M1677
Matrix Metalloproteinase-3 from human fibroblasts
≥95% (SDS-PAGE), buffered aqueous solution
Synonym(s):
MMP-3, Proteoglycanase, Stromelysin-1, Transin
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
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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
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
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
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