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Matrix Metalloproteinase-7 (MMP-7) Human ELISA

  • Regulatory status:RUO
  • Type:Sandwich ELISA, Biotin-labelled antibody
  • Other names:Matrix metalloproteinase-7
  • Species:Human
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Cat. No. Size Price


RD193438200CS 96 wells (1 kit)
PubMed Product Details
Technical Data

Type

Sandwich ELISA, Biotin-labelled antibody

Applications

Serum, Plasma (EDTA, citrate, heparin)

Sample Requirements

35 µl/well

Shipping

At ambient temperature. Upon receipt, store the product at the temperature recommended below.

Storage/Expiration

Store the complete kit at 2–8°C. Under these conditions, the kit is stable until the expiration date (see label on the box)

Calibration Curve

Calibration Range

0.125–4 ng/ml

Summary

Features

  • It is intended for research use only
  • The total assay time is less than 3 hours
  • The kit measures MMP-7 in human serum and plasma (EDTA, citrate, heparin)
  • Assay format is 96 wells
  • Standard is a recombinant protein produced in NS0 cells
  • Components of the kit are provided ready to use, concentrated or lyophilized

Research topic

Immune Response, Infection and Inflammation, Oncology, Others, Pulmonary diseases

Summary

Matrix metalloproteinases (MMPs) constitute a family of structurally related zinc-dependent endopeptidases capable of degrading basement membrane and all components of the extracellular matrix. Tissue inhibitors of metalloproteinases (TIMPs) inhibit the proteolytic activity of MMPs. The balance between metalloproteinases and their inhibitors has been shown to be important in the development of pancreatic cancer. Pancreatic cancer progression is associated with changes in the levels of MMP and TIMP expression. The overexpression of MMP-7 is significantly associated with metastasis and the 1-year survival rate in pancreatic cancer.
MMPs perform multiple roles including tissue remodeling, repair, and modulation of immune responses. In healthy tissues, MMPs are rarely expressed: their biological activity is tightly regulated by various mechanisms. Excessive MMP production has been reported in diverse inflammatory conditions such as cancer, chronic obstructive pulmonary disease, sarcoidosis, interstitial lung disease, arthritis, and atherosclerosis.
MMP-7 is produced mainly by glandular epithelial cells and macrophages in diseased tissues and is overexpressed by cancer cells in human tumors. It has been linked to the development of metastases and is also considered to play a role in tumorigenesis and tumor progression. MMP-7 (matrilysin) cleaves collagen IV, elastin, intactin, fibronectin, gelatin, laminin and tenascin, and is known to be involved in several lung malignancies and non-malignancies, including IPF and NSCLC.
MMP-7 has been found to be over-expressed in several tumors, such as those associated with esophageal, cholangiocarcinoma, gastric, colon, prostate and bladder cancer.
Huang et al (2005) have reported that MMP-7 is a major matrix metalloproteinase associated with tissue remodeling during the progression of liver fibrosis in biliary atresia.
Zuo et al (2002) have identified expression of MMP-7 as a mediator of pulmonary fibrosis and reported that knock-out mice lacking expression of MMP-7 are protected from pulmonary fibrosis in response to intratracheal bleomycin.
Saarialho-Kere et al (1996) have reported enhanced expression of MMP-7 in gastrointestinal ulcers, suggesting a significant role in epithelial remodelling occurring in gastrointestinal ulcerations. Matsuno et al (2003) have reported that MMP-7 appears to be expressed only in the epithelial cells on the edge of ulcers and indicates the degree of inflammation in ulcerative colitis.

Clinical use and areas of investigation:

  • Pancreatic cancer
  • Colorectal cancer
  • Inflammatory diseases
  • Tissue regeneration
References to Summary

References to MMP-7

  • Gunes M, Kemik AS, Pirincci N, Gecit I, Taken K, Yuksel MB, Kaba M, Eryilmaz R. Preoperative levels of matrix metalloproteinase-7 and -9 and tissue inhibitor of matrix metalloproteinase-1 relation to pathologic parameters in bladder carcinoma patients. Asian Pac J Cancer Prev. 2013;14 (2):873-6
  • Park HD, Kang ES, Kim JW, Lee KT, Lee KH, Park YS, Park JO, Lee J, Heo JS, Choi SH, Choi DW, Kim S, Lee JK, Lee SY. Serum CA19-9, cathepsin D, and matrix metalloproteinase-7 as a diagnostic panel for pancreatic ductal adenocarcinoma. Proteomics. 2012 Dec;12 (23-24):3590-7
  • Tadokera R, Meintjes GA, Wilkinson KA, Skolimowska KH, Walker N, Friedland JS, Maartens G, Elkington PT, Wilkinson RJ. Matrix metalloproteinases and tissue damage in HIV-tuberculosis immune reconstitution inflammatory syndrome. Eur J Immunol. 2014 Jan;44 (1):127-36
  • Ulivi P, Casoni GL, Foschi G, Scarpi E, Tomassetti S, Romagnoli M, Ravaglia C, Mengozzi M, Zoli W, Poletti V. MMP-7 and fcDNA serum levels in early NSCLC and idiopathic interstitial pneumonia: preliminary study. Int J Mol Sci. 2013;14 (12):24097-112
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