Home » Products » Immunoassays » 7664-93-9 MMP-3 ELISA

7664-93-9
MMP-3 ELISA
FormatELISA/EIA
Storage2 - 8℃
Package96 wells
SpeciesMouse monoclonal
Sample typesSerum
Sample size40μL
Sensitivity2.5 ng/mL
Range12.5 - 800 ng/mL
Protocol

1st Incubation 1.5 hrs, 2nd incubation 30 min

Download (protocol)protocol
Note

Detection Target name
MMP-3

Target Synonyms
MMP-3,Matrix metalloproteinase 3, Stromelysin-1, Transin-1, SL-1

Description
Matrix metalloproteinase-3 (MMP-3) is a useful marker to evaluate the prognosis of joint destruction in rheumatoid arthritis (RA), in Japan. MMP-3 is expressed in synovial tissues and involved in cartilage destruction in RA and osteoarthritis (OA). MMP-3 plays an important role in degradation and reconstitution of extracellular matrix by degrading proteoglycan, fibronectin, type IV collagen, laminin and type IX collagen. MMP-3 is secreted as a latent form and activated out of membrane, which participate in metabolism of matrix tissue. Activity of MMP-3 is inhibited specifically by tissue inhibitors of metalloprotienases (TIMPs).


Specificity

MMP-1 : 0%

MMP-2 : 0%

MMP-3 : 100%

MMP-7 : 0%

MMP-8 : 0%

MMP-9 : 0%

MMP-10 : 1%

MMP-13 : 0%

MT1-MMP : 0%

TIMP-1 : 0%

TIMP-2 : 0%

TIMP-3 : 0%

 

Standard curve

 

MMP-3_standard_curves.jpg

 


This product is useful for Immunology and Rheumatoid Arthritis study.


News Article

MMP-3 ELISA Kit - New Best RA monitoring Marker

 

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Reference

(1) Y. Okada et al.: “A metalloproteinase from human rheumatoid synovial fibroblast that digests connective tissue matrix components.” J. Biol. Chem., 261, 14245-14255, 1986.

(2) K. Obata et al.: “A one-step sandwich enzyme immunoassay for human matrix metallopreoteinase 3 (stromelysin-1) using monoclonal antibodies.” Clin. Chim. Acta, 211, 59-72, 1992.

(3) J. Martel-Peletier et al.: “Excess of metalloproteases over tissue inhibitor of metalloprotease may contribute to cartilage degradation in osteoarthritis and rheumatoid arthritis.” Lab. Invest., 70, 807-815, 1994.

(4) S. Sasaki et al.: “Detection of stromelysin in synovial fluid and serum from patients with rheumatoid arthritis and osteoarthritis.” Clin. Rheum., 13, 228-233,1994.

(5) Y. Yoshihara et al.: “Increased levels of stromelysin-1 and tissue inhibitor of metalloproteinases-1 in sera from patients with rheumatoid arthritis.” Arthritis. Rheum., 38, 969-975,1995.

(6) K. Yokouchi et al.: J. New Rem. & Clin., 50, 215-221, 2001.

(7) C Ribbens et al.: “Increased matrix metalloproteinase-3 serum levels in rheumatic diseases: relationship with synovitis and steroid treatment.” Ann Rheum Dis., 61, 161 – 166, 2002

(8) M. Shinozaki et al., “Elevation of serum matrix metalloproteinase-3 as a predictive marker for the long-term disability of rheumatoid arthritis patients in a prospective obserbational cohort IORRA.” Mod. Rheumatol. 17, 403 – 408, 2007

(9) S. Tsukahara et al., “Effect of matrix metalloproteinase-3 functional SNP on serum matrix metalloproteinase-3 level and outcome measures in Japanese RA patients.” Rheumatology, 47, 41 – 44, 2008

(10) Kobayashi A. et al., “Serum levels of matrix metalloproteinase 3 (stromelysin 1) for monitoring synovitis in rheumatoid arthritis.” Arch Pathol Lab Med., 131(4), 563-70, 2007

(11) Viswanath V. et al., “Levels of serum matrix metalloproteinase-3 correlate with disease activity in the enthesitis-related arthritis category of juvenile idiopathic arthritis.” J. Rheumatol., 38(11), 2482-7, 2011