Matrix Metalloproteinase-1 (MMP-1) ELISA Kit


Human MMP-1 ELISA kit can be used for determining in vitro quantitative levels of matrix metalloproteinase-1 (MMP1, MMP-1, interstitial or fibroblast collagenase) in human cell culture supernatant, serum, cell lysates, other biological fluids and plasma. This assay has a minimum sensitivity limit of 0.065 ng/mL.


Matrix metalloproteinase-1 (more commonly referred to as MMP-1 or MMP1) is also referred to as fibroblast collagenase or interstitial collagenase and is part of the MMP genes that can be found located on chromosome 11q22.3. MMPs are made up of around 20 proteolytic enzymes that are essential in tissue remodelling. MMP-1 is found to play a critical role in the degradation of collagen which is present in inflammatory diseases. It possesses an archetypal structure that is made up of a pre-domain, a catalytic domain, a hemopexin-like domain, a pro-domain and a linker region. The catalytic domain consists of 5 highly twisted beta-strands, 3 alpha-helix and an overall total of eight loops which enclose 5 metal ions, one of which with found to possess the catalytic role.

The following MMP-1 ELISA kit is designed to be used for analysing many diagnostic applications. MMPs are important for breaking down of extracellular matrix in normal physiological processes (for example in tissue remodelling, reproduction and embryonic development) and also in many disease processes (for example metastasis and arthritis). MMP-1 are a specific function in the breakdown of interstitial collagens (I, II and III). It also has the ability to interact with CD49b and mechanical forces have been identified which can lead to increasing the expression of MMP1 in human periodontal ligament cells. This MMP-1 ELISA kit offers a sensitivity limit of 0.065 ng/mL and it can be used to measure human samples of serum, biological fluids, plasma, cell culture supernatant and cell lysates.


The minimum detection sensitivity level of matrix metalloproteinase-1 (MMP-1, MMP1, fibroblast or interstitial collagenase) using current human MMP-1 ELISA kit was 0.065 ng/mL. The dynamic range for this assay is 0.156 – 10 ng/mL.


  1. Matrix metalloproteinases as therapeutic targets for idiopathic pulmonary fibrosis. Am J Respir Cell Mol Biol. (2015) 53 (5): 585-600. Review. Craig V.J., et al.
  2. MMP-1 polymorphism and its relationship to pathological processes. J Biosci. (2009) 34 (2): 313-20. Review. Arakaki P.A., et al.
  3. Role of Matrix Metalloproteinases in Photoaging and Photocarcinogenesis. Int J Mol Sci. (2016) 17 (6). pii: E868. Review. Pittayapruek P., et al.
  4. Membrane-type matrix metalloproteinases (MT-MMPs) in tumor metastasis. J Biochem. (1996) 119 (2): 209-15. Review. Sato H. and Seiki M.
  5. MMP-1: the elder of the family. Int J Biochem Cell Biol. (2005) 37 (2): 283-8. Review. Pardo A. and Selman M.


  • Full Name: Matrix Metalloproteinase-1 (MMP-1) ELISA Kit
  • Reactivity: Human
  • Sample Type: Cell Culture Supernatant, Plasma, Cell Lysates, Other Biological Fluids, Serum
  • Sensitivity: 0.065 ng/mL



Your secretory IgA ELISA gave good results and I was also really impressed with how quickly we received it.

L. Johnston
PhD Student / University of Glasgow

It is refreshing to know that you have a technical team that is very knowledgeable. I have already recommended your company to other researchers in our department.

Dr. P. Anderson
Lecturer / University College London (UCL)

I am a first time user and found that your instruction manual was very easy to follow. The insulin ELISA assay performed well and I was happy with the results that were generated.

J. Thomas
Senior Technician / Addenbrooke’s Hospital

I carried out a pilot study comparing the performance of many ELISA assay's from different suppliers and found your kits to be one of the better performers. We observed good linearity and tight replicates.

Dr. C. Davies
Lead Scientists / AstraZeneca

You are my first point of contact when I am looking to purchase ELISA. You have such an easy and simple system, yet it is very effective.

A. Shaw
Purchasing / University of Oxford