COL1A1 Activators
COL1A1 activators constitute a diverse array of chemicals that play a crucial role in the regulation and modification of the collagen type I alpha 1 chain, which is a primary component of type I collagen-the most abundant collagen of the human body. This group of chemicals does not directly interact with the collagen protein itself but influences the various cellular processes and enzymatic pathways that lead to the synthesis, assembly, and post-translational modification of COL1A1. These modifications are essential for the proper formation of the collagen triple helix structure, which is vital for the tensile strength and structural integrity of connective tissues. The activators can include vitamins, trace elements, and other organic and inorganic compounds that serve as cofactors or inhibitors of enzymes directly involved in the biosynthesis of collagen. For example, ascorbic acid (vitamin C) is a well-established molecule that is required for the hydroxylation of proline residues in COL1A1, a step that is catalyzed by the enzyme prolyl hydroxylase. This hydroxylation is critical for the stabilization of the collagen helix.
Moreover, certain activators are involved in the regulation of gene expression related to COL1A1, influencing the rate at which the gene is transcribed. Others may interact with signaling pathways that govern the proliferation and differentiation of cells that produce collagen, such as fibroblasts. There are also compounds that act as chelators, binding to metal ions that serve as essential cofactors for enzymes like lysyl oxidase, which is responsible for the cross-linking of collagen fibers-an important step in strengthening the extracellular matrix. By modulating the activity of these enzymes, COL1A1 activators can indirectly affect the maturation and organization of collagen fibers. Additionally, some chemicals within this class serve to regulate the turnover and recycling of collagen by influencing proteolytic enzymes and their inhibitors.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $45.00 | 5 | |
Ascorbic acid is crucial for the hydroxylation of proline residues in collagen by prolyl hydroxylase. This post-translational modification is essential for the stability and triple helical structure of collagen. Thus, ascorbic acid indirectly enhances the function of COL1A1 by promoting proper collagen formation. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $45.00 $120.00 $185.00 | 3 | |
Copper is a cofactor for lysyl oxidase, which is involved in the cross-linking of collagen molecules. Adequate levels of copper can enhance the activity of lysyl oxidase, indirectly increasing the functional activity of COL1A1 by facilitating proper collagen cross-linking. | ||||||
Manganese(II) chloride beads | 7773-01-5 | sc-252989 sc-252989A | 100 g 500 g | $19.00 $30.00 | ||
Manganese is an essential cofactor for the enzyme prolidase, which is involved in collagen turnover and recycling. By supporting prolidase activity, manganese indirectly supports the synthesis and function of COL1A1 in the extracellular matrix remodeling. | ||||||
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 | $26.00 $92.00 $120.00 $310.00 $500.00 $908.00 $1821.00 | 46 | |
Genistein can inhibit tyrosine kinases which are involved in the downstream signaling of various cellular processes, including collagen synthesis. By this action, genistein can indirectly enhance the functional activity of COL1A1 by upregulating the synthesis of collagen. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $45.00 $94.00 | ||
D-Penicillamine works by chelating copper, which may lead to reduced activity of lysyl oxidase, thereby affecting collagen cross-linking. This can cause an upregulation of collagen synthesis as a compensatory mechanism, indirectly enhancing COL1A1 activity. | ||||||
(S)-(−)-Blebbistatin | 856925-71-8 | sc-204253 sc-204253A sc-204253B sc-204253C | 1 mg 5 mg 10 mg 25 mg | $71.00 $260.00 $485.00 $949.00 | ||
LPA acts on its receptors to induce a variety of cellular responses, including cell proliferation and survival. These responses can lead to increased synthesis of extracellular matrix components, such as COL1A1, to support new cell growth. | ||||||
D-erythro-Sphingosine-1-phosphate | 26993-30-6 | sc-201383 sc-201383D sc-201383A sc-201383B sc-201383C | 1 mg 2 mg 5 mg 10 mg 25 mg | $162.00 $316.00 $559.00 $889.00 $1693.00 | 7 | |
S1P interacts with its receptors to promote cellular activities that include differentiation and survival. These processes can enhance the production of extracellular matrix proteins, including COL1A1, thereby indirectly enhancing its functional activity. | ||||||
Calcium chloride anhydrous | 10043-52-4 | sc-207392 sc-207392A | 100 g 500 g | $65.00 $262.00 | 1 | |
Calcium ions are essential for various cellular processes, including those involved in the synthesis and secretion of extracellular matrix proteins. By supporting these cellular functions, calcium chloride can indirectly enhance the production and function of COL1A1. | ||||||
Retinoic Acid, all trans | 302-79-4 | sc-200898 sc-200898A sc-200898B sc-200898C | 500 mg 5 g 10 g 100 g | $65.00 $319.00 $575.00 $998.00 | 28 | |
Retinoic acid influences gene expression and is involved in cell growth and differentiation. It can indirectly enhance COL1A1 activity by promoting the differentiation of cells that produce collagen, thereby increasing the synthesis of the protein. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc is crucial for the function of multiple enzymes and transcription factors that are involved in collagen synthesis. Adequate zinc levels can enhance the synthesis and incorporation of COL1A1 into the extracellular matrix. | ||||||