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Neutrophil collagenase (EC 3.4.24.34) (Matrix metalloproteinase-8) (MMP-8) (PMNL collagenase) (PMNL-CL)

 MMP8_HUMAN              Reviewed;         467 AA.
P22894; Q45F99;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
05-DEC-2018, entry version 191.
RecName: Full=Neutrophil collagenase;
EC=3.4.24.34;
AltName: Full=Matrix metalloproteinase-8;
Short=MMP-8;
AltName: Full=PMNL collagenase;
Short=PMNL-CL;
Flags: Precursor;
Name=MMP8; Synonyms=CLG1;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 314-337; 347-363
AND 424-441.
TISSUE=Neutrophil;
PubMed=2164002;
Hasty K.A., Pourmotabbed T.F., Goldberg G.I., Thompson J.P.,
Spinella D.G., Stevens R.M., Mainardi C.L.;
"Human neutrophil collagenase. A distinct gene product with homology
to other matrix metalloproteinases.";
J. Biol. Chem. 265:11421-11424(1990).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS CYS-3; ILE-32; GLU-87;
GLU-154; VAL-193; TYR-246; ALA-436 AND THR-460.
NIEHS SNPs program;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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).
[4]
PROTEIN SEQUENCE OF 21-140, AND VARIANT ILE-32.
TISSUE=Neutrophil;
PubMed=2159879; DOI=10.1111/j.1432-1033.1990.tb15489.x;
Knaeuper V., Kraemer S., Reinke H., Tschesche H.;
"Characterization and activation of procollagenase from human
polymorphonuclear leucocytes. N-terminal sequence determination of the
proenzyme and various proteolytically activated forms.";
Eur. J. Biochem. 189:295-300(1990).
[5]
PROTEIN SEQUENCE OF 21-103.
TISSUE=Neutrophil;
PubMed=1662606; DOI=10.1111/j.1432-1033.1991.tb16494.x;
Blaeser J., Knaeuper V., Osthues A., Reinke H., Tschesche H.;
"Mercurial activation of human polymorphonuclear leucocyte
procollagenase.";
Eur. J. Biochem. 202:1223-1230(1991).
[6]
PROTEIN SEQUENCE OF 85-120, AND CHARACTERIZATION.
TISSUE=Neutrophil;
PubMed=2176876; DOI=10.1021/bi00499a008;
Mallya S.K., Mookthiar K.A., Gao Y., Brew K., Dioszegi M.,
Birkedal-Hansen H., van Wart H.E.;
"Characterization of 58-kilodalton human neutrophil collagenase:
comparison with human fibroblast collagenase.";
Biochemistry 29:10628-10634(1990).
[7]
PARTIAL PROTEIN SEQUENCE.
PubMed=2169256;
Knaeuper V., Kraemer S., Reinke H., Tschesche H.;
"Partial amino acid sequence of human PMN leukocyte procollagenase.";
Biol. Chem. Hoppe-Seyler 371:295-304(1990).
[8]
ERRATUM.
PubMed=2169766;
Knaeuper V., Kraemer S., Reinke H., Tschesche H.;
Biol. Chem. Hoppe-Seyler 371:733-733(1990).
[9]
CYSTEINE-SWITCH MECHANISM.
TISSUE=Neutrophil;
PubMed=1330697; DOI=10.1016/0014-5793(92)81184-N;
Blaeser J., Triebel S., Reinke H., Tschesche H.;
"Formation of a covalent Hg-Cys-bond during mercurial activation of
PMNL procollagenase gives evidence of a cysteine-switch mechanism.";
FEBS Lett. 313:59-61(1992).
[10]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 100-262.
PubMed=8137810;
Bode W., Reinemer P., Huber R., Klein T., Schnierer S., Tschesche H.;
"The X-ray crystal structure of the catalytic domain of human
neutrophil collagenase inhibited by a substrate analogue reveals the
essentials for catalysis and specificity.";
EMBO J. 13:1263-1269(1994).
[11]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 100-262.
PubMed=8307185; DOI=10.1016/0014-5793(94)80370-6;
Reinemer P., Grams F., Huber R., Kleine T., Schnierer S., Piper M.,
Tschesche H., Bode W.;
"Structural implications for the role of the N-terminus in the
'superactivation' of collagenases. A crystallographic study.";
FEBS Lett. 338:227-233(1994).
[12]
X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 100-262.
PubMed=7656015; DOI=10.1038/nsb0294-119;
Stams T., Spurlino J.C., Smith D.L., Wahl R.C., Ho T.F.,
Qoronfleh M.W., Banks T.M., Rubin B.;
"Structure of human neutrophil collagenase reveals large S1'
specificity pocket.";
Nat. Struct. Biol. 1:119-123(1994).
[13]
X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 100-262.
PubMed=9249047; DOI=10.1111/j.1432-1033.1997.00356.x;
Betz M., Huxley P., Davies S.J., Mushtaq Y., Pieper M., Tschesche H.,
Bode W., Gomis-Rueth F.-X.;
"1.8-A crystal structure of the catalytic domain of human neutrophil
collagenase (matrix metalloproteinase-8) complexed with a
peptidomimetic hydroxamate primed-side inhibitor with a distinct
selectivity profile.";
Eur. J. Biochem. 247:356-363(1997).
[14]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 105-262.
PubMed=9655333; DOI=10.1002/pro.5560070605;
Brandstetter H., Engh R.A., von Roedern E.G., Moroder L., Huber R.,
Bode W., Grams F.;
"Structure of malonic acid-based inhibitors bound to human neutrophil
collagenase. A new binding mode explains apparently anomalous data.";
Protein Sci. 7:1303-1309(1998).
-!- FUNCTION: Can degrade fibrillar type I, II, and III collagens.
-!- CATALYTIC ACTIVITY:
Reaction=Cleavage of interstitial collagens in the triple helical
domain. Unlike EC 3.4.24.7, this enzyme cleaves type III
collagen more slowly than type I.; EC=3.4.24.34;
-!- COFACTOR:
Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
Note=Binds 3 Ca(2+) ions per subunit.;
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Note=Binds 2 Zn(2+) ions per subunit.;
-!- ACTIVITY REGULATION: Cannot be activated without removal of the
activation peptide.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule. Secreted, extracellular
space, extracellular matrix {ECO:0000305}. Note=Stored in
intracellular granules.
-!- TISSUE SPECIFICITY: Neutrophils.
-!- 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.
-!- SIMILARITY: Belongs to the peptidase M10A family. {ECO:0000305}.
-!- WEB RESOURCE: Name=NIEHS-SNPs;
URL="http://egp.gs.washington.edu/data/mmp8/";
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EMBL; J05556; AAA88021.1; -; mRNA.
EMBL; DQ141306; AAZ38714.1; -; Genomic_DNA.
EMBL; BC074988; AAH74988.1; -; mRNA.
EMBL; BC074989; AAH74989.1; -; mRNA.
CCDS; CCDS8320.1; -.
PIR; A37073; KCHUN.
RefSeq; NP_001291370.1; NM_001304441.1.
RefSeq; NP_001291371.1; NM_001304442.1.
RefSeq; NP_002415.1; NM_002424.2.
UniGene; Hs.161839; -.
PDB; 1A85; X-ray; 2.00 A; A=105-262.
PDB; 1A86; X-ray; 2.00 A; A=105-262.
PDB; 1BZS; X-ray; 1.70 A; A=99-262.
PDB; 1I73; X-ray; 1.40 A; A=100-262.
PDB; 1I76; X-ray; 1.20 A; A=100-262.
PDB; 1JAN; X-ray; 2.50 A; A=99-262.
PDB; 1JAO; X-ray; 2.40 A; A=100-262.
PDB; 1JAP; X-ray; 1.82 A; A=100-262.
PDB; 1JAQ; X-ray; 2.40 A; A=100-262.
PDB; 1JH1; X-ray; 2.70 A; A=105-262.
PDB; 1JJ9; X-ray; 2.00 A; A=100-262.
PDB; 1KBC; X-ray; 1.80 A; A/B=99-262.
PDB; 1MMB; X-ray; 2.10 A; A=100-262.
PDB; 1MNC; X-ray; 2.10 A; A=101-263.
PDB; 1ZP5; X-ray; 1.80 A; A=100-262.
PDB; 1ZS0; X-ray; 1.56 A; A=100-262.
PDB; 1ZVX; X-ray; 1.87 A; A=100-262.
PDB; 2OY2; X-ray; 1.50 A; A/F=105-262.
PDB; 2OY4; X-ray; 1.70 A; A/F=105-262.
PDB; 3DNG; X-ray; 2.00 A; A/B=100-262.
PDB; 3DPE; X-ray; 1.60 A; A=100-262.
PDB; 3DPF; X-ray; 2.10 A; A/B=100-262.
PDB; 3TT4; X-ray; 1.88 A; A=104-262.
PDB; 4QKZ; X-ray; 1.20 A; A=100-262.
PDB; 5H8X; X-ray; 1.30 A; A=100-262.
PDBsum; 1A85; -.
PDBsum; 1A86; -.
PDBsum; 1BZS; -.
PDBsum; 1I73; -.
PDBsum; 1I76; -.
PDBsum; 1JAN; -.
PDBsum; 1JAO; -.
PDBsum; 1JAP; -.
PDBsum; 1JAQ; -.
PDBsum; 1JH1; -.
PDBsum; 1JJ9; -.
PDBsum; 1KBC; -.
PDBsum; 1MMB; -.
PDBsum; 1MNC; -.
PDBsum; 1ZP5; -.
PDBsum; 1ZS0; -.
PDBsum; 1ZVX; -.
PDBsum; 2OY2; -.
PDBsum; 2OY4; -.
PDBsum; 3DNG; -.
PDBsum; 3DPE; -.
PDBsum; 3DPF; -.
PDBsum; 3TT4; -.
PDBsum; 4QKZ; -.
PDBsum; 5H8X; -.
ProteinModelPortal; P22894; -.
SMR; P22894; -.
BioGrid; 110460; 2.
STRING; 9606.ENSP00000236826; -.
BindingDB; P22894; -.
ChEMBL; CHEMBL4588; -.
DrugBank; DB02326; 1-Hydroxyamine-2-Isobutylmalonic Acid.
DrugBank; DB02953; 2-Thiomethyl-3-Phenylpropanoic Acid.
DrugBank; DB08476; 3-AMINO-AZACYCLOTRIDECAN-2-ONE.
DrugBank; DB07900; 3-FORMYL-2-HYDROXY-5-METHYL-HEXANOIC ACID HYDROXYAMIDE.
DrugBank; DB03880; Batimastat.
DrugBank; DB03636; Glycinamid.
DrugBank; DB00786; Marimastat.
DrugBank; DB08403; METHYLAMINO-PHENYLALANYL-LEUCYL-HYDROXAMIC ACID.
GuidetoPHARMACOLOGY; 1632; -.
MEROPS; M10.002; -.
iPTMnet; P22894; -.
PhosphoSitePlus; P22894; -.
BioMuta; MMP8; -.
DMDM; 116862; -.
PaxDb; P22894; -.
PeptideAtlas; P22894; -.
PRIDE; P22894; -.
ProteomicsDB; 54047; -.
TopDownProteomics; P22894; -.
Ensembl; ENST00000236826; ENSP00000236826; ENSG00000118113.
GeneID; 4317; -.
KEGG; hsa:4317; -.
UCSC; uc001phe.2; human.
CTD; 4317; -.
DisGeNET; 4317; -.
EuPathDB; HostDB:ENSG00000118113.11; -.
GeneCards; MMP8; -.
HGNC; HGNC:7175; MMP8.
HPA; HPA021221; -.
HPA; HPA022935; -.
MalaCards; MMP8; -.
MIM; 120355; gene.
neXtProt; NX_P22894; -.
OpenTargets; ENSG00000118113; -.
PharmGKB; PA30888; -.
eggNOG; KOG1565; Eukaryota.
eggNOG; ENOG410XQ5D; LUCA.
GeneTree; ENSGT00940000161871; -.
HOGENOM; HOG000217927; -.
HOVERGEN; HBG052484; -.
InParanoid; P22894; -.
KO; K01402; -.
OMA; EETWTKT; -.
OrthoDB; EOG091G03DP; -.
PhylomeDB; P22894; -.
TreeFam; TF315428; -.
BRENDA; 3.4.24.34; 2681.
Reactome; R-HSA-1442490; Collagen degradation.
Reactome; R-HSA-1474228; Degradation of the extracellular matrix.
Reactome; R-HSA-1592389; Activation of Matrix Metalloproteinases.
Reactome; R-HSA-6798695; Neutrophil degranulation.
EvolutionaryTrace; P22894; -.
GeneWiki; MMP8; -.
GenomeRNAi; 4317; -.
PMAP-CutDB; P22894; -.
PRO; PR:P22894; -.
Proteomes; UP000005640; Chromosome 11.
Bgee; ENSG00000118113; Expressed in 79 organ(s), highest expression level in bone marrow.
CleanEx; HS_MMP8; -.
ExpressionAtlas; P22894; baseline and differential.
Genevisible; P22894; HS.
GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0035580; C:specific granule lumen; TAS:Reactome.
GO; GO:1904724; C:tertiary granule lumen; TAS:Reactome.
GO; GO:0004175; F:endopeptidase activity; IMP:ARUK-UCL.
GO; GO:0004222; F:metalloendopeptidase activity; TAS:Reactome.
GO; GO:0004252; F:serine-type endopeptidase activity; IDA:UniProtKB.
GO; GO:0008270; F:zinc ion binding; TAS:UniProtKB.
GO; GO:0030574; P:collagen catabolic process; TAS:Reactome.
GO; GO:0035987; P:endodermal cell differentiation; IEP:UniProtKB.
GO; GO:0022617; P:extracellular matrix disassembly; TAS:Reactome.
GO; GO:0010629; P:negative regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0032693; P:negative regulation of interleukin-10 production; ISS:ARUK-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0043388; P:positive regulation of DNA binding; ISS:ARUK-UCL.
GO; GO:0010628; P:positive regulation of gene expression; ISS:ARUK-UCL.
GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:ARUK-UCL.
GO; GO:0046330; P:positive regulation of JNK cascade; ISS:ARUK-UCL.
GO; GO:0043410; P:positive regulation of MAPK cascade; ISS:ARUK-UCL.
GO; GO:1903980; P:positive regulation of microglial cell activation; ISS:ARUK-UCL.
GO; GO:0150078; P:positive regulation of neuroinflammatory response; ISS:ARUK-UCL.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; ISS:ARUK-UCL.
GO; GO:0045429; P:positive regulation of nitric oxide biosynthetic process; ISS:ARUK-UCL.
GO; GO:1903428; P:positive regulation of reactive oxygen species biosynthetic process; ISS:ARUK-UCL.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; ISS:ARUK-UCL.
GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
GO; GO:1903978; P:regulation of microglial cell activation; TAS:ARUK-UCL.
GO; GO:0150077; P:regulation of neuroinflammatory response; TAS:ARUK-UCL.
CDD; cd00094; HX; 1.
CDD; cd04278; ZnMc_MMP; 1.
Gene3D; 1.10.101.10; -; 1.
Gene3D; 2.110.10.10; -; 1.
Gene3D; 3.40.390.10; -; 2.
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; IPR028709; MMP8.
InterPro; IPR001818; Pept_M10_metallopeptidase.
InterPro; IPR021190; Pept_M10A.
InterPro; IPR021158; Pept_M10A_Zn_BS.
InterPro; IPR006026; Peptidase_Metallo.
InterPro; IPR002477; Peptidoglycan-bd-like.
InterPro; IPR036365; PGBD-like_sf.
InterPro; IPR036366; PGBDSf.
PANTHER; PTHR10201:SF137; PTHR10201:SF137; 1.
Pfam; PF00045; Hemopexin; 3.
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; Calcium; Collagen degradation; Complete proteome;
Direct protein sequencing; Disulfide bond; Extracellular matrix;
Glycoprotein; Hydrolase; Metal-binding; Metalloprotease; Polymorphism;
Protease; Reference proteome; Repeat; Secreted; Signal; Zinc; Zymogen.
SIGNAL 1 20 {ECO:0000269|PubMed:1662606,
ECO:0000269|PubMed:2159879}.
PROPEP 21 100 Activation peptide.
/FTId=PRO_0000028744.
CHAIN 101 467 Neutrophil collagenase.
/FTId=PRO_0000028745.
REPEAT 276 325 Hemopexin 1.
REPEAT 326 372 Hemopexin 2.
REPEAT 374 420 Hemopexin 3.
REPEAT 421 464 Hemopexin 4.
MOTIF 89 96 Cysteine switch. {ECO:0000250}.
ACT_SITE 218 218
METAL 91 91 Zinc 2; in inhibited form.
METAL 157 157 Calcium 1.
METAL 167 167 Zinc 1. {ECO:0000269|PubMed:8137810}.
METAL 169 169 Zinc 1. {ECO:0000269|PubMed:8137810}.
METAL 174 174 Calcium 2. {ECO:0000269|PubMed:8137810}.
METAL 175 175 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:8137810}.
METAL 177 177 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:8137810}.
METAL 179 179 Calcium 2; via carbonyl oxygen.
{ECO:0000269|PubMed:8137810}.
METAL 182 182 Zinc 1. {ECO:0000269|PubMed:8137810}.
METAL 189 189 Calcium 1; via carbonyl oxygen.
METAL 191 191 Calcium 1; via carbonyl oxygen.
METAL 193 193 Calcium 1.
METAL 195 195 Zinc 1. {ECO:0000269|PubMed:8137810}.
METAL 197 197 Calcium 2. {ECO:0000269|PubMed:8137810}.
METAL 200 200 Calcium 2. {ECO:0000269|PubMed:8137810}.
METAL 217 217 Zinc 2; catalytic.
{ECO:0000269|PubMed:8137810}.
METAL 221 221 Zinc 2; catalytic.
{ECO:0000269|PubMed:8137810}.
METAL 227 227 Zinc 2; catalytic.
{ECO:0000269|PubMed:8137810}.
METAL 286 286 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 378 378 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
METAL 425 425 Calcium 3; via carbonyl oxygen.
{ECO:0000250}.
CARBOHYD 54 54 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 73 73 N-linked (GlcNAc...) asparagine.
{ECO:0000305}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
CARBOHYD 204 204 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 246 246 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 279 464 {ECO:0000305}.
VARIANT 3 3 S -> C (in dbSNP:rs17099450).
{ECO:0000269|Ref.2}.
/FTId=VAR_025036.
VARIANT 32 32 T -> I (in dbSNP:rs3765620).
{ECO:0000269|PubMed:2159879,
ECO:0000269|Ref.2}.
/FTId=VAR_025037.
VARIANT 87 87 K -> E (in dbSNP:rs1940475).
{ECO:0000269|Ref.2}.
/FTId=VAR_006730.
VARIANT 154 154 G -> E (in dbSNP:rs35056226).
{ECO:0000269|Ref.2}.
/FTId=VAR_025038.
VARIANT 193 193 D -> V (in dbSNP:rs34428739).
{ECO:0000269|Ref.2}.
/FTId=VAR_025039.
VARIANT 246 246 N -> Y (in dbSNP:rs35243553).
{ECO:0000269|Ref.2}.
/FTId=VAR_025040.
VARIANT 436 436 V -> A (in dbSNP:rs34009635).
{ECO:0000269|Ref.2}.
/FTId=VAR_025041.
VARIANT 460 460 K -> T (in dbSNP:rs35866072).
{ECO:0000269|Ref.2}.
/FTId=VAR_025042.
CONFLICT 40 40 F -> I (in Ref. 4; AA sequence).
{ECO:0000305}.
CONFLICT 48 48 Y -> V (in Ref. 4; AA sequence).
{ECO:0000305}.
STRAND 107 109 {ECO:0000244|PDB:1MNC}.
STRAND 111 117 {ECO:0000244|PDB:1I76}.
STRAND 122 124 {ECO:0000244|PDB:1JAQ}.
HELIX 126 141 {ECO:0000244|PDB:1I76}.
STRAND 147 150 {ECO:0000244|PDB:1I76}.
STRAND 152 154 {ECO:0000244|PDB:1I76}.
STRAND 157 163 {ECO:0000244|PDB:1I76}.
STRAND 168 170 {ECO:0000244|PDB:1I76}.
STRAND 175 178 {ECO:0000244|PDB:1I76}.
STRAND 181 183 {ECO:0000244|PDB:1I76}.
STRAND 186 188 {ECO:0000244|PDB:1I76}.
TURN 189 192 {ECO:0000244|PDB:1I76}.
STRAND 194 197 {ECO:0000244|PDB:1I76}.
STRAND 203 208 {ECO:0000244|PDB:1I76}.
HELIX 211 223 {ECO:0000244|PDB:1I76}.
STRAND 236 238 {ECO:0000244|PDB:1I76}.
STRAND 244 246 {ECO:0000244|PDB:1ZP5}.
HELIX 251 261 {ECO:0000244|PDB:1I76}.
SEQUENCE 467 AA; 53412 MW; 4D4602A53AD7F8BC CRC64;
MFSLKTLPFL LLLHVQISKA FPVSSKEKNT KTVQDYLEKF YQLPSNQYQS TRKNGTNVIV
EKLKEMQRFF GLNVTGKPNE ETLDMMKKPR CGVPDSGGFM LTPGNPKWER TNLTYRIRNY
TPQLSEAEVE RAIKDAFELW SVASPLIFTR ISQGEADINI AFYQRDHGDN SPFDGPNGIL
AHAFQPGQGI GGDAHFDAEE TWTNTSANYN LFLVAAHEFG HSLGLAHSSD PGALMYPNYA
FRETSNYSLP QDDIDGIQAI YGLSSNPIQP TGPSTPKPCD PSLTFDAITT LRGEILFFKD
RYFWRRHPQL QRVEMNFISL FWPSLPTGIQ AAYEDFDRDL IFLFKGNQYW ALSGYDILQG
YPKDISNYGF PSSVQAIDAA VFYRSKTYFF VNDQFWRYDN QRQFMEPGYP KSISGAFPGI
ESKVDAVFQQ EHFFHVFSGP RYYAFDLIAQ RVTRVARGNK WLNCRYG


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E0103h ELISA kit CLG1,Homo sapiens,Human,Matrix metalloproteinase-8,MMP8,MMP-8,Neutrophil collagenase,PMNL collagenase,PMNL-CL 96T
U0103h CLIA CLG1,Homo sapiens,Human,Matrix metalloproteinase-8,MMP8,MMP-8,Neutrophil collagenase,PMNL collagenase,PMNL-CL 96T
15-288-21119 Neutrophil collagenase - EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL Polyclonal 0.1 mg
15-288-21119 Neutrophil collagenase - EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL Polyclonal 0.05 mg
10-663-45324 Matrix Metalloproteinase-8 (MMP-8) Human - EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL N_A 2.5 U
10-663-45324 Matrix Metalloproteinase-8 (MMP-8) Human - EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL N_A 1 Units
10-663-45324 Matrix Metalloproteinase-8 (MMP-8) Human - EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL N_A 10 Unit
18-272-195463 MMP8 - Rabbit polyclonal to MMP8; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL Polyclonal 0.05 mg
18-272-195461 MMP8 - Rabbit polyclonal to MMP8; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL Polyclonal 0.025 mg
18-272-195462 MMP8 - Rabbit polyclonal to MMP8; EC 3.4.24.34; Matrix metalloproteinase-8; MMP-8; PMNL collagenase; PMNL-CL Polyclonal 0.05 mg
E0103m ELISA Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
U0103m CLIA Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
E0103m ELISA kit Collagenase 2,Matrix metalloproteinase-8,Mmp8,MMP-8,Mouse,Mus musculus,Neutrophil collagenase 96T
U0097r CLIA Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
E0097r ELISA Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
E0097r ELISA kit Fibroblast collagenase,Interstitial collagenase,Matrix metalloproteinase-1,Mmp1,MMP-1,Myocardial collagenase,Rat,Rattus norvegicus 96T
15-288-21115 Interstitial collagenase - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Polyclonal 0.05 mg
15-288-21115 Interstitial collagenase - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Polyclonal 0.1 mg
20-783-73156 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
20-783-73157 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
20-783-73158 MOUSE ANTI HUMAN COLLAGENASE - EC 3.4.24.7; Matrix metalloproteinase-1; MMP-1; Fibroblast collagenase Monoclonal 0.2 mg
E0320Ra Rat matrix metalloproteinase 8 per Neutrophil collagenase,MMP-8 ELISA kit 48T
SL0488Ra Rat matrix metalloproteinase 8 Neutrophil collagenase,MMP-8 ELISA kit 96T
YHB0723Ra Rat matrix metalloproteinase 8-Neutrophil collagenase,MMP-8 ELISA kit 96T


 

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