Matrix Metalloproteinase 8 (MMP8)

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CLG2; HNC; PMNL-CL; Collagenase 2; Neutrophil Collagenase; PMNL collagenase

Matrix Metalloproteinase 8 (MMP8)

MMP8 degrades fibrillar collagens types I, II, III, aggrecan, serpins and alpha 2 macroglobulin. The substrate specificity of collagenases is variable: MMP1 degrades type III collagen more efficiently than type I or type II collagen, whereas MMP8 is more potent in degrading type I collagen than type III or type II collagen. Unlike other members, MMP8 is expressed exclusively in inflammatory conditions. MMP8 is highly expressed in the postpartum uterus, and it is thought to be involved in the postpartum involution of the uterus. MMP8 is also the predominant collagenase expressed in ulcers and healing wounds. MMP8 is very similar to MMP1, sharing 57 % amino acid identity. MMP8 is heavily glycosylated, and the zymogen has a mass of 85 Kd.

Organism species: Homo sapiens (Human)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA103Hu01 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA103Hu01 Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
MAA103Hu22 Monoclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB,IHC
LAA103Hu71 Biotin-Linked Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC.
LAA103Hu81 FITC-Linked Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IF.
MAA103Hu21 Monoclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
Assay Kits SEA103Hu ELISA Kit for Matrix Metalloproteinase 8 (MMP8) Enzyme-linked immunosorbent assay for Antigen Detection.
SCA103Hu CLIA Kit for Matrix Metalloproteinase 8 (MMP8) Chemiluminescent immunoassay for Antigen Detection.

Organism species: Mus musculus (Mouse)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA103Mu01 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
RPA103Mu02 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA103Mu01 Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
PAA103Mu02 Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
Assay Kits SEA103Mu ELISA Kit for Matrix Metalloproteinase 8 (MMP8) Enzyme-linked immunosorbent assay for Antigen Detection.
SCA103Mu CLIA Kit for Matrix Metalloproteinase 8 (MMP8) Chemiluminescent immunoassay for Antigen Detection.

Organism species: Rattus norvegicus (Rat)

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA103Ra01 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
RPA103Ra02 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA103Ra01 Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
MAA103Ra21 Monoclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
MAA103Ra22 Monoclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
Assay Kits SEA103Ra ELISA Kit for Matrix Metalloproteinase 8 (MMP8) Enzyme-linked immunosorbent assay for Antigen Detection.
SCA103Ra CLIA Kit for Matrix Metalloproteinase 8 (MMP8) Chemiluminescent immunoassay for Antigen Detection.

Organism species: Cavia (Guinea pig )

CATALOG NO. PRODUCT NAME APPLICATIONS
Proteins RPA103Gu01 Recombinant Matrix Metalloproteinase 8 (MMP8) Positive Control; Immunogen; SDS-PAGE; WB.
Antibodies PAA103Gu01 Polyclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
MAA103Gu21 Monoclonal Antibody to Matrix Metalloproteinase 8 (MMP8) WB; IHC; ICC; IP.
Assay Kits SEA103Gu ELISA Kit for Matrix Metalloproteinase 8 (MMP8) Enzyme-linked immunosorbent assay for Antigen Detection.
  1. "Human neutrophil collagenase. A distinct gene product with homology to other matrix metalloproteinases."J. Biol. Chem. 265:11421-11424(1990) [PubMed] [Europe PMC] [Abstract]
  2. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
  3. "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) [PubMed] [Europe PMC] [Abstract]
  4. "Mercurial activation of human polymorphonuclear leucocyte procollagenase."Eur. J. Biochem. 202:1223-1230(1991) [PubMed] [Europe PMC] [Abstract]
  5. "Characterization of 58-kilodalton human neutrophil collagenase: comparison with human fibroblast collagenase."Biochemistry 29:10628-10634(1990) [PubMed] [Europe PMC] [Abstract]
  6. "Partial amino acid sequence of human PMN leukocyte procollagenase."Biol. Chem. Hoppe-Seyler 371:295-304(1990) [PubMed] [Europe PMC] [Abstract]
  7. ErratumBiol. Chem. Hoppe-Seyler 371:733-733(1990) [PubMed] [Europe PMC] [Abstract]
  8. "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) [PubMed] [Europe PMC] [Abstract]
  9. "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) [PubMed] [Europe PMC] [Abstract]
  10. "Structural implications for the role of the N-terminus in the 'superactivation' of collagenases. A crystallographic study."FEBS Lett. 338:227-233(1994) [PubMed] [Europe PMC] [Abstract]
  11. "Structure of human neutrophil collagenase reveals large S1' specificity pocket."Nat. Struct. Biol. 1:119-123(1994) [PubMed] [Europe PMC] [Abstract]
  12. "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) [PubMed] [Europe PMC] [Abstract]
  13. "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) [PubMed] [Europe PMC] [Abstract]