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Disintegrin and metalloproteinase domain-containing protein 15 (ADAM 15) (EC 3.4.24.-) (Metalloprotease RGD disintegrin protein) (Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15) (MDC-15) (Metargidin)

 ADA15_HUMAN             Reviewed;         863 AA.
Q13444; B3KQU5; B4DLB5; B4DMH8; E9PN65; Q13493; Q53XQ0; Q5SR68;
Q5SR69; Q6R267; Q71S61; Q71S62; Q71S63; Q71S64; Q71S65; Q71S66;
Q71S67; Q71S68; Q71S69; Q96C78; U3KQL5;
01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
13-JUL-2010, sequence version 4.
25-OCT-2017, entry version 190.
RecName: Full=Disintegrin and metalloproteinase domain-containing protein 15;
Short=ADAM 15;
EC=3.4.24.-;
AltName: Full=Metalloprotease RGD disintegrin protein;
AltName: Full=Metalloproteinase-like, disintegrin-like, and cysteine-rich protein 15;
Short=MDC-15;
AltName: Full=Metargidin;
Flags: Precursor;
Name=ADAM15; Synonyms=MDC15;
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 2), AND VARIANT THR-191.
TISSUE=Mammary carcinoma;
PubMed=8617717; DOI=10.1074/jbc.271.9.4593;
Kraetzschmar J., Lum L., Blobel C.P.;
"Metargidin, a membrane-anchored metalloprotease-disintegrin protein
with an RGD integrin binding sequence.";
J. Biol. Chem. 271:4593-4596(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT THR-191.
TISSUE=Umbilical vein;
PubMed=9039960;
Herren B., Raines E.W., Ross R.;
"Expression of a disintegrin-like protein in cultured human vascular
cells and in vivo.";
FASEB J. 11:173-180(1997).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 10), FUNCTION, TISSUE SPECIFICITY,
AND ALTERNATIVE SPLICING (ISOFORM 2).
PubMed=15358598; DOI=10.1152/ajpgi.00262.2004;
Charrier L., Yan Y., Driss A., Laboisse C.L., Sitaraman S.V.,
Merlin D.;
"ADAM-15 inhibits wound healing in human intestinal epithelial cell
monolayers.";
Am. J. Physiol. 288:G346-G353(2005).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1;
2; 3; 4; 5; 6; 7; 8; 9; 10), AND VARIANT THR-191.
PubMed=17937806; DOI=10.1186/1471-2199-8-90;
Kleino I., Ortiz R.M., Huovila A.P.;
"ADAM15 gene structure and differential alternative exon use in human
tissues.";
BMC Mol. Biol. 8:90-90(2007).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 4 AND 10), ALTERNATIVE
SPLICING, AND INTERACTION WITH GRB2; MAPK1; MAPK3; NCK1; PTK6;
SH3PXD2A AND SRC.
PubMed=18296648; DOI=10.1158/1541-7786.MCR-07-2028;
Zhong J.L., Poghosyan Z., Pennington C.J., Scott X., Handsley M.M.,
Warn A., Gavrilovic J., Honert K., Kruger A., Span P.N., Sweep F.C.,
Edwards D.R.;
"Distinct functions of natural ADAM-15 cytoplasmic domain variants in
human mammary carcinoma.";
Mol. Cancer Res. 6:383-394(2008).
[6]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5; 6; 7; 8 AND 9),
AND VARIANT THR-191.
Karkkainen I., Ortiz R.M., Huovila A.-P.J.;
"Characterization of human ADAM15 gene and promoter, and evidence for
alternative exon use.";
Submitted (FEB-2004) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
THR-191.
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 (AUG-2003) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 12 AND 13), AND
VARIANTS THR-191 AND LYS-216.
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).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 11).
TISSUE=Embryo;
PubMed=16303743; DOI=10.1093/dnares/12.2.117;
Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
Isogai T.;
"Signal sequence and keyword trap in silico for selection of full-
length human cDNAs encoding secretion or membrane proteins from oligo-
capped cDNA libraries.";
DNA Res. 12:117-126(2005).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT
THR-191.
TISSUE=Kidney;
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).
[12]
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).
[13]
INTERACTION WITH INTEGRIN ALPHAV-BETA3.
PubMed=9516430; DOI=10.1074/jbc.273.13.7345;
Zhang X.P., Kamata T., Yokoyama K., Puzon-McLaughlin W., Takada Y.;
"Specific interaction of the recombinant disintegrin-like domain of
MDC-15 (metargidin, ADAM-15) with integrin alphavbeta3.";
J. Biol. Chem. 273:7345-7350(1998).
[14]
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).
[15]
INTERACTION WITH INTEGRIN ALPHAV-BETA3 AND INTEGRIN ALPHA5-BETA1.
PubMed=9914169;
Nath D., Slocombe P.M., Stephens P.E., Warn A., Hutchinson G.R.,
Yamada K.M., Docherty A.J., Murphy G.;
"Interaction of metargidin (ADAM-15) with alphavbeta3 and alpha5beta1
integrins on different haemopoietic cells.";
J. Cell Sci. 112:579-587(1999).
[16]
SUBCELLULAR LOCATION.
PubMed=12243749; DOI=10.1006/excr.2002.5606;
Ham C., Levkau B., Raines E.W., Herren B.;
"ADAM15 is an adherens junction molecule whose surface expression can
be driven by VE-cadherin.";
Exp. Cell Res. 279:239-247(2002).
[17]
PHOSPHORYLATION AT TYR-715 AND TYR-735, AND INTERACTION WITH GRB2; LCK
AND HCK.
PubMed=11741929; DOI=10.1074/jbc.M107430200;
Poghosyan Z., Robbins S.M., Houslay M.D., Webster A., Murphy G.,
Edwards D.R.;
"Phosphorylation-dependent interactions between ADAM15 cytoplasmic
domain and Src family protein-tyrosine kinases.";
J. Biol. Chem. 277:4999-5007(2002).
[18]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=12091380; DOI=10.1074/jbc.M200988200;
Martin J., Eynstone L.V., Davies M., Williams J.D., Steadman R.;
"The role of ADAM 15 in glomerular mesangial cell migration.";
J. Biol. Chem. 277:33683-33689(2002).
[19]
INTERACTION WITH SH3PXD2A.
PubMed=12615925; DOI=10.1074/jbc.M300267200;
Abram C.L., Seals D.F., Pass I., Salinsky D., Maurer L., Roth T.M.,
Courtneidge S.A.;
"The adaptor protein fish associates with members of the ADAMs family
and localizes to podosomes of Src-transformed cells.";
J. Biol. Chem. 278:16844-16851(2003).
[20]
FUNCTION.
PubMed=15818704; DOI=10.1002/art.20974;
Bohm B.B., Aigner T., Roy B., Brodie T.A., Blobel C.P., Burkhardt H.;
"Homeostatic effects of the metalloproteinase disintegrin ADAM15 in
degenerative cartilage remodeling.";
Arthritis Rheum. 52:1100-1109(2005).
[21]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=17575078; DOI=10.1165/rcmb.2006-0364OC;
Lu D., Xie S., Sukkar M.B., Lu X., Scully M.F., Chung K.F.;
"Inhibition of airway smooth muscle adhesion and migration by the
disintegrin domain of ADAM-15.";
Am. J. Respir. Cell Mol. Biol. 37:494-500(2007).
[22]
FUNCTION, AND MUTAGENESIS OF 484-ARG-GLY-485.
PubMed=17416588; DOI=10.1074/jbc.M700158200;
Charrier L., Yan Y., Nguyen H.T., Dalmasso G., Laboisse C.L.,
Gewirtz A.T., Sitaraman S.V., Merlin D.;
"ADAM-15/metargidin mediates homotypic aggregation of human T
lymphocytes and heterotypic interactions of T lymphocytes with
intestinal epithelial cells.";
J. Biol. Chem. 282:16948-16958(2007).
[23]
FUNCTION.
PubMed=18387333; DOI=10.1016/j.biocel.2008.02.021;
Chen Q., Meng L.H., Zhu C.H., Lin L.P., Lu H., Ding J.;
"ADAM15 suppresses cell motility by driving integrin alpha5beta1 cell
surface expression via Erk inactivation.";
Int. J. Biochem. Cell Biol. 40:2164-2173(2008).
[24]
FUNCTION.
PubMed=18434311; DOI=10.1074/jbc.M801329200;
Najy A.J., Day K.C., Day M.L.;
"The ectodomain shedding of E-cadherin by ADAM15 supports ErbB
receptor activation.";
J. Biol. Chem. 283:18393-18401(2008).
[25]
ENZYME REGULATION.
PubMed=19207106; DOI=10.1042/BJ20082127;
Maretzky T., Yang G., Ouerfelli O., Overall C.M., Worpenberg S.,
Hassiepen U., Eder J., Blobel C.P.;
"Characterization of the catalytic activity of the membrane-anchored
metalloproteinase ADAM15 in cell-based assays.";
Biochem. J. 420:105-113(2009).
[26]
INTERACTION WITH HCK; ITSN1; ITSN2; LYN; NCF1; NEPHROCYSTIN; SH3PXD2A;
SNX33; SNX9 AND SRC.
PubMed=19718658; DOI=10.1002/jcb.22317;
Kleino I., Ortiz R.M., Yritys M., Huovila A.P., Saksela K.;
"Alternative splicing of ADAM15 regulates its interactions with
cellular SH3 proteins.";
J. Cell. Biochem. 108:877-885(2009).
-!- FUNCTION: Active metalloproteinase with gelatinolytic and
collagenolytic activity. Plays a role in the wound healing
process. Mediates both heterotypic intraepithelial cell/T-cell
interactions and homotypic T-cell aggregation. Inhibits beta-1
integrin-mediated cell adhesion and migration of airway smooth
muscle cells. Suppresses cell motility on or towards fibronectin
possibly by driving alpha-v/beta-1 integrin (ITAGV-ITGB1) cell
surface expression via ERK1/2 inactivation. Cleaves E-cadherin in
response to growth factor deprivation. Plays a role in glomerular
cell migration. Plays a role in pathological neovascularization.
May play a role in cartilage remodeling. May be proteolytically
processed, during sperm epididymal maturation and the acrosome
reaction. May play a role in sperm-egg binding through its
disintegrin domain. {ECO:0000269|PubMed:12091380,
ECO:0000269|PubMed:15358598, ECO:0000269|PubMed:15818704,
ECO:0000269|PubMed:17416588, ECO:0000269|PubMed:17575078,
ECO:0000269|PubMed:18387333, ECO:0000269|PubMed:18434311}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- ENZYME REGULATION: Inhibited by hydroxamate-type metalloproteinase
inhibitors such as marimastat. Inhibited by metalloproteinase
inhibitor 2 (TIMP-2) and TIMP-3 at nanomolar concentrations. Not
significantly inhibited by TIMP-1 at concentrations of up to 100
nM. Not activated by PMA or ionomycin.
{ECO:0000269|PubMed:19207106}.
-!- SUBUNIT: Interacts with ITAGV-ITGB3 (vitronectin receptor).
Interacts with SH3GL2 and SNX9; this interaction occurs
preferentially with ADAM15 precursor, rather than the processed
form, suggesting it occurs in a secretory pathway compartment
prior to the medial Golgi. Interacts with ITAG9-ITGB1 (By
similarity). Interacts specifically with Src family protein-
tyrosine kinases (PTKs). Interacts with SH3PXD2A. Interacts with
ITAGV-ITGB1. Interacts with GRB2, HCK, ITSN1, ITSN2, LYN, MAPK1,
MAPK3, NCF1, NCK1, nephrocystin, PTK6, SNX33, LCK and SRC.
{ECO:0000250, ECO:0000269|PubMed:10531379,
ECO:0000269|PubMed:11741929, ECO:0000269|PubMed:12615925,
ECO:0000269|PubMed:18296648, ECO:0000269|PubMed:19718658,
ECO:0000269|PubMed:9516430, ECO:0000269|PubMed:9914169}.
-!- INTERACTION:
Q8N9N5:BANP; NbExp=3; IntAct=EBI-77818, EBI-744695;
Q13643:FHL3; NbExp=3; IntAct=EBI-77818, EBI-741101;
P06241:FYN; NbExp=2; IntAct=EBI-77818, EBI-515315;
P62993:GRB2; NbExp=3; IntAct=EBI-77818, EBI-401755;
P08631:HCK; NbExp=3; IntAct=EBI-77818, EBI-346340;
P06239:LCK; NbExp=3; IntAct=EBI-77818, EBI-1348;
O15259:NPHP1; NbExp=2; IntAct=EBI-77818, EBI-953828;
P37198:NUP62; NbExp=3; IntAct=EBI-77818, EBI-347978;
Q9UKS6:PACSIN3; NbExp=3; IntAct=EBI-77818, EBI-77926;
Q93062:RBPMS; NbExp=3; IntAct=EBI-77818, EBI-740322;
Q99962:SH3GL2; NbExp=2; IntAct=EBI-77818, EBI-77938;
Q5TCZ1:SH3PXD2A; NbExp=2; IntAct=EBI-77818, EBI-2483234;
Q8WV41:SNX33; NbExp=2; IntAct=EBI-77818, EBI-2481535;
Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-77818, EBI-77848;
Q02446:SP4; NbExp=3; IntAct=EBI-77818, EBI-10198587;
P12931:SRC; NbExp=3; IntAct=EBI-77818, EBI-621482;
-!- SUBCELLULAR LOCATION: Endomembrane system
{ECO:0000269|PubMed:12243749}; Single-pass type I membrane protein
{ECO:0000269|PubMed:12243749}. Cell junction, adherens junction
{ECO:0000269|PubMed:12243749}. Cell projection, cilium, flagellum
{ECO:0000250}. Cytoplasmic vesicle, secretory vesicle, acrosome
{ECO:0000250}. Note=The majority of the protein is localized in a
perinuclear compartment which may correspond to the trans-Golgi
network or the late endosome. The pro-protein is the major
detectable form on the cell surface, whereas the majority of the
protein in the cell is processed (By similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=13;
Name=1; Synonyms=6b;
IsoId=Q13444-1; Sequence=Displayed;
Name=2;
IsoId=Q13444-2; Sequence=VSP_039527;
Name=3; Synonyms=6a;
IsoId=Q13444-3; Sequence=VSP_039529;
Name=4; Synonyms=4a;
IsoId=Q13444-4; Sequence=VSP_039531;
Name=5;
IsoId=Q13444-5; Sequence=VSP_039528;
Name=6; Synonyms=7b;
IsoId=Q13444-6; Sequence=VSP_039533;
Name=7; Synonyms=7a;
IsoId=Q13444-7; Sequence=VSP_039529, VSP_039533;
Name=8;
IsoId=Q13444-8; Sequence=VSP_039528, VSP_039533;
Name=9; Synonyms=3a;
IsoId=Q13444-9; Sequence=VSP_039526, VSP_039532;
Name=10; Synonyms=1;
IsoId=Q13444-10; Sequence=VSP_039525, VSP_039530;
Name=11;
IsoId=Q13444-11; Sequence=VSP_039524, VSP_039527;
Name=12;
IsoId=Q13444-12; Sequence=VSP_044695, VSP_039527;
Note=No experimental confirmation available.;
Name=13;
IsoId=Q13444-13; Sequence=VSP_055143, VSP_055144, VSP_055145;
Note=No experimental confirmation available.;
-!- TISSUE SPECIFICITY: Expressed in colon and small intestine.
Expressed in airway smooth muscle and glomerular mesangial cells
(at protein level). Ubiquitously expressed. Overexpressed in
atherosclerotic lesions. Constitutively expressed in cultured
endothelium and smooth muscle. Expressed in chondrocytes.
Expressed in airway smooth muscle and glomerular mesangial cells.
{ECO:0000269|PubMed:12091380, ECO:0000269|PubMed:15358598,
ECO:0000269|PubMed:17575078, ECO:0000269|PubMed:9016778}.
-!- DOMAIN: The cytoplasmic domain is required for SH3GL2- and SNX9-
binding.
-!- DOMAIN: Disintegrin domain binds to integrin alphaV-beta3.
-!- DOMAIN: The conserved cysteine present in the cysteine-switch
motif binds the catalytic zinc ion, thus inhibiting the enzyme.
The dissociation of the cysteine from the zinc ion upon the
activation-peptide release activates the enzyme.
-!- PTM: The precursor is cleaved by a furin endopeptidase.
{ECO:0000250}.
-!- PTM: Phosphorylation increases association with PTKs.
{ECO:0000269|PubMed:11741929}.
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EMBL; U41767; AAC50404.1; -; mRNA.
EMBL; U46005; AAC51112.1; -; mRNA.
EMBL; AY518542; AAR99331.1; -; mRNA.
EMBL; AF314227; AAM44189.1; -; Genomic_DNA.
EMBL; AF314227; AAS48590.1; -; Genomic_DNA.
EMBL; AF314227; AAS48591.1; -; Genomic_DNA.
EMBL; AF314227; AAS48592.1; -; Genomic_DNA.
EMBL; AF314227; AAS48593.1; -; Genomic_DNA.
EMBL; AF314227; AAS48594.1; -; Genomic_DNA.
EMBL; AF314227; AAS48595.1; -; Genomic_DNA.
EMBL; AF314227; AAS48596.1; -; Genomic_DNA.
EMBL; AF314227; AAS48597.1; -; Genomic_DNA.
EMBL; AF314227; AAS72298.1; -; Genomic_DNA.
EMBL; AY560593; AAS72991.1; -; mRNA.
EMBL; AY560594; AAS72992.1; -; mRNA.
EMBL; AY560595; AAS72993.1; -; mRNA.
EMBL; AY560596; AAS72994.1; -; mRNA.
EMBL; AY560597; AAS72995.1; -; mRNA.
EMBL; AY560598; AAS72996.1; -; mRNA.
EMBL; AY560599; AAS72997.1; -; mRNA.
EMBL; AY560600; AAS72998.1; -; mRNA.
EMBL; AY560601; AAS72999.1; -; mRNA.
EMBL; AY576417; AAS73000.1; -; mRNA.
EMBL; BT009764; AAP88766.1; -; mRNA.
EMBL; AK296925; BAG59477.1; -; mRNA.
EMBL; AK297468; BAG59890.1; -; mRNA.
EMBL; AK075498; BAG52157.1; -; mRNA.
EMBL; AL451085; CAI13273.1; -; Genomic_DNA.
EMBL; AL691442; CAI13273.1; JOINED; Genomic_DNA.
EMBL; AL451085; CAI13274.1; -; Genomic_DNA.
EMBL; AL691442; CAI13274.1; JOINED; Genomic_DNA.
EMBL; AL691442; CAI15327.1; -; Genomic_DNA.
EMBL; AL451085; CAI15327.1; JOINED; Genomic_DNA.
EMBL; AL691442; CAI15328.1; -; Genomic_DNA.
EMBL; AL451085; CAI15328.1; JOINED; Genomic_DNA.
EMBL; BC014566; AAH14566.1; -; mRNA.
CCDS; CCDS1084.1; -. [Q13444-2]
CCDS; CCDS1085.1; -. [Q13444-4]
CCDS; CCDS1086.1; -. [Q13444-5]
CCDS; CCDS1087.1; -. [Q13444-1]
CCDS; CCDS1088.1; -. [Q13444-10]
CCDS; CCDS44236.1; -. [Q13444-3]
CCDS; CCDS58031.1; -. [Q13444-12]
CCDS; CCDS58032.1; -. [Q13444-9]
CCDS; CCDS60282.1; -. [Q13444-13]
PIR; G02390; G02390.
RefSeq; NP_001248393.1; NM_001261464.1. [Q13444-12]
RefSeq; NP_001248394.1; NM_001261465.1. [Q13444-9]
RefSeq; NP_001248395.1; NM_001261466.1. [Q13444-13]
RefSeq; NP_003806.3; NM_003815.4. [Q13444-2]
RefSeq; NP_997074.1; NM_207191.2. [Q13444-10]
RefSeq; NP_997077.1; NM_207194.2. [Q13444-4]
RefSeq; NP_997078.1; NM_207195.2. [Q13444-5]
RefSeq; NP_997079.1; NM_207196.2. [Q13444-3]
RefSeq; NP_997080.1; NM_207197.2. [Q13444-1]
UniGene; Hs.312098; -.
ProteinModelPortal; Q13444; -.
SMR; Q13444; -.
BioGrid; 114287; 33.
CORUM; Q13444; -.
ELM; Q13444; -.
IntAct; Q13444; 38.
MINT; MINT-108799; -.
STRING; 9606.ENSP00000349436; -.
ChEMBL; CHEMBL2331050; -.
MEROPS; M12.215; -.
iPTMnet; Q13444; -.
PhosphoSitePlus; Q13444; -.
BioMuta; ADAM15; -.
DMDM; 300669614; -.
EPD; Q13444; -.
MaxQB; Q13444; -.
PaxDb; Q13444; -.
PeptideAtlas; Q13444; -.
PRIDE; Q13444; -.
DNASU; 8751; -.
Ensembl; ENST00000271836; ENSP00000271836; ENSG00000143537. [Q13444-2]
Ensembl; ENST00000355956; ENSP00000348227; ENSG00000143537. [Q13444-4]
Ensembl; ENST00000356955; ENSP00000349436; ENSG00000143537. [Q13444-1]
Ensembl; ENST00000359280; ENSP00000352226; ENSG00000143537. [Q13444-5]
Ensembl; ENST00000360674; ENSP00000353892; ENSG00000143537. [Q13444-10]
Ensembl; ENST00000368412; ENSP00000357397; ENSG00000143537. [Q13444-9]
Ensembl; ENST00000368413; ENSP00000357398; ENSG00000143537. [Q13444-11]
Ensembl; ENST00000447332; ENSP00000476000; ENSG00000143537. [Q13444-13]
Ensembl; ENST00000449910; ENSP00000403843; ENSG00000143537. [Q13444-3]
Ensembl; ENST00000526491; ENSP00000432347; ENSG00000143537. [Q13444-6]
Ensembl; ENST00000529473; ENSP00000434227; ENSG00000143537. [Q13444-8]
Ensembl; ENST00000531455; ENSP00000432927; ENSG00000143537. [Q13444-12]
GeneID; 8751; -.
KEGG; hsa:8751; -.
UCSC; uc001fgr.3; human. [Q13444-1]
CTD; 8751; -.
DisGeNET; 8751; -.
EuPathDB; HostDB:ENSG00000143537.13; -.
GeneCards; ADAM15; -.
HGNC; HGNC:193; ADAM15.
HPA; HPA011633; -.
HPA; HPA072878; -.
MIM; 605548; gene.
neXtProt; NX_Q13444; -.
OpenTargets; ENSG00000143537; -.
PharmGKB; PA24510; -.
eggNOG; KOG3607; Eukaryota.
eggNOG; ENOG410XX2M; LUCA.
GeneTree; ENSGT00760000118888; -.
HOGENOM; HOG000230884; -.
HOVERGEN; HBG006978; -.
InParanoid; Q13444; -.
KO; K06836; -.
OMA; HGVCDSN; -.
OrthoDB; EOG091G01NX; -.
PhylomeDB; Q13444; -.
TreeFam; TF314733; -.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-8941237; Invadopodia formation.
SIGNOR; Q13444; -.
GeneWiki; ADAM15; -.
GenomeRNAi; 8751; -.
PRO; PR:Q13444; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000143537; -.
CleanEx; HS_ADAM15; -.
Genevisible; Q13444; HS.
GO; GO:0001669; C:acrosomal vesicle; IEA:UniProtKB-SubCell.
GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0005178; F:integrin binding; IMP:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0008237; F:metallopeptidase activity; IDA:BHF-UCL.
GO; GO:0017124; F:SH3 domain binding; IPI:BHF-UCL.
GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
GO; GO:0060317; P:cardiac epithelial to mesenchymal transition; IEA:Ensembl.
GO; GO:0007160; P:cell-matrix adhesion; TAS:ProtInc.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0030198; P:extracellular matrix organization; TAS:Reactome.
GO; GO:0045087; P:innate immune response; IDA:UniProtKB.
GO; GO:0007229; P:integrin-mediated signaling pathway; IMP:UniProtKB.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0030308; P:negative regulation of cell growth; IMP:UniProtKB.
GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
GO; GO:0001953; P:negative regulation of cell-matrix adhesion; IMP:UniProtKB.
GO; GO:1900121; P:negative regulation of receptor binding; IMP:UniProtKB.
GO; GO:0070528; P:protein kinase C signaling; IDA:UniProtKB.
GO; GO:0042246; P:tissue regeneration; IEA:Ensembl.
CDD; cd04269; ZnMc_adamalysin_II_like; 1.
Gene3D; 3.40.390.10; -; 1.
Gene3D; 4.10.70.10; -; 1.
InterPro; IPR033605; ADAM15.
InterPro; IPR006586; ADAM_Cys-rich.
InterPro; IPR001762; Disintegrin_dom.
InterPro; IPR036436; Disintegrin_dom_sf.
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.
PANTHER; PTHR11905:SF130; PTHR11905:SF130; 1.
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; PS50214; DISINTEGRIN_2; 1.
PROSITE; PS01186; EGF_2; 1.
PROSITE; PS50026; EGF_3; 1.
PROSITE; PS00142; ZINC_PROTEASE; 1.
1: Evidence at protein level;
Alternative splicing; Angiogenesis; Cell adhesion; Cell junction;
Cell projection; Cleavage on pair of basic residues;
Collagen degradation; Complete proteome; Cytoplasmic vesicle;
Disulfide bond; EGF-like domain; Glycoprotein; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Polymorphism;
Protease; Reference proteome; SH3-binding; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 17 {ECO:0000255}.
PROPEP 18 206 {ECO:0000250}.
/FTId=PRO_0000029082.
CHAIN 207 863 Disintegrin and metalloproteinase domain-
containing protein 15.
/FTId=PRO_0000029083.
TOPO_DOM 207 696 Extracellular. {ECO:0000255}.
TRANSMEM 697 717 Helical. {ECO:0000255}.
TOPO_DOM 718 863 Cytoplasmic. {ECO:0000255}.
DOMAIN 213 414 Peptidase M12B. {ECO:0000255|PROSITE-
ProRule:PRU00276}.
DOMAIN 421 508 Disintegrin. {ECO:0000255|PROSITE-
ProRule:PRU00068}.
DOMAIN 657 685 EGF-like. {ECO:0000255|PROSITE-
ProRule:PRU00076}.
MOTIF 177 184 Cysteine switch. {ECO:0000250}.
MOTIF 484 486 Cell attachment site.
{ECO:0000255|PROSITE-ProRule:PRU00068}.
MOTIF 815 821 SH3-binding. {ECO:0000255}.
MOTIF 850 856 SH3-binding. {ECO:0000255}.
COMPBIAS 509 656 Cys-rich.
ACT_SITE 349 349 {ECO:0000255|PROSITE-ProRule:PRU00276,
ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 179 179 Zinc; in inhibited form. {ECO:0000250}.
METAL 348 348 Zinc; catalytic. {ECO:0000250}.
METAL 352 352 Zinc; catalytic. {ECO:0000250}.
METAL 358 358 Zinc; catalytic. {ECO:0000250}.
MOD_RES 715 715 Phosphotyrosine; by HCK and LCK.
{ECO:0000269|PubMed:11741929}.
MOD_RES 735 735 Phosphotyrosine; by HCK and LCK.
{ECO:0000269|PubMed:11741929}.
CARBOHYD 237 237 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 389 389 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 392 392 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 606 606 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 611 611 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 323 409 {ECO:0000250}.
DISULFID 365 393 {ECO:0000250}.
DISULFID 367 376 {ECO:0000250}.
DISULFID 480 500 {ECO:0000250}.
DISULFID 657 667 {ECO:0000250}.
DISULFID 661 673 {ECO:0000250}.
DISULFID 675 684 {ECO:0000250}.
VAR_SEQ 26 26 I -> IVLSWGVLGPA (in isoform 12).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_044695.
VAR_SEQ 27 87 GGTEEQQAESEKAPREPLEPQVLQDDLPISLKKVLQTSLPE
PLRIKLELDGDSHILELLQN -> VSACNVEAPQVALRSSR
QSQRRPRGSPWSPRSFRTISQLASKRCF (in isoform
13). {ECO:0000303|PubMed:14702039}.
/FTId=VSP_055143.
VAR_SEQ 94 387 Missing (in isoform 11).
{ECO:0000303|PubMed:16303743}.
/FTId=VSP_039524.
VAR_SEQ 641 649 CIDHRCQRV -> SSLGGQDQV (in isoform 13).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055144.
VAR_SEQ 650 863 Missing (in isoform 13).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_055145.
VAR_SEQ 736 772 RAAQSGPSERPGPPQRALLARGTKQASALSFPAPPSR ->
SLRGQPSPHPQGSHCLPTPRAGAHRVTCPAQGLESRP (in
isoform 10).
{ECO:0000303|PubMed:15358598,
ECO:0000303|PubMed:18296648,
ECO:0000303|Ref.6}.
/FTId=VSP_039525.
VAR_SEQ 737 796 AAQSGPSERPGPPQRALLARGTKQASALSFPAPPSRPLPPD
PVSKRLQAELADRPNPPTR -> LVLSASRPPLPGRCRLTL
CPRDSSLRGQPSPHPQGSHCLPTPRAGAHRVTCPAQGLESR
P (in isoform 9). {ECO:0000303|Ref.6}.
/FTId=VSP_039526.
VAR_SEQ 760 808 Missing (in isoform 2, isoform 11 and
isoform 12).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16303743,
ECO:0000303|PubMed:18296648,
ECO:0000303|PubMed:8617717,
ECO:0000303|PubMed:9039960,
ECO:0000303|Ref.6, ECO:0000303|Ref.7}.
/FTId=VSP_039527.
VAR_SEQ 760 784 Missing (in isoform 5 and isoform 8).
{ECO:0000303|Ref.6}.
/FTId=VSP_039528.
VAR_SEQ 760 760 Missing (in isoform 3 and isoform 7).
{ECO:0000303|Ref.6}.
/FTId=VSP_039529.
VAR_SEQ 773 863 Missing (in isoform 10).
{ECO:0000303|PubMed:15358598,
ECO:0000303|PubMed:18296648,
ECO:0000303|Ref.6}.
/FTId=VSP_039530.
VAR_SEQ 785 808 Missing (in isoform 4).
{ECO:0000303|PubMed:18296648,
ECO:0000303|Ref.6}.
/FTId=VSP_039531.
VAR_SEQ 797 863 Missing (in isoform 9).
{ECO:0000303|Ref.6}.
/FTId=VSP_039532.
VAR_SEQ 809 863 SQGPAKPPPPRKPLPADPQGRCPSGDLPGPGAGIPPLVVPS
RPAPPPPTVSSLYL -> VTVGGEKGTASPPT (in
isoform 6, isoform 7 and isoform 8).
{ECO:0000303|Ref.6}.
/FTId=VSP_039533.
VARIANT 191 191 K -> T (in dbSNP:rs6427128).
{ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:17937806,
ECO:0000269|PubMed:8617717,
ECO:0000269|PubMed:9039960,
ECO:0000269|Ref.6, ECO:0000269|Ref.7}.
/FTId=VAR_060315.
VARIANT 216 216 E -> K (in dbSNP:rs115753757).
{ECO:0000269|PubMed:14702039}.
/FTId=VAR_068970.
VARIANT 294 294 P -> H (in dbSNP:rs2306122).
/FTId=VAR_060316.
MUTAGEN 484 485 RG->SV: Reduces ADAM15-mediated T-cell
aggregation.
{ECO:0000269|PubMed:17416588}.
CONFLICT 81 81 I -> V (in Ref. 9; BAG52157).
{ECO:0000305}.
CONFLICT 104 104 G -> C (in Ref. 8; BAG59890).
{ECO:0000305}.
CONFLICT 191 191 K -> T (in Ref. 8; BAG59890).
{ECO:0000305}.
CONFLICT 286 286 H -> Y (in Ref. 8; BAG59477).
{ECO:0000305}.
CONFLICT 649 649 V -> A (in Ref. 9; BAG52157).
{ECO:0000305}.
CONFLICT 714 714 S -> G (in Ref. 2; AAC50404).
{ECO:0000305}.
CONFLICT 840 840 A -> P (in Ref. 1; AAC51112).
{ECO:0000305}.
SEQUENCE 863 AA; 92959 MW; 004936E9182629CA CRC64;
MRLALLWALG LLGAGSPLPS WPLPNIGGTE EQQAESEKAP REPLEPQVLQ DDLPISLKKV
LQTSLPEPLR IKLELDGDSH ILELLQNREL VPGRPTLVWY QPDGTRVVSE GHTLENCCYQ
GRVRGYAGSW VSICTCSGLR GLVVLTPERS YTLEQGPGDL QGPPIISRIQ DLHLPGHTCA
LSWRESVHTQ KPPEHPLGQR HIRRRRDVVT ETKTVELVIV ADHSEAQKYR DFQHLLNRTL
EVALLLDTFF RPLNVRVALV GLEAWTQRDL VEISPNPAVT LENFLHWRRA HLLPRLPHDS
AQLVTGTSFS GPTVGMAIQN SICSPDFSGG VNMDHSTSIL GVASSIAHEL GHSLGLDHDL
PGNSCPCPGP APAKTCIMEA STDFLPGLNF SNCSRRALEK ALLDGMGSCL FERLPSLPPM
AAFCGNMFVE PGEQCDCGFL DDCVDPCCDS LTCQLRPGAQ CASDGPCCQN CQLRPSGWQC
RPTRGDCDLP EFCPGDSSQC PPDVSLGDGE PCAGGQAVCM HGRCASYAQQ CQSLWGPGAQ
PAAPLCLQTA NTRGNAFGSC GRNPSGSYVS CTPRDAICGQ LQCQTGRTQP LLGSIRDLLW
ETIDVNGTEL NCSWVHLDLG SDVAQPLLTL PGTACGPGLV CIDHRCQRVD LLGAQECRSK
CHGHGVCDSN RHCYCEEGWA PPDCTTQLKA TSSLTTGLLL SLLVLLVLVM LGASYWYRAR
LHQRLCQLKG PTCQYRAAQS GPSERPGPPQ RALLARGTKQ ASALSFPAPP SRPLPPDPVS
KRLQAELADR PNPPTRPLPA DPVVRSPKSQ GPAKPPPPRK PLPADPQGRC PSGDLPGPGA
GIPPLVVPSR PAPPPPTVSS LYL


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