Human Total MMP-3 Quantikine ELISA Kit

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Product Details

Summary
Reactivity HuSpecies Glossary
Applications ELISA
Conjugate
HRP

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Human Total MMP-3 Quantikine ELISA Kit Summary

Background
The Quantikine Human Total MMP-3 Immunoassay is a 4.5 hour solid phase immunoassay designed to measure total MMP-3 (pro- and active MMP-3) in cell culture supernates, serum, and plasma. It contains NS0-expressed recombinant human Pro-MMP-3 and antibodies raised against the recombinant factor. Both antibodies also recognize recombinant human active MMP-3. Natural human MMP-3 showed dose-respo...nse curves that were parallel to the standard curves obtained using the recombinant Quantikine kit standards, indicating that this kit can be used to determine relative levels of natural human MMP-3.
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Specificity
Natural and recombinant human total MMP-3
Source
N/A
Assay Type
Solid Phase Sandwich ELISA
Inter-Assay
See PDF Datasheet for details
Intra-Assay
See PDF Datasheet for details
Spike Recovery
See PDF Datasheet for details
Sample Volume
See PDF Datasheet for details
Gene
MMP3

Applications/Dilutions

Application Notes
No significant interference observed with available related molecules.
Publications
Read Publications using DMP300.

Packaging, Storage & Formulations

Storage
Store the unopened product at 2 - 8 °C. Do not use past expiration date.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Human Total MMP-3 Quantikine ELISA Kit

  • CHDS6
  • EC 3.4.24
  • EC 3.4.24.17
  • matrix metallopeptidase 3 (stromelysin 1, progelatinase)
  • matrix metalloproteinase 3 (stromelysin 1, progelatinase)
  • Matrix metalloproteinase-3
  • MGC126102
  • MGC126103
  • MMP3
  • MMP-3
  • proteoglycanase
  • SL-1
  • STMY
  • STMY1MGC126104
  • STR1
  • Stromelysin 1
  • stromelysin-1
  • transin-1

Background

Matrix metalloproteinases (MMPs), also called matrixins, constitute a family of zinc and calcium dependent endopeptidases that function in the breakdown of extracellular matrix (ECM). They play an important role in many normal physiological processes such as embryonic development, morphogenesis, reproduction and tissue remodeling (1). They also participate in many pathological processes such as arthritis, cancer and cardiovascular disease (2). While the amounts of newly synthesized MMPs are regulated mainly at the levels of transcription, the proteolytic activities of existing MMPs are controlled through both the activation of proenzymes or zymogens and the inhibition of active enzymes by endogenous inhibitors, alpha -macroglobulins and tissue inhibitors of metalloproteinases (TIMPs). 
MMP-3 (also referred to as stromelysin-1) may be expressed in fibroblasts, chondrocytes, endothelial cells, macrophages, vascular smooth muscle cells, osteoblasts, and keratinocytes in response to appropriate stimuli (3). Various agents regulate its biosynthesis. Inflammatory cytokines such as IL-1 and TNF-alpha, epidermal growth factor, platelet-derived growth factor, phorbol and oncogenic cellular transformation are the inductive agents. In comparison, retinoic acid, glucocorticoids, estrogen, progesterone and TGF-beta suppress MMP-3 synthesis. 
MMP-3 is secreted from the cells as a proenzyme. The proenzyme has been shown to stimulate plasminogen activation (4). The N-terminal pro-domain contains the cysteine switch motif conserved in MMPs that maintains MMP-3 in the latent state (5). Activation of the proenzyme results in the removal of the pro-domain. MMP-3 activation can be achieved in vitro by proteases such as itself, chyrotrypsin, neutrophil elastase and plasma kallikrein, and by mercury compounds (3). The resulting active enzyme consists of a catalytic domain with a zinc-binding motif conserved in metzincins (6,7). A short hinge peptide links the catalytic domain to the C-terminal hemopexin-like domain. The active MMP-3 is capable of cleaving types III, IV, IX and X collagen, aggrecan, fibronectin, laminin, IGFBP-3, serpins, and IL-1 beta. The active enzyme also activates proMMP-1, -8, -9, and -13. Therefore, it is suggested that MMP-3 may participate in physiological matrix turnover and pathological destruction of the tissue. For example, MMP-3 is required for the generation of a macrophage chemoattractant in a model of herniated disc resorption (8).

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⚠ WARNING: This product can expose you to chemicals including N,N-Dimethylforamide, which is known to the State of California to cause cancer. For more information, go to www.P65Warnings.ca.gov.

Publications for MMP-3 (DMP300)(39)

We have publications tested in 1 confirmed species: Human.


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Human
(39)
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Showing Publications 1 - 10 of 39. Show All 39 Publications.
Publications using DMP300 Applications Species
YY Liu, SY Wang, YN Li, WJ Bian, LQ Zhang, YH Li, L Long, X Liu, XW Zhang, ZG Li Activity of fibroblast-like synoviocytes in rheumatoid arthritis was impaired by dickkopf-1 targeting siRNA Chin. Med. J., 2020;0(6):679-686. 2020 [PMID: 32068606] (Human) Human
DP Zhang, YF Peng, HL Zhang, JG Ma, M Zhao, S Yin, TT Wei Basilar Artery Tortuosity Is Associated With White Matter Hyperintensities by TIMP-1 Front Neurosci, 2019;13(0):836. 2019 [PMID: 31474817] (Human) Human
B Kollar, A Shubin, TJ Borges, S Tasigiorgo, TS Win, CG Lian, ST Dillon, X Gu, I Wyrobnik, GF Murphy, B Pomahac, TA Libermann, LV Riella Increased levels of circulating MMP3 correlate with severe rejection in face transplantation Sci Rep, 2018;8(1):14915. 2018 [PMID: 30297859] (Human) Human
CH Hulme, EL Wilson, HR Fuller, S Roberts, JB Richardson, P Gallacher, MJ Peffers, SL Shirran, CH Botting, KT Wright Two independent proteomic approaches provide a comprehensive analysis of the synovial fluid proteome response to Autologous Chondrocyte Implantation Arthritis Res. Ther., 2018;20(1):87. 2018 [PMID: 29720234] (Human) Human
R Audo, V Deckert, CI Daien, H Che, J Elhmioui, S Lemaire, JP Pais de Ba, C Desrumaux, B Combe, M Hahne, L Lagrost, J Morel PhosphoLipid transfer protein (PLTP) exerts a direct pro-inflammatory effect on rheumatoid arthritis (RA) fibroblasts-like-synoviocytes (FLS) independently of its lipid transfer activity PLoS ONE, 2018;13(3):e0193815. 2018 [PMID: 29565987] (Human) Human
C Robinson, L Tsang, A Solomon, AJ Woodiwiss, S Gunter, M Mer, HC Hsu, M Gomes, GR Norton, AME Millen, PH Dessein Nesfatin-1 and visfatin expression is associated with reduced atherosclerotic disease risk in patients with rheumatoid arthritis Peptides, 2018;102(0):31-37. 2018 [PMID: 29475075] (Human) Human
SM Hou, CH Hou, JF Liu CX3CL1 promotes MMP-3 production via the CX3CR1, c-Raf, MEK, ERK, and NF-?B signaling pathway in osteoarthritis synovial fibroblasts Arthritis Res. Ther., 2017;19(1):282. 2017 [PMID: 29268768] (Human) Human
DR Jadon, R Sengupta, A Nightingal, H Lu, J Dunphy, A Green, JT Elder, RP Nair, E Korendowyc, MA Lindsay, NJ McHugh Serum bone-turnover biomarkers are associated with the occurrence of peripheral and axial arthritis in psoriatic disease: a prospective cross-sectional comparative study Arthritis Res. Ther., 2017;19(1):210. 2017 [PMID: 28934972] (Human) Human
R Mechmeche, A Zaroui, S Aloui, M Boukhris, M Allal-Elas, N Kaabachi, B Zouari Late mitral restenosis after percutaneous commissurotomy: Predictive value of inflammation and extracellular matrix remodeling biomarkers Heart Lung, 2017;0(0):. 2017 [PMID: 28450150] (Human) Human
Concomitant elevations of MMP-9, NGAL, proMMP-9/NGAL and neutrophil elastase in serum of smokers with chronic obstructive pulmonary disease J. Cell. Mol. Med, 2016;0(0):. 2016 [PMID: 28004483] (Human) Human
Show All 39 Publications.

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Product General Protocols

Find general support by application which include: protocols, troubleshooting, illustrated assays, videos and webinars.

FAQs for MMP-3 (DMP300). (Showing 1 - 1 of 1 FAQs).

  1. wondering what the difference is between your quantikine and duo set elisas?
    • Usually the duosets do not have the entire kit such as plates and buffers, whereas the other kits are complete.

Other Available Formats

HRP DMP300
HRP DMP300
HRP DMP300

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Blogs on MMP-3.

MMP3 - a potential target for arthritis therapies
Matrix metalloproteinases (MMPs) are responsible for the degradation of extracellular matrix proteins. MMPs are essential for tissue remodeling during normal processes such as embryonic development as well as pathological conditions such as arthri...  Read full blog post.

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Bioinformatics

Gene Symbol MMP3