc ion per subunit. {ECO:0000305};
-!- ACTIVITY 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.
Inhibited by hydroxamic acid-based inhibitors.
{ECO:0000250|UniProtKB:Q61072}.
-!- SUBUNIT: Interacts with SH3GL2 and SNX9 through its cytoplasmic
tail (PubMed:10531379). Interacts with ITGA6.
{ECO:0000250|UniProtKB:Q61072, ECO:0000269|PubMed:10531379}.
-!- INTERACTION:
Q9UI95:MAD2L2; NbExp=3; IntAct=EBI-77903, EBI-77889;
Q9UKS6:PACSIN3; NbExp=2; IntAct=EBI-77903, EBI-77926;
Q99962:SH3GL2; NbExp=2; IntAct=EBI-77903, EBI-77938;
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane
{ECO:0000269|PubMed:8647900}; Single-pass type I membrane protein
{ECO:0000255}.
-!- SUBCELLULAR LOCATION: Isoform 2: Secreted
{ECO:0000269|PubMed:12054541}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q13443-1; Sequence=Displayed;
Name=2;
IsoId=Q13443-2; Sequence=VSP_011057, VSP_011058;
Note=May be produced at very low levels due to a premature stop
codon in the mRNA, leading to nonsense-mediated mRNA decay.;
-!- TISSUE SPECIFICITY: Widely expressed. Expressed in chondrocytes.
Isoform 2 is highly expressed in liver and heart.
{ECO:0000269|PubMed:12054541, ECO:0000269|PubMed:7584026,
ECO:0000269|PubMed:8647900, ECO:0000269|PubMed:9016778}.
-!- 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:0000250|UniProtKB:Q61072}.
-!- PTM: Phosphorylation is induced in vitro by phorbol-12-myristate-
13-acetate (PMA). {ECO:0000250|UniProtKB:Q61072}.
-!- DISEASE: Cone-rod dystrophy 9 (CORD9) [MIM:612775]: An inherited
retinal dystrophy characterized by retinal pigment deposits
visible on fundus examination, predominantly in the macular
region, and initial loss of cone photoreceptors followed by rod
degeneration. This leads to decreased visual acuity and
sensitivity in the central visual field, followed by loss of
peripheral vision. Severe loss of vision occurs earlier than in
retinitis pigmentosa, due to cone photoreceptors degenerating at a
higher rate than rod photoreceptors.
{ECO:0000269|PubMed:19409519}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- CAUTION: Has sometimes been referred to as ADAM-12. {ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/ADAM9ID573ch8p11.html";
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EMBL; U41766; AAC50403.1; -; mRNA.
EMBL; AF495383; AAM49575.1; -; mRNA.
EMBL; D14665; BAA03499.2; -; mRNA.
EMBL; CH471080; EAW63284.1; -; Genomic_DNA.
EMBL; BC143923; AAI43924.1; -; mRNA.
CCDS; CCDS6112.1; -. [Q13443-1]
PIR; JC7850; JC7850.
PIR; S71949; S71949.
RefSeq; NP_003807.1; NM_003816.2. [Q13443-1]
UniGene; Hs.591852; -.
PDB; 1M1V; Model; -; A=208-404.
PDBsum; 1M1V; -.
ProteinModelPortal; Q13443; -.
SMR; Q13443; -.
BioGrid; 114290; 28.
CORUM; Q13443; -.
IntAct; Q13443; 12.
MINT; Q13443; -.
STRING; 9606.ENSP00000419446; -.
BindingDB; Q13443; -.
ChEMBL; CHEMBL5982; -.
DrugBank; DB05033; INCB7839.
GuidetoPHARMACOLOGY; 1657; -.
MEROPS; M12.209; -.
GlyConnect; 1181; -.
iPTMnet; Q13443; -.
PhosphoSitePlus; Q13443; -.
BioMuta; ADAM9; -.
DMDM; 24211441; -.
EPD; Q13443; -.
MaxQB; Q13443; -.
PaxDb; Q13443; -.
PeptideAtlas; Q13443; -.
PRIDE; Q13443; -.
ProteomicsDB; 59440; -.
ProteomicsDB; 59441; -. [Q13443-2]
Ensembl; ENST00000379917; ENSP00000369249; ENSG00000168615. [Q13443-2]
Ensembl; ENST00000487273; ENSP00000419446; ENSG00000168615. [Q13443-1]
GeneID; 8754; -.
KEGG; hsa:8754; -.
UCSC; uc003xmr.4; human. [Q13443-1]
CTD; 8754; -.
DisGeNET; 8754; -.
EuPathDB; HostDB:ENSG00000168615.11; -.
GeneCards; ADAM9; -.
HGNC; HGNC:216; ADAM9.
HPA; HPA004000; -.
MalaCards; ADAM9; -.
MIM; 602713; gene.
MIM; 612775; phenotype.
neXtProt; NX_Q13443; -.
OpenTargets; ENSG00000168615; -.
Orphanet; 1872; Cone rod dystrophy.
PharmGKB; PA24534; -.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00910000144019; -.
HOGENOM; HOG000230883; -.
HOVERGEN; HBG006978; -.
InParanoid; Q13443; -.
KO; K06834; -.
OMA; FYRMDDV; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q13443; -.
TreeFam; TF314733; -.
BRENDA; 3.4.24.B9; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
ChiTaRS; ADAM9; human.
GeneWiki; ADAM9; -.
GenomeRNAi; 8754; -.
PRO; PR:Q13443; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000168615; Expressed in 233 organ(s), highest expression level in amniotic fluid.
CleanEx; HS_ADAM9; -.
ExpressionAtlas; Q13443; baseline and differential.
Genevisible; Q13443; HS.
GO; GO:0016323; C:basolateral plasma membrane; IEA:Ensembl.
GO; GO:0009986; C:cell surface; ISS:BHF-UCL.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005615; C:extracellular space; IDA:BHF-UCL.
GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0031233; C:intrinsic component of external side of plasma membrane; ISS:BHF-UCL.
GO; GO:0005518; F:collagen binding; IMP:BHF-UCL.
GO; GO:0005178; F:integrin binding; IDA:BHF-UCL.
GO; GO:0043236; F:laminin binding; IMP:BHF-UCL.
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; IMP:BHF-UCL.
GO; GO:0005080; F:protein kinase C binding; ISS:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0000186; P:activation of MAPKK activity; IDA:BHF-UCL.
GO; GO:0007155; P:cell adhesion; IMP:BHF-UCL.
GO; GO:0033627; P:cell adhesion mediated by integrin; IMP:BHF-UCL.
GO; GO:0016477; P:cell migration; ISS:UniProtKB.
GO; GO:0033631; P:cell-cell adhesion mediated by integrin; IEP:BHF-UCL.
GO; GO:0007160; P:cell-matrix adhesion; IMP:BHF-UCL.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IMP:BHF-UCL.
GO; GO:0007229; P:integrin-mediated signaling pathway; IC:BHF-UCL.
GO; GO:0030216; P:keratinocyte differentiation; IEP:BHF-UCL.
GO; GO:0006509; P:membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0042117; P:monocyte activation; IMP:BHF-UCL.
GO; GO:0051088; P:PMA-inducible membrane protein ectodomain proteolysis; IDA:BHF-UCL.
GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IMP:BHF-UCL.
GO; GO:0051549; P:positive regulation of keratinocyte migration; IMP:BHF-UCL.
GO; GO:0034241; P:positive regulation of macrophage fusion; IMP:BHF-UCL.
GO; GO:0051044; P:positive regulation of membrane protein ectodomain proteolysis; ISS:BHF-UCL.
GO; GO:0050714; P:positive regulation of protein secretion; IDA:BHF-UCL.
GO; GO:0097327; P:response to antineoplastic agent; IEA:Ensembl.
GO; GO:0051592; P:response to calcium ion; IMP:BHF-UCL.
GO; GO:0051384; P:response to glucocorticoid; ISS:BHF-UCL.
GO; GO:0042542; P:response to hydrogen peroxide; IMP:BHF-UCL.
GO; GO:0034616; P:response to laminar fluid shear stress; IEA:Ensembl.
GO; GO:0010042; P:response to manganese ion; IMP:BHF-UCL.
GO; GO:0034612; P:response to tumor necrosis factor; IDA:BHF-UCL.
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; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR018358; Disintegrin_CS.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
InterPro; IPR013032; EGF-like_CS.
InterPro; IPR000742; EGF-like_dom.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
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.
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;
3D-structure; Alternative splicing; Cell membrane; Complete proteome;
Cone-rod dystrophy; Disulfide bond; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc.
SIGNAL 1 28 {ECO:0000255}.
CHAIN 29 819 Disintegrin and metalloproteinase domain-
containing protein 9.
/FTId=PRO_0000029062.
TOPO_DOM 29 697 Extracellular. {ECO:0000255}.
TRANSMEM 698 718 Helical. {ECO:0000255}.
TOPO_DOM 719 819 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.
COMPBIAS 790 795 Poly-Pro.
ACT_SITE 348 348 {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:0000250|UniProtKB:Q61072}.
SITE 205 206 Cleavage; by furin-like protease.
{ECO:0000250|UniProtKB:Q61072}.
MOD_RES 758 758 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 761 761 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
CARBOHYD 125 125 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
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}.
DISULFID 322 401 {ECO:0000250}.
DISULFID 363 385 {ECO:0000250}.
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}.
VAR_SEQ 655 655 V -> K (in isoform 2).
{ECO:0000303|PubMed:12054541,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011057.
VAR_SEQ 656 819 Missing (in isoform 2).
{ECO:0000303|PubMed:12054541,
ECO:0000303|PubMed:15489334}.
/FTId=VSP_011058.
CONFLICT 1 118 Missing (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 117 117 R -> Q (in Ref. 4; BAA03499).
{ECO:0000305}.
CONFLICT 119 135 YVEGVHNSSIALSDCFG -> MWREFIIHPLLLATVLD
(in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 154 154 N -> M (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
CONFLICT 566 566 G -> GLSLKFHAPFLSTMLQEAVRQTGTYLGGSVCCMKSD
CRIVTLVK (in Ref. 2; no nucleotide
entry). {ECO:0000305}.
CONFLICT 713 735 AIFIFIKRDQLWRSYFRKKRSQT -> DYFYLHQEGSTVEK
LLQKEEITN (in Ref. 2; no nucleotide
entry). {ECO:0000305}.
CONFLICT 736 819 Missing (in Ref. 2; no nucleotide entry).
{ECO:0000305}.
SEQUENCE 819 AA; 90556 MW; BC186641833137FF CRC64;
MGSGARFPSG TLRVRWLLLL GLVGPVLGAA RPGFQQTSHL SSYEIITPWR LTRERREAPR
PYSKQVSYVI QAEGKEHIIH LERNKDLLPE DFVVYTYNKE GTLITDHPNI QNHCHYRGYV
EGVHNSSIAL SDCFGLRGLL HLENASYGIE PLQNSSHFEH IIYRMDDVYK EPLKCGVSNK
DIEKETAKDE EEEPPSMTQL LRRRRAVLPQ TRYVELFIVV DKERYDMMGR NQTAVREEMI
LLANYLDSMY IMLNIRIVLV GLEIWTNGNL INIVGGAGDV LGNFVQWREK FLITRRRHDS
AQLVLKKGFG GTAGMAFVGT VCSRSHAGGI NVFGQITVET FASIVAHELG HNLGMNHDDG
RDCSCGAKSC IMNSGASGSR NFSSCSAEDF EKLTLNKGGN CLLNIPKPDE AYSAPSCGNK
LVDAGEECDC GTPKECELDP CCEGSTCKLK SFAECAYGDC CKDCRFLPGG TLCRGKTSEC
DVPEYCNGSS QFCQPDVFIQ NGYPCQNNKA YCYNGMCQYY DAQCQVIFGS KAKAAPKDCF
IEVNSKGDRF GNCGFSGNEY KKCATGNALC GKLQCENVQE IPVFGIVPAI IQTPSRGTKC
WGVDFQLGSD VPDPGMVNEG TKCGAGKICR NFQCVDASVL NYDCDVQKKC HGHGVCNSNK
NCHCENGWAP PNCETKGYGG SVDSGPTYNE MNTALRDGLL VFFFLIVPLI VCAIFIFIKR
DQLWRSYFRK KRSQTYESDG KNQANPSRQP GSVPRHVSPV TPPREVPIYA NRFAVPTYAA
KQPQQFPSRP PPPQPKVSSQ GNLIPARPAP APPLYSSLT


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U1829h CLIA ADAM 9,ADAM9,Cellular disintegrin-related protein,Disintegrin and metalloproteinase domain-containing protein 9,Homo sapiens,Human,KIAA0021,MCMP,MDC9,Meltrin-gamma,Metalloprotease_disintegrin_cys 96T
E1829h ELISA kit ADAM 9,ADAM9,Cellular disintegrin-related protein,Disintegrin and metalloproteinase domain-containing protein 9,Homo sapiens,Human,KIAA0021,MCMP,MDC9,Meltrin-gamma,Metalloprotease_disintegr 96T
U1829h CLIA kit ADAM 9,ADAM9,Cellular disintegrin-related protein,Disintegrin and metalloproteinase domain-containing protein 9,Homo sapiens,Human,KIAA0021,MCMP,MDC9,Meltrin-gamma,Metalloprotease_disintegri 96T
E1829h ELISA ADAM 9,ADAM9,Cellular disintegrin-related protein,Disintegrin and metalloproteinase domain-containing protein 9,Homo sapiens,Human,KIAA0021,MCMP,MDC9,Meltrin-gamma,Metalloprotease_disintegrin_cy 96T
U1829m CLIA ADAM 9,Adam9,Disintegrin and metalloproteinase domain-containing protein 9,Kiaa0021,Mdc9,Meltrin-gamma,Metalloprotease_disintegrin_cysteine-rich protein 9,Mltng,Mouse,Mus musculus,Myeloma cell me 96T
E1829m ELISA ADAM 9,Adam9,Disintegrin and metalloproteinase domain-containing protein 9,Kiaa0021,Mdc9,Meltrin-gamma,Metalloprotease_disintegrin_cysteine-rich protein 9,Mltng,Mouse,Mus musculus,Myeloma cell m 96T
15-288-21429 ADAM 23 - A disintegrin and metalloproteinase domain 23; Metalloproteinase-like. disintegrin-like. and cysteine-rich protein 3; MDC-3 Polyclonal 0.05 mg
15-288-21429 ADAM 23 - A disintegrin and metalloproteinase domain 23; Metalloproteinase-like. disintegrin-like. and cysteine-rich protein 3; MDC-3 Polyclonal 0.1 mg
E1829m ELISA kit ADAM 9,Adam9,Disintegrin and metalloproteinase domain-containing protein 9,Kiaa0021,Mdc9,Meltrin-gamma,Metalloprotease_disintegrin_cysteine-rich protein 9,Mltng,Mouse,Mus musculus,Myeloma c 96T
U1829m CLIA kit ADAM 9,Adam9,Disintegrin and metalloproteinase domain-containing protein 9,Kiaa0021,Mdc9,Meltrin-gamma,Metalloprotease_disintegrin_cysteine-rich protein 9,Mltng,Mouse,Mus musculus,Myeloma ce 96T
18-272-195343 ADAM9 - Rabbit polyclonal to ADAM9; EC 3.4.24.-; A disintegrin and metalloproteinase domain 9; Metalloprotease_disintegrin_cysteine-rich protein 9; Myeloma cell metalloproteinase; Meltrin gamma; Cellu 0.05 mg
18-272-195434 ADAM15 - Rabbit polyclonal to ADAM15; EC 3.4.24.-; A disintegrin and metalloproteinase domain 15; Metalloproteinase-like. disintegrin-like. and cysteine-rich protein 15; MDC-15; Metalloprotease RGD di 0.025 mg
E0766p ELISA kit 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
U0766p CLIA ADAM 10,ADAM10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Mammalian disintegrin-metalloprotease,Pig,Sus scrofa 96T
E0766r ELISA 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
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 kit ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Rat,Rattus norvegicus 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
U0766r CLIA ADAM 10,Adam10,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,Madm,Mammalian disintegrin-metalloprotease,Rat,Rattus norvegicus 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
U0766h CLIA ADAM 10,ADAM10,CDw156,Disintegrin and metalloproteinase domain-containing protein 10,Homo sapiens,Human,KUZ,Kuzbanian protein homolog,MADM,Mammalian disintegrin-metalloprotease 96T
E0766b ELISA kit ADAM 10,ADAM10,Bos taurus,Bovine,Disintegrin and metalloproteinase domain-containing protein 10,Kuzbanian protein homolog,MADM,Mammalian disintegrin-metalloprotease,Myelin-associated metall 96T
E0766h ELISA kit ADAM 10,ADAM10,CDw156,Disintegrin and metalloproteinase domain-containing protein 10,Homo sapiens,Human,KUZ,Kuzbanian protein homolog,MADM,Mammalian disintegrin-metalloprotease 96T


 

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