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Matrix metalloproteinase-14 (MMP-14) (EC 3.4.24.80) (MMP-X1) (MT-MMP) (Membrane-type matrix metalloproteinase 1) (MT-MMP 1) (MTMMP1) (Membrane-type-1 matrix metalloproteinase) (MT1-MMP) (MT1MMP)

 MMP14_MOUSE             Reviewed;         582 AA.
P53690; O08645; O35369; Q8BTX2;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
27-SEP-2017, entry version 166.
RecName: Full=Matrix metalloproteinase-14;
Short=MMP-14;
EC=3.4.24.80;
AltName: Full=MMP-X1;
AltName: Full=MT-MMP;
AltName: Full=Membrane-type matrix metalloproteinase 1;
Short=MT-MMP 1;
Short=MTMMP1;
AltName: Full=Membrane-type-1 matrix metalloproteinase;
Short=MT1-MMP;
Short=MT1MMP;
Flags: Precursor;
Name=Mmp14; Synonyms=Mtmmp;
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].
PubMed=7708715; DOI=10.1073/pnas.92.7.2730;
Okada A., Bellocq J.-P., Rouyer N., Chenard M.P., Rio M.C.,
Chambon P., Basset P.;
"Membrane-type matrix metalloproteinase (MT-MMP) gene is expressed in
stromal cells of human colon, breast, and head and neck carcinomas.";
Proc. Natl. Acad. Sci. U.S.A. 92:2730-2734(1995).
[2]
SEQUENCE REVISION.
Odaka A.;
Submitted (DEC-1999) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=129/Sv;
PubMed=9325265; DOI=10.1074/jbc.272.41.25511;
Apte S.S., Fukai N., Beier D.R., Olsen B.R.;
"The matrix metalloproteinase-14 (MMP-14) gene is structurally
distinct from other MMP genes and is co-expressed with the TIMP-2 gene
during mouse embryogenesis.";
J. Biol. Chem. 272:25511-25517(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=CD-1; TISSUE=Kidney;
PubMed=9648071;
Ota K., Stetler-Stevenson W.G., Yang Q., Kumar A., Wada J.,
Kashihara N., Wallner E.I., Kanwar Y.S.;
"Cloning of murine membrane-type-1-matrix metalloproteinase (MT-1-MMP)
and its metanephric developmental regulation with respect to MMP-2 and
its inhibitor.";
Kidney Int. 54:131-142(1998).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
STRAIN=FVB/N;
PubMed=16778201; DOI=10.1158/0008-5472.CAN-06-0539;
Rozanov D.V., Savinov A.Y., Golubkov V.S., Tomlinson S.,
Strongin A.Y.;
"Interference with the complement system by tumor cell membrane type-1
matrix metalloproteinase plays a significant role in promoting
metastasis in mice.";
Cancer Res. 66:6258-6263(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J, and NOD;
TISSUE=Bone marrow, Eye, Spinal cord, and Thymus;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
FUNCTION.
PubMed=10520996; DOI=10.1016/S0092-8674(00)80064-1;
Holmbeck K., Bianco P., Caterina J., Yamada S., Kromer M.,
Kuznetsov S.A., Mankani M., Robey P.G., Poole A.R., Pidoux I.,
Ward J.M., Birkedal-Hansen H.;
"MT1-MMP-deficient mice develop dwarfism, osteopenia, arthritis, and
connective tissue disease due to inadequate collagen turnover.";
Cell 99:81-92(1999).
-!- FUNCTION: Endopeptidase that degrades various components of the
extracellular matrix, such as collagen. Activates progelatinase A.
Essential for pericellular collagenolysis and modeling of skeletal
and extraskeletal connective tissues during development. May be
involved in actin cytoskeleton reorganization by cleaving PTK7 (By
similarity). Acts as a positive regulator of cell growth and
migration via activation of MMP15. Involved in the formation of
the fibrovascular tissues (By similarity). {ECO:0000250,
ECO:0000269|PubMed:10520996}.
-!- CATALYTIC ACTIVITY: Endopeptidase activity. Activates
progelatinase A by cleavage of the propeptide at 37-Asn-|-Leu-38.
Other bonds hydrolyzed include 35-Gly-|-Ile-36 in the propeptide
of collagenase 3, and 341-Asn-|-Phe-342, 441-Asp-|-Leu-442 and
354-Gln-|-Thr-355 in the aggrecan interglobular domain.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
Note=Binds 1 zinc ion per subunit. {ECO:0000250};
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
-!- SUBUNIT: Interacts (via C-terminal cytoplasmic tail) with BST2.
Interacts with DLL1; inhibits DLL1-induced Notch signaling.
{ECO:0000250|UniProtKB:P50281}.
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}; Extracellular side {ECO:0000305}.
Melanosome {ECO:0000250}. Cytoplasm {ECO:0000250}. Note=Forms a
complex with BST2 and localizes to the cytoplasm. {ECO:0000250}.
-!- TISSUE SPECIFICITY: Highly expressed in placenta, kidney, heart,
lung, embryonic skeletal and periskeletal tissues.
-!- DEVELOPMENTAL STAGE: Not detected before day 10.5. At day 12.5,
prominently expressed in large arteries and the umbilical
arteries, expressed at lower levels in the myocardium,
craniofacial mesenchyme, nasal epithelium and liver capsule. At
days 14.5 and 17.5, expressed in the musculoskeletal system, and
ossification areas, with continued expression in the arterial
tunica media.
-!- 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: Tyrosine phosphorylated by PKDCC/VLK.
{ECO:0000250|UniProtKB:P50281}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
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EMBL; X83536; CAA58520.2; -; mRNA.
EMBL; AF022432; AAB86602.1; -; Genomic_DNA.
EMBL; AF022424; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022425; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022426; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022427; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022428; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022429; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022430; AAB86602.1; JOINED; Genomic_DNA.
EMBL; AF022431; AAB86602.1; JOINED; Genomic_DNA.
EMBL; U54984; AAB51753.1; -; mRNA.
EMBL; DQ249870; ABB45784.1; -; mRNA.
EMBL; AK088476; BAC40377.1; -; mRNA.
EMBL; AK138611; BAE23719.1; -; mRNA.
EMBL; AK149907; BAE29158.1; -; mRNA.
EMBL; AK149988; BAE29216.1; -; mRNA.
EMBL; AK165014; BAE38000.1; -; mRNA.
EMBL; CH466535; EDL36348.1; -; Genomic_DNA.
CCDS; CCDS36922.1; -.
PIR; I48673; I48673.
RefSeq; NP_032634.3; NM_008608.4.
UniGene; Mm.280175; -.
UniGene; Mm.486486; -.
ProteinModelPortal; P53690; -.
SMR; P53690; -.
IntAct; P53690; 1.
STRING; 10090.ENSMUSP00000087119; -.
MEROPS; M10.014; -.
iPTMnet; P53690; -.
PhosphoSitePlus; P53690; -.
SwissPalm; P53690; -.
MaxQB; P53690; -.
PaxDb; P53690; -.
PeptideAtlas; P53690; -.
PRIDE; P53690; -.
Ensembl; ENSMUST00000089688; ENSMUSP00000087119; ENSMUSG00000000957.
GeneID; 17387; -.
KEGG; mmu:17387; -.
UCSC; uc007twc.2; mouse.
CTD; 4323; -.
MGI; MGI:101900; Mmp14.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00760000118870; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; P53690; -.
KO; K07763; -.
OMA; VMFPWYQ; -.
OrthoDB; EOG091G03DP; -.
TreeFam; TF352396; -.
Reactome; R-MMU-1442490; Collagen degradation.
Reactome; R-MMU-1474228; Degradation of the extracellular matrix.
Reactome; R-MMU-1592389; Activation of Matrix Metalloproteinases.
ChiTaRS; Mmp14; mouse.
PRO; PR:P53690; -.
Proteomes; UP000000589; Chromosome 14.
Bgee; ENSMUSG00000000957; -.
CleanEx; MM_MMP14; -.
ExpressionAtlas; P53690; baseline and differential.
Genevisible; P53690; MM.
GO; GO:0031410; C:cytoplasmic vesicle; ISO:MGI.
GO; GO:0005829; C:cytosol; ISO:MGI.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0005925; C:focal adhesion; ISO:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0045111; C:intermediate filament cytoskeleton; ISO:MGI.
GO; GO:0044354; C:macropinosome; ISO:MGI.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISO:MGI.
GO; GO:0005178; F:integrin binding; IEA:Ensembl.
GO; GO:0070006; F:metalloaminopeptidase activity; ISO:MGI.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:UniProtKB.
GO; GO:0016504; F:peptidase activator activity; IEA:Ensembl.
GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
GO; GO:0001525; P:angiogenesis; IEA:Ensembl.
GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
GO; GO:0060348; P:bone development; IGI:MGI.
GO; GO:0048754; P:branching morphogenesis of an epithelial tube; IMP:MGI.
GO; GO:0016477; P:cell migration; IMP:MGI.
GO; GO:0035988; P:chondrocyte proliferation; IGI:MGI.
GO; GO:0030574; P:collagen catabolic process; IGI:MGI.
GO; GO:0097094; P:craniofacial suture morphogenesis; IGI:MGI.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IGI:MGI.
GO; GO:0001958; P:endochondral ossification; IGI:MGI.
GO; GO:0035987; P:endodermal cell differentiation; IEA:Ensembl.
GO; GO:0001935; P:endothelial cell proliferation; IEA:Ensembl.
GO; GO:0030324; P:lung development; IMP:MGI.
GO; GO:0008584; P:male gonad development; IEA:Ensembl.
GO; GO:0051895; P:negative regulation of focal adhesion assembly; IEA:Ensembl.
GO; GO:0045746; P:negative regulation of Notch signaling pathway; IMP:UniProtKB.
GO; GO:0001503; P:ossification; IGI:MGI.
GO; GO:0001541; P:ovarian follicle development; IEA:Ensembl.
GO; GO:0045579; P:positive regulation of B cell differentiation; IMP:UniProtKB.
GO; GO:0030307; P:positive regulation of cell growth; ISO:MGI.
GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
GO; GO:1905523; P:positive regulation of macrophage migration; IMP:BHF-UCL.
GO; GO:0010831; P:positive regulation of myotube differentiation; IMP:UniProtKB.
GO; GO:0006508; P:proteolysis; ISO:MGI.
GO; GO:0043627; P:response to estrogen; IEA:Ensembl.
GO; GO:0009725; P:response to hormone; IEA:Ensembl.
GO; GO:0001666; P:response to hypoxia; IEA:Ensembl.
GO; GO:0009612; P:response to mechanical stimulus; IEA:Ensembl.
GO; GO:1990834; P:response to odorant; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0006979; P:response to oxidative stress; IEA:Ensembl.
GO; GO:0048771; P:tissue remodeling; IEA:Ensembl.
GO; GO:0031638; P:zymogen activation; IMP:MGI.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 1.
InterPro; IPR000585; Hemopexin-like_dom.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom.
InterPro; IPR028693; MMP14.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021805; Pept_M10A_metallopeptidase_C.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
PANTHER; PTHR10201:SF184; PTHR10201:SF184; 1.
Pfam; PF11857; DUF3377; 1.
Pfam; PF00045; Hemopexin; 4.
Pfam; PF00413; Peptidase_M10; 1.
Pfam; PF01471; PG_binding_1; 1.
PIRSF; PIRSF001191; Peptidase_M10A_matrix; 1.
PRINTS; PR00138; MATRIXIN.
SMART; SM00120; HX; 4.
SMART; SM00235; ZnMc; 1.
SUPFAM; SSF47090; SSF47090; 1.
SUPFAM; SSF50923; SSF50923; 1.
PROSITE; PS00546; CYSTEINE_SWITCH; 1.
PROSITE; PS00024; HEMOPEXIN; 1.
PROSITE; PS51642; HEMOPEXIN_2; 4.
PROSITE; PS00142; ZINC_PROTEASE; 1.
2: Evidence at transcript level;
Calcium; Cleavage on pair of basic residues; Collagen degradation;
Complete proteome; Cytoplasm; Disulfide bond; Hydrolase; Membrane;
Metal-binding; Metalloprotease; Phosphoprotein; Protease;
Reference proteome; Repeat; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000255}.
PROPEP 21 111 {ECO:0000250}.
/FTId=PRO_0000028800.
CHAIN 112 582 Matrix metalloproteinase-14.
/FTId=PRO_0000028801.
TOPO_DOM 112 541 Extracellular. {ECO:0000255}.
TRANSMEM 542 562 Helical. {ECO:0000255}.
TOPO_DOM 563 582 Cytoplasmic. {ECO:0000255}.
REPEAT 316 364 Hemopexin 1.
REPEAT 365 410 Hemopexin 2.
REPEAT 412 460 Hemopexin 3.
REPEAT 461 508 Hemopexin 4.
MOTIF 91 98 Cysteine switch. {ECO:0000250}.
ACT_SITE 240 240 {ECO:0000255|PROSITE-ProRule:PRU10095}.
METAL 93 93 Zinc; in inhibited form. {ECO:0000250}.
METAL 239 239 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 243 243 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
METAL 249 249 Zinc; catalytic. {ECO:0000255|PROSITE-
ProRule:PRU10095}.
MOD_RES 399 399 Phosphotyrosine; by PKDCC.
{ECO:0000250|UniProtKB:P50281}.
DISULFID 319 508 {ECO:0000250}.
CONFLICT 133 133 P -> S (in Ref. 3; AAB86602).
{ECO:0000305}.
CONFLICT 255 255 A -> D (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 258 258 A -> S (in Ref. 1; CAA58520 and 4;
AAB51753). {ECO:0000305}.
CONFLICT 341 341 F -> L (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 346 346 N -> P (in Ref. 3; AAB86602).
{ECO:0000305}.
CONFLICT 378 378 K -> T (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 390 391 FD -> CV (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 400 401 PK -> AN (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 407 407 G -> V (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 412 412 T -> S (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 417 417 A -> T (in Ref. 1; CAA58520).
{ECO:0000305}.
CONFLICT 512 512 G -> R (in Ref. 4; AAB51753).
{ECO:0000305}.
SEQUENCE 582 AA; 65919 MW; 6CA95CFD5811B093 CRC64;
MSPAPRPSRS LLLPLLTLGT ALASLGWAQG SNFSPEAWLQ QYGYLPPGDL RTHTQRSPQS
LSAAIAAMQK FYGLQVTGKA DLATMMAMRR PRCGVPDKFG TEIKANVRRK RYAIQGLKWQ
HNEITFCIQN YTPKVGEYAT FEAIRKAFRV WESATPLRFR EVPYAYIREG HEKQADIMIL
FAEGFHGDST PFDGEGGFLA HAYFPGPNIG GDTHFDSAEP WTVQNEDLNG NDIFLVAVHE
LGHALGLEHS NDPSAIMAPF YQWMDTENFV LPDDDRRGIQ QLYGSKSGSP TKMPPQPRTT
SRPSVPDKPK NPAYGPNICD GNFDTVAMLR GEMFVFKERW FWRVRNNQVM DGYPMPIGQF
WRGLPASINT AYERKDGKFV FFKGDKHWVF DEASLEPGYP KHIKELGRGL PTDKIDAALF
WMPNGKTYFF RGNKYYRFNE EFRAVDSEYP KNIKVWEGIP ESPRGSFMGS DEVFTYFYKG
NKYWKFNNQK LKVEPGYPKS ALRDWMGCPS GGRPDEGTEE ETEVIIIEVD EEGSGAVSAA
AVVLPVLLLL LVLAVGLAVF FFRRHGTPKR LLYCQRSLLD KV


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U2056h CLIA kit Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
U2056m CLIA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus muscul 96T
U2056h CLIA Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056Rb ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Oryctolagus cuniculus,Rabbit 96T
E2056r ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Rat,Rattus norvegicus 96T
E2056m ELISA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,Mmp14,MMP-14,MMP-X1,Mouse,MT1MMP,MT1-MMP,Mtmmp,MT-MMP,MT-MMP 1,MTMMP1,Mus musculus 96T
E2056h ELISA Homo sapiens,Human,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MMP-X1,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056b ELISA Bos taurus,Bovine,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
U2056b CLIA Bos taurus,Bovine,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056b ELISA kit Bos taurus,Bovine,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
U2056b CLIA kit Bos taurus,Bovine,Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1 96T
E2056p ELISA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Pig,Sus scrofa 96T
U2056p CLIA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Pig,Sus scrofa 96T
E2056p ELISA Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Pig,Sus scrofa 96T
U2056p CLIA kit Matrix metalloproteinase-14,Membrane-type matrix metalloproteinase 1,Membrane-type-1 matrix metalloproteinase,MMP14,MMP-14,MT1MMP,MT1-MMP,MT-MMP 1,MTMMP1,Pig,Sus scrofa 96T
15-288-21125 Matrix metalloproteinase-14 - EC 3.4.24.80; MMP-14; Membrane-type matrix metalloproteinase 1; MT-MMP 1; MTMMP1; Membrane-type-1 matrix metalloproteinase; MT1-MMP; MT1MMP; MMP-X1 Polyclonal 0.05 mg


 

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