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Matrix metalloproteinase-16 (MMP-16) (EC 3.4.24.-) (MMP-X2) (Membrane-type matrix metalloproteinase 3) (MT-MMP 3) (MTMMP3) (Membrane-type-3 matrix metalloproteinase) (MT3-MMP) (MT3MMP)

 MMP16_HUMAN             Reviewed;         607 AA.
P51512; B2RAN7; Q14824; Q52H48;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 2.
05-DEC-2018, entry version 184.
RecName: Full=Matrix metalloproteinase-16;
Short=MMP-16;
EC=3.4.24.-;
AltName: Full=MMP-X2;
AltName: Full=Membrane-type matrix metalloproteinase 3;
Short=MT-MMP 3;
Short=MTMMP3;
AltName: Full=Membrane-type-3 matrix metalloproteinase;
Short=MT3-MMP;
Short=MT3MMP;
Flags: Precursor;
Name=MMP16 {ECO:0000312|HGNC:HGNC:7162};
Synonyms=C8orf57 {ECO:0000312|HGNC:HGNC:7162}, MMPX2;
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 LONG).
TISSUE=Placenta;
PubMed=7559440; DOI=10.1074/jbc.270.39.23013;
Takino T., Sato H., Shinagawa A., Seiki M.;
"Identification of the second membrane-type matrix metalloproteinase
(MT-MMP-2) gene from a human placenta cDNA library. MT-MMPs form a
unique membrane-type subclass in the MMP family.";
J. Biol. Chem. 270:23013-23020(1995).
[2]
SEQUENCE REVISION.
Seiki M.;
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS LONG AND SHORT).
TISSUE=Ovary;
PubMed=9396633; DOI=10.1016/S0167-4781(97)00120-6;
Matsumoto S., Katoh M., Saito S., Watanabe T., Masuho Y.;
"Identification of soluble type of membrane-type matrix
metalloproteinase-3 formed by alternatively spliced mRNA.";
Biochim. Biophys. Acta 1354:159-170(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM LONG).
TISSUE=Fetal brain;
PubMed=9092507; DOI=10.1074/jbc.272.15.9749;
Shofuda K., Yasumitsu H., Nishihashi A., Miki K., Miyazaki K.;
"Expression of three membrane-type matrix metalloproteinases (MT-MMPs)
in rat vascular smooth muscle cells and characterization of MT3-MMPs
with and without transmembrane domain.";
J. Biol. Chem. 272:9749-9754(1997).
[5]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
NIEHS SNPs program;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
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).
[7]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM LONG).
TISSUE=Brain;
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).
[9]
INTERACTION WITH CSPG4, SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=11278606; DOI=10.1074/jbc.M010053200;
Iida J., Pei D., Kang T., Simpson M.A., Herlyn M., Furcht L.T.,
McCarthy J.B.;
"Melanoma chondroitin sulfate proteoglycan regulates matrix
metalloproteinase-dependent human melanoma invasion into type I
collagen.";
J. Biol. Chem. 276:18786-18794(2001).
[10]
X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 124-292 IN COMPLEX WITH
INHIBITOR, ZINC-BINDING SITES, AND CALCIUM-BINDING SITES.
PubMed=14741217; DOI=10.1016/j.jmb.2003.12.022;
Lang R., Braun M., Sounni N.E., Noel A., Frankenne F., Foidart J.M.,
Bode W., Maskos K.;
"Crystal structure of the catalytic domain of MMP-16/MT3-MMP:
characterization of MT-MMP specific features.";
J. Mol. Biol. 336:213-225(2004).
-!- FUNCTION: Endopeptidase that degrades various components of the
extracellular matrix, such as collagen type III and fibronectin.
Activates progelatinase A. Involved in the matrix remodeling of
blood vessels. Isoform short cleaves fibronectin and also collagen
type III, but at lower rate. It has no effect on type I, II, IV
and V collagen. However, upon interaction with CSPG4, it may be
involved in degradation and invasion of type I collagen by
melanoma cells. {ECO:0000269|PubMed:11278606}.
-!- 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};
-!- ACTIVITY REGULATION: TIMP-2 shows little inhibitory activity
compared to TIMP-1. TIMP-1 seems to have less binding affinity
than TIMP-2 for the short isoform.
-!- SUBUNIT: Interacts with CSPG4 through CSPG4 chondroitin sulfate
glycosaminoglycan. {ECO:0000269|PubMed:11278606,
ECO:0000269|PubMed:14741217}.
-!- SUBCELLULAR LOCATION: Isoform Long: Cell membrane {ECO:0000305};
Single-pass type I membrane protein {ECO:0000305}; Extracellular
side {ECO:0000305}. Note=Localized at the cell surface of melanoma
cells.
-!- SUBCELLULAR LOCATION: Isoform Short: Secreted, extracellular
space, extracellular matrix. Cell surface. Note=Localized at the
cell surface of melanoma cells.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=Long;
IsoId=P51512-1; Sequence=Displayed;
Name=Short; Synonyms=SM3;
IsoId=P51512-2; Sequence=VSP_005453, VSP_005454;
-!- TISSUE SPECIFICITY: Expressed in heart, brain, placenta, ovary and
small intestine. Isoform Short is found in the ovary.
-!- DEVELOPMENTAL STAGE: Expressed in tissues undergoing
reconstruction. Present in fetal tissues, especially in brain.
Expression seems to decline with advanced development.
-!- 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}.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp16/";
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EMBL; AB009303; BAA23742.1; -; mRNA.
EMBL; D83646; BAA12022.1; -; mRNA.
EMBL; D83647; BAA12023.1; -; mRNA.
EMBL; D85511; BAA22226.1; -; mRNA.
EMBL; DQ003082; AAX84515.1; -; Genomic_DNA.
EMBL; AK314274; BAG36934.1; -; mRNA.
EMBL; CH471060; EAW91651.1; -; Genomic_DNA.
EMBL; BC069500; AAH69500.1; -; mRNA.
EMBL; BC075004; AAH75004.1; -; mRNA.
EMBL; BC075005; AAH75005.1; -; mRNA.
CCDS; CCDS6246.1; -. [P51512-1]
RefSeq; NP_005932.2; NM_005941.4. [P51512-1]
UniGene; Hs.492187; -.
UniGene; Hs.546267; -.
PDB; 1RM8; X-ray; 1.80 A; A=124-292.
PDBsum; 1RM8; -.
ProteinModelPortal; P51512; -.
SMR; P51512; -.
BioGrid; 110468; 1.
IntAct; P51512; 1.
MINT; P51512; -.
STRING; 9606.ENSP00000286614; -.
BindingDB; P51512; -.
ChEMBL; CHEMBL2200; -.
DrugBank; DB03880; Batimastat.
DrugBank; DB00786; Marimastat.
GuidetoPHARMACOLOGY; 1640; -.
MEROPS; M10.016; -.
iPTMnet; P51512; -.
PhosphoSitePlus; P51512; -.
BioMuta; MMP16; -.
DMDM; 3041669; -.
EPD; P51512; -.
PaxDb; P51512; -.
PeptideAtlas; P51512; -.
PRIDE; P51512; -.
ProteomicsDB; 56313; -.
ProteomicsDB; 56314; -. [P51512-2]
Ensembl; ENST00000286614; ENSP00000286614; ENSG00000156103. [P51512-1]
GeneID; 4325; -.
KEGG; hsa:4325; -.
UCSC; uc003yeb.5; human. [P51512-1]
CTD; 4325; -.
DisGeNET; 4325; -.
EuPathDB; HostDB:ENSG00000156103.15; -.
GeneCards; MMP16; -.
HGNC; HGNC:7162; MMP16.
HPA; HPA023693; -.
MIM; 602262; gene.
neXtProt; NX_P51512; -.
OpenTargets; ENSG00000156103; -.
PharmGKB; PA30874; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000157532; -.
HOGENOM; HOG000217928; -.
HOVERGEN; HBG052484; -.
InParanoid; P51512; -.
KO; K07996; -.
OMA; KFWVFKD; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P51512; -.
TreeFam; TF352396; -.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
ChiTaRS; MMP16; human.
EvolutionaryTrace; P51512; -.
GeneWiki; MMP16; -.
GenomeRNAi; 4325; -.
PMAP-CutDB; P51512; -.
PRO; PR:P51512; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000156103; Expressed in 167 organ(s), highest expression level in forebrain.
CleanEx; HS_MMP16; -.
ExpressionAtlas; P51512; baseline and differential.
Genevisible; P51512; HS.
GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell.
GO; GO:0031012; C:extracellular matrix; IEA:InterPro.
GO; GO:0005796; C:Golgi lumen; TAS:Reactome.
GO; GO:0005887; C:integral component of plasma membrane; IDA:ParkinsonsUK-UCL.
GO; GO:0005886; C:plasma membrane; TAS:Reactome.
GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc.
GO; GO:0070006; F:metalloaminopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; IDA:ParkinsonsUK-UCL.
GO; GO:0008270; F:zinc ion binding; IDA:ParkinsonsUK-UCL.
GO; GO:0035988; P:chondrocyte proliferation; IEA:Ensembl.
GO; GO:0030574; P:collagen catabolic process; IEA:UniProtKB-KW.
GO; GO:0097094; P:craniofacial suture morphogenesis; IEA:Ensembl.
GO; GO:0048701; P:embryonic cranial skeleton morphogenesis; IEA:Ensembl.
GO; GO:0001958; P:endochondral ossification; IEA:Ensembl.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0019538; P:protein metabolic process; TAS:ParkinsonsUK-UCL.
GO; GO:0016485; P:protein processing; IDA:ParkinsonsUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:ParkinsonsUK-UCL.
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; IPR036375; Hemopexin-like_dom_sf.
InterPro; IPR018487; Hemopexin-like_repeat.
InterPro; IPR018486; Hemopexin_CS.
InterPro; IPR033739; M10A_MMP.
InterPro; IPR024079; MetalloPept_cat_dom_sf.
InterPro; IPR028697; MMP16.
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.
InterPro; IPR036365; PGBD-like_sf.
PANTHER; PTHR10201:SF26; PTHR10201:SF26; 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.
1: Evidence at protein level;
3D-structure; Alternative splicing; Calcium; Cell membrane;
Cleavage on pair of basic residues; Collagen degradation;
Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
Hydrolase; Membrane; Metal-binding; Metalloprotease; Protease;
Reference proteome; Repeat; Secreted; Signal; Transmembrane;
Transmembrane helix; Zinc; Zymogen.
SIGNAL 1 31 {ECO:0000255}.
PROPEP 32 119 {ECO:0000250}.
/FTId=PRO_0000028812.
CHAIN 120 607 Matrix metalloproteinase-16.
/FTId=PRO_0000028813.
TOPO_DOM 120 564 Extracellular. {ECO:0000255}.
TRANSMEM 565 585 Helical. {ECO:0000255}.
TOPO_DOM 586 607 Cytoplasmic. {ECO:0000255}.
REPEAT 340 388 Hemopexin 1.
REPEAT 389 434 Hemopexin 2.
REPEAT 436 484 Hemopexin 3.
REPEAT 485 532 Hemopexin 4.
MOTIF 99 106 Cysteine switch. {ECO:0000250}.
ACT_SITE 247 247
METAL 101 101 Zinc 1; in inhibited form. {ECO:0000250}.
METAL 183 183 Calcium 1; via carbonyl oxygen.
METAL 193 193 Zinc 1.
METAL 195 195 Zinc 1.
METAL 200 200 Calcium 2.
METAL 201 201 Calcium 2; via carbonyl oxygen.
METAL 203 203 Calcium 2; via carbonyl oxygen.
METAL 205 205 Calcium 2; via carbonyl oxygen.
METAL 215 215 Calcium 1; via carbonyl oxygen.
METAL 217 217 Calcium 1; via carbonyl oxygen.
METAL 219 219 Calcium 1.
METAL 223 223 Calcium 2.
METAL 226 226 Calcium 2.
METAL 246 246 Zinc 2; catalytic.
METAL 250 250 Zinc 2; catalytic.
METAL 256 256 Zinc 2; catalytic.
CARBOHYD 83 83 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 343 532 {ECO:0000250}.
VAR_SEQ 408 457 GNKYWVFKDTTLQPGYPHDLITLGSGIPPHGIDSAIWWEDV
GKTYFFKGD -> VKGDTLSVIQDGWLYKYHWKWILEQRQS
VPVLSRQTEKHKTYEELSSITY (in isoform
Short). {ECO:0000303|PubMed:9396633}.
/FTId=VSP_005453.
VAR_SEQ 458 607 Missing (in isoform Short).
{ECO:0000303|PubMed:9396633}.
/FTId=VSP_005454.
CONFLICT 521 521 Y -> H (in Ref. 1; BAA23742).
{ECO:0000305}.
STRAND 128 136 {ECO:0000244|PDB:1RM8}.
TURN 141 143 {ECO:0000244|PDB:1RM8}.
HELIX 145 160 {ECO:0000244|PDB:1RM8}.
STRAND 166 169 {ECO:0000244|PDB:1RM8}.
STRAND 177 179 {ECO:0000244|PDB:1RM8}.
STRAND 183 191 {ECO:0000244|PDB:1RM8}.
STRAND 194 196 {ECO:0000244|PDB:1RM8}.
STRAND 201 204 {ECO:0000244|PDB:1RM8}.
STRAND 207 209 {ECO:0000244|PDB:1RM8}.
TURN 215 218 {ECO:0000244|PDB:1RM8}.
STRAND 220 223 {ECO:0000244|PDB:1RM8}.
STRAND 228 231 {ECO:0000244|PDB:1RM8}.
STRAND 234 239 {ECO:0000244|PDB:1RM8}.
HELIX 240 251 {ECO:0000244|PDB:1RM8}.
STRAND 265 267 {ECO:0000244|PDB:1RM8}.
HELIX 280 290 {ECO:0000244|PDB:1RM8}.
SEQUENCE 607 AA; 69521 MW; 30D6247D9CB21663 CRC64;
MILLTFSTGR RLDFVHHSGV FFLQTLLWIL CATVCGTEQY FNVEVWLQKY GYLPPTDPRM
SVLRSAETMQ SALAAMQQFY GINMTGKVDR NTIDWMKKPR CGVPDQTRGS SKFHIRRKRY
ALTGQKWQHK HITYSIKNVT PKVGDPETRK AIRRAFDVWQ NVTPLTFEEV PYSELENGKR
DVDITIIFAS GFHGDSSPFD GEGGFLAHAY FPGPGIGGDT HFDSDEPWTL GNPNHDGNDL
FLVAVHELGH ALGLEHSNDP TAIMAPFYQY METDNFKLPN DDLQGIQKIY GPPDKIPPPT
RPLPTVPPHR SIPPADPRKN DRPKPPRPPT GRPSYPGAKP NICDGNFNTL AILRREMFVF
KDQWFWRVRN NRVMDGYPMQ ITYFWRGLPP SIDAVYENSD GNFVFFKGNK YWVFKDTTLQ
PGYPHDLITL GSGIPPHGID SAIWWEDVGK TYFFKGDRYW RYSEEMKTMD PGYPKPITVW
KGIPESPQGA FVHKENGFTY FYKGKEYWKF NNQILKVEPG YPRSILKDFM GCDGPTDRVK
EGHSPPDDVD IVIKLDNTAS TVKAIAIVIP CILALCLLVL VYTVFQFKRK GTPRHILYCK
RSMQEWV


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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
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
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
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
E2056m ELISA 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 muscu 96T
E2056h ELISA 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
E2056Rb ELISA 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
U2056r CLIA 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
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
U2056m CLIA 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
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
U2056Rb CLIA 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
U2056r CLIA 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


 

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