生化/生理作用
基质金属蛋白酶的有机汞活化剂。
免责声明
对于美国客户:本品含汞。废弃后切勿放入垃圾桶,须按照地方、州或联邦法律处置。


警示用语:
Danger
危险分类
Acute Tox. 1 Dermal - Acute Tox. 2 Inhalation - Acute Tox. 2 Oral - Aquatic Acute 1 - Aquatic Chronic 1 - STOT RE 2
储存分类代码
6.1A - Combustible acute toxic Cat. 1 and 2 / very toxic hazardous materials
WGK
WGK 3
闪点(°F)
Not applicable
闪点(°C)
Not applicable
个人防护装备
Eyeshields, Faceshields, Gloves, type P3 (EN 143) respirator cartridges
Reihane Ziadlou et al.
Biomolecules, 10(6) (2020-06-25)
In osteoarthritis (OA), inhibition of excessively expressed pro-inflammatory cytokines in the OA joint and increasing the anabolism for cartilage regeneration are necessary. In this ex-vivo study, we used an inflammatory model of human OA chondrocytes microtissues, consisting of treatment with
A Bianchi et al.
Osteoarthritis and cartilage, 24(11), 1961-1969 (2016-10-21)
Fibroblast Growth Factor 23 (FGF23) may represent an attractive candidate that could participate to the osteoarthritic (OA)-induced phenotype switch of chondrocytes. To address this hypothesis, we investigated the expression of FGF23, its receptors (FGFRs) and co-receptor (Klotho) in human cartilage
Equine laminitis: glucose deprivation and MMP activation induce dermo-epidermal separation in vitro.
K R French et al.
Equine veterinary journal, 36(3), 261-266 (2004-05-19)
Acute laminitis is characterised by hoof lamellar dermal-epidermal separation at the basement membrane (BM) zone. Hoof lamellar explants cultured in vitro can also be made to separate at the basement membrane zone and investigating how this occurs may give insight
Jan-Olof Winberg et al.
European journal of biochemistry, 270(19), 3996-4007 (2003-09-27)
In the leukemic macrophage cell-line THP-1, a fraction of the secreted matrix metalloproteinase 9 (MMP-9) is linked to the core protein of chondroitin sulfate proteoglycans (CSPG). Unlike the monomeric and homodimeric forms of MMP-9, the addition of exogenous CaCl2 to
Georgina S Butler et al.
The Journal of biological chemistry, 279(15), 15615-15620 (2004-01-21)
Matrix metalloproteinases (MMPs) are an important family of extracellular proteases that process a variety of biologically significant molecules. MMPs are members of the metzincin superfamily of >770 zinc endopeptidases, which includes astacins, serralysins, adamalysins, leishmanolysins, and snapalysins. Metzincins are characterized
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