Skip to Content
Merck
CN

M1677

Matrix Metalloproteinase-3 from human fibroblasts

≥95% (SDS-PAGE), buffered aqueous solution

Synonym(s):

MMP-3, Proteoglycanase, Stromelysin-1, Transin

Sign In to View Organizational & Contract Pricing.

Select a Size


About This Item

EC Number:
EC Number:
231-791-2
UNSPSC Code:
12352200
MDL number:
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist
Technical Service
Need help? Our team of experienced scientists is here for you.
Let Us Assist

assay

≥95% (SDS-PAGE)

form

buffered aqueous solution

UniProt accession no.

shipped in

dry ice

storage temp.

−70°C

Gene Information

human ... MMP3(4314)

Biochem/physiol Actions

Breaks down proteoglycan, fibronectin, laminin, and type IV collagen, but not interstitial type I collagen.

Physical form

Solution in 50 mM Tris, pH 7.4, 0.5 M sodium chloride, 10 mM calcium chloride, 0.05% Brij-35, and 0.02% sodium azide.

Storage Class

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, multi-purpose combination respirator cartridge (US)

Regulatory Information

新产品
This item has

Choose from one of the most recent versions:

Certificates of Analysis (COA)

Lot/Batch Number

Don't see the Right Version?

If you require a particular version, you can look up a specific certificate by the Lot or Batch number.

Already Own This Product?

Find documentation for the products that you have recently purchased in the Document Library.

Visit the Document Library

Tayo Kawazu et al.
Medical molecular morphology, 45(4), 190-198 (2012-12-12)
We investigated the mechanism of development and repair process of glomerular injury in a rat model of habu snake (Trimeresurus flavoviridis) venom (HSV)-induced glomerulonephritis. Glomerulonephritis was induced in rats by intravenously injecting HSV at 3 mg/kg. Renal tissue was isolated
Azadeh Andisheh Tadbir et al.
Asian Pacific journal of cancer prevention : APJCP, 13(9), 4545-4548 (2012-11-22)
MMP-3 is a proteolytic enzyme of the matrix metalloproteinase family. Protein degradation which is their fundamental action regulates different activities of tumor cell such as their growth, differentiation, apoptosis, migration, invasion, angiogenesis as well as their resistance to the immune
Hisanori Eba et al.
PloS one, 7(12), e52523-e52523 (2013-01-04)
Matrix metalloproteinases (MMPs) are involved in extracellular matrix degradation and the modulation of cell behavior. These proteinases have also been implicated in tissue repair and regeneration. Our previous studies have demonstrated that MMP-3 elicits stimulatory effects on the proliferation and
Jyotica Batra et al.
PloS one, 7(11), e50028-e50028 (2012-11-28)
Excess proteolytic activity of matrix metalloproteinases (MMPs) contributes to the development of arthritis, cardiovascular diseases and cancer progression, implicating these enzymes as therapeutic targets. While many small molecule inhibitors of MMPs have been developed, clinical uses have been limited, in
Inge Tency et al.
PloS one, 7(11), e49042-e49042 (2012-11-13)
Matrix metalloproteinases (MMPs) are involved in remodeling of the extracellular matrix (ECM) during pregnancy and parturition. Aberrant ECM degradation by MMPs or an imbalance between MMPs and their tissue inhibitors (TIMPs) have been implicated in the pathogenesis of preterm labor

Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.

Contact Technical Service