COL1A2 inhibitors belong to a specific chemical class of compounds designed to target and inhibit the activity of Collagen Type I Alpha 2 Chain (COL1A2). COL1A2 is a crucial component of collagen type I, the most abundant protein in the extracellular matrix of connective tissues. Collagen type I provides structural integrity to various tissues, including skin, bones, and tendons, and plays a vital role in maintaining tissue strength and resilience.
COL1A2 inhibitors work by specifically targeting the COL1A2 gene or its protein product, interfering with collagen type I synthesis and assembly. By doing so, these inhibitors may influence the composition and properties of connective tissues, impacting their mechanical and structural characteristics. Research into COL1A2 inhibitors is ongoing to unravel their precise mechanisms of action and explore their implications in understanding extracellular matrix dynamics. The study of COL1A2 inhibitors contributes to a deeper understanding of the intricate mechanisms governing tissue integrity and mechanical properties.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
LY2157299 | 700874-72-2 | sc-391123 sc-391123A | 5 mg 10 mg | $209.00 $352.00 | 3 | |
LY2157299 is a small molecule inhibitor of TGF-β receptor I kinase. It may impact the signaling pathway that regulates Col1A2 expression, potentially leading to reduced collagen synthesis. This inhibition could be beneficial in fibrotic conditions where excessive collagen production, including that of Col1A2, contributes to tissue fibrosis. | ||||||
Pirfenidone | 53179-13-8 | sc-203663 sc-203663A | 10 mg 50 mg | $100.00 $408.00 | 6 | |
Pirfenidone is an anti-fibrotic drug with unclear mechanisms. It might indirectly affect Col1A2 by modulating TGF-β and other profibrotic signaling pathways. By targeting these pathways, pirfenidone could potentially lead to reduced collagen production, impacting tissue fibrosis in conditions like idiopathic pulmonary fibrosis. | ||||||
Tranilast | 53902-12-8 | sc-200389 sc-200389A sc-200389B sc-200389C | 10 mg 50 mg 1 g 5 g | $30.00 $101.00 $277.00 $959.00 | 2 | |
Tranilast is an anti-inflammatory and anti-fibrotic agent. Its mechanisms involve modulation of various signaling pathways, potentially including those that impact Col1A2 expression. By interfering with fibrotic processes, tranilast might mitigate excessive collagen production in certain diseases. | ||||||
SB 431542 | 301836-41-9 | sc-204265 sc-204265A sc-204265B | 1 mg 10 mg 25 mg | $80.00 $212.00 $408.00 | 48 | |
SB431542 is a TGF-β receptor I kinase inhibitor. Since TGF-β signaling plays a role in collagen synthesis, inhibiting this pathway with SB431542 could potentially downregulate Col1A2 expression, offering a strategy to manage conditions characterized by excessive collagen production, such as fibrosis. | ||||||
Gallotannin | 1401-55-4 | sc-202619 sc-202619A sc-202619B sc-202619C sc-202619D sc-202619E sc-202619F | 1 g 10 g 100 g 250 g 1 kg 2.5 kg 5 kg | $25.00 $36.00 $66.00 $76.00 $229.00 $525.00 $964.00 | 12 | |
Gallotannin is a polyphenol compound that may affect TGF-β signaling. As TGF-β signaling contributes to Col1A2 expression, gallotannin could modulate collagen synthesis by targeting the underlying signaling pathways, offering potential applications in fibrotic disorders and tissue remodeling. | ||||||
Curcumin | 458-37-7 | sc-200509 sc-200509A sc-200509B sc-200509C sc-200509D sc-200509F sc-200509E | 1 g 5 g 25 g 100 g 250 g 1 kg 2.5 kg | $36.00 $68.00 $107.00 $214.00 $234.00 $862.00 $1968.00 | 47 | |
Curcumin is a natural compound with anti-inflammatory and anti-fibrotic properties. It might influence Col1A2 expression by modulating TGF-β signaling or other pathways. Its potential mechanisms of action could involve interfering with profibrotic processes, leading to reduced collagen production. | ||||||
D-Galactose | 59-23-4 | sc-202564 | 100 g | $224.00 | 4 | |
Galactose is a simple sugar that has been proposed to affect collagen production. Its exact mechanism is unclear, but it might disrupt collagen maturation and assembly, potentially leading to altered Col1A2 expression and collagen synthesis. This could offer insights into novel approaches for managing collagen-related disorders. | ||||||