96 Tests PN: B115629

Components:

45x Ab-conjugated beads (S4P7 - Human MMP-7 Ab-bead). PN: B115629A. One vial containing 100 µL of anti-human MMP-7 conjugated to AimPlex Bead S4P7.

25x Biotin-detection Ab (Human MMP-7 Biotin-dAb). PN: B115629B. One vial containing 100 µL of biotinylated anti- Human MMP-7.

Lyophilized Standard Mix - Human MMP-7. PN: B115629S. One vial containing lyophilized MMP-7.

Application: Optimal antibody pair and antigen standard for assaying human MMP-7/PUMP-1. To be used in conjunction with the AimPlex NR Basic Kit (PN: P100001) and a diluent kit. Refer to the AimPlex Multiplex Immunoassay User Manual and kit inserts for the assay procedure.

Storage:  2-8 C in the dark.

Important: Sodium azide forms explosive compounds with heavy metals. These products contain <0.05% (w/w) azide which with repeated contact with lead and copper commonly found in plumbing drains may result in the buildup of shock sensitive compounds. Dispose in accordance with regulations from your institute.

For Research Use Only. Not for use in diagnostic procedures.

Assay Specifications:

  • Sample types: Cell culture supernatant, serum, plasma, bodily fluid and tissue/cell lysate

  • Sensitivity (LOD): < 100 pg/mL

  • Quantitation range:

  • LLOQ: <200 pg/mL

  • ULOQ: > 20,000 pg/mL

  • Standard dose recovery: 70-130%

  • Intra-assay CV: < 10%

  • Inter-assay CV: < 20%

  • Sample volume: 15 µL/test

Description:

Matrilysin, or matrix metalloproteinase-7 (MMP-7), pump-1 protease (PUMP-1), or uterine metalloproteinase is an enzyme in humans that is a member of the matrix metalloproteinase (MMP) family consisting of structural-related zinc-dependent endopeptidases. The primary role of cleaved/activated MMP7 is to break down extracellular matrix by degrading macromolecules including casein, type I, II, IV, and V gelatins, fibronectin, and proteoglycan. MMP-7 is involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and tumor metastasis. The upregulation of MMP7 is associated with many malignant tumors including esophagus, stomach, colon, liver, pancreas, and renal cell carcinomas. High MMP7 expression facilitates cancer invasion and angiogenesis by degrading extracellular matrix macromolecules and connective tissues. Theses degradations are associated with many mechanisms including embryogenesis, postpartum uterine involution, tissue repair, angiogenesis, bone remodeling, arthritis, decubitus ulcer, and tumor metastasis/invasion.

References:

  1. Knox JD, Boreham DR, Walker JA, Morrison DP, Matrisian LM, Nagle RB, Bowden GT (Jan 1997). "Mapping of the metalloproteinase gene matrilysin (MMP7) to human chromosome 11q21-->q22". Cytogenet Cell Genet 72 (2–3): 179–82. doi:10.1159/000134181. PMID 8978768.

  2. Woessner JF, Taplin CJ (November 1988). "Purification and properties of a small latent matrix metalloproteinase of the rat uterus". J. Biol. Chem. 263 (32): 16918–25. PMID 3182822.

  3. Parks WC, Mecham RP (1988). "Matrix Metalloproteinases" 263. San Diego: Academic.

  4. Yokoyama Y, Grünebach F, Schmidt SM, Heine A, Häntschel M, Stevanovic S, Rammensee HG, Brossart P (2008). "Matrilysin (MMP-7) is a novel broadly expressed tumor antigen recognized by antigen-specific T cells". Clin. Cancer Res. 14 (17): 5503–11. doi:10.1158/1078-0432.CCR-07-4041. PMID 18765542.