Fibrillin-2 inhibitors constitute a specialized class of chemical compounds designed to modulate the activity of fibrillin-2, a crucial component of the extracellular matrix (ECM) in various tissues. Fibrillins are large, glycoprotein-rich molecules that form microfibrils, contributing to the structural integrity of connective tissues. Specifically, fibrillin-2 is predominantly found in elastic fibers within tissues such as the skin, blood vessels, and lungs. These fibers provide elasticity and resilience to these tissues, playing a fundamental role in maintaining their structural integrity and function. Fibrillin-2 inhibitors aim to selectively target and impede the function of fibrillin-2, thereby influencing the formation and properties of the associated microfibrils.
fibrillin-2 inhibitors is rooted in the recognition of the essential role played by fibrillins in tissue biomechanics and homeostasis. By modulating fibrillin-2 activity, these inhibitors offer a means to investigate the underlying molecular mechanisms of tissue elasticity and provide potential tools for manipulating tissue properties in a controlled manner. The study and understanding of fibrillin-2 inhibitors contribute to advancing our knowledge of extracellular matrix dynamics and hold promise for uncovering novel insights into the regulation of tissue elasticity, with potential implications for various fields including biomaterials and tissue engineering. Ongoing research in this chemical class seeks to elucidate the precise mechanisms of fibrillin-2 inhibition and explore potential applications in the modulation of tissue mechanics for scientific inquiry and innovation.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Genistein | 446-72-0 | sc-3515 sc-3515A sc-3515B sc-3515C sc-3515D sc-3515E sc-3515F | 100 mg 500 mg 1 g 5 g 10 g 25 g 100 g | $45.00 $164.00 $200.00 $402.00 $575.00 $981.00 $2031.00 | 46 | |
Interferes with tyrosine kinase which plays a role in the phosphorylation of proteins involved in extracellular matrix formation. | ||||||
3-Aminopropionitrile | 151-18-8 | sc-266473 | 1 g | $104.00 | ||
Inhibits lysyl oxidase, an enzyme that catalyzes crosslinking of collagen and elastin fibers, thereby potentially altering the microfibril assembly in which fibrillin-2 is involved. | ||||||
Disulfiram | 97-77-8 | sc-205654 sc-205654A | 50 g 100 g | $53.00 $89.00 | 7 | |
Inhibits lysyl oxidase, potentially affecting the integrity of microfibrils. | ||||||
Halofuginone | 55837-20-2 | sc-507290 | 100 mg | $1775.00 | ||
Inhibits collagen type I synthesis and could indirectly affect the microfibril network associated with fibrillin-2. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $46.00 $96.00 | ||
Binds to pyridinoline cross-links in collagen, potentially disrupting the microfibrillar network. | ||||||
Catechin | 154-23-4 | sc-205624 sc-205624A | 1 mg 5 mg | $133.00 $299.00 | 3 | |
An antioxidant that may protect against oxidative stress-related damage to fibrillin and other extracellular matrix proteins. | ||||||
(−)-Epigallocatechin Gallate | 989-51-5 | sc-200802 sc-200802A sc-200802B sc-200802C sc-200802D sc-200802E | 10 mg 50 mg 100 mg 500 mg 1 g 10 g | $43.00 $73.00 $126.00 $243.00 $530.00 $1259.00 | 11 | |
Modulates fibroblast activity and could indirectly influence the turnover of extracellular matrix components including fibrillin-2. | ||||||
Baicalein | 491-67-8 | sc-200494 sc-200494A sc-200494B sc-200494C | 10 mg 100 mg 500 mg 1 g | $32.00 $42.00 $162.00 $292.00 | 12 | |
Inhibits elastase and other proteolytic enzymes that could degrade extracellular matrix components. | ||||||
L-Mimosine | 500-44-7 | sc-201536A sc-201536B sc-201536 sc-201536C | 25 mg 100 mg 500 mg 1 g | $36.00 $88.00 $220.00 $436.00 | 8 | |
Inhibits lysyl oxidase activity and thus may impact the crosslinking within the extracellular matrix. | ||||||
PD 98059 | 167869-21-8 | sc-3532 sc-3532A | 1 mg 5 mg | $40.00 $92.00 | 212 | |
An inhibitor of MAP kinase which affects cell signaling pathways that could alter extracellular matrix synthesis. | ||||||