Ascorbic acid, a quintessential co-factor in collagen synthesis, ensures the hydroxylation of specific amino acid residues, a step indispensable for the structural integrity of the collagen triple helix. It acts as a guardian of collagen maturation, facilitating the proper assembly of collagen fibers encoded by genes such as COL27A1. Copper sulfate found in manganese sulfate, serve as vital cofactors for enzymes directly involved in the post-translational processing of collagen. Copper is pivotal for lysyl oxidase, which catalyzes the cross-linking of collagen fibers, thereby influencing the tensile strength and resilience of collagen structures. Manganese plays a similar role by supporting enzymes such as prolidase, thus ensuring the efficient recycling of proline for collagen synthesis, which indirectly sustains the production of COL27A1 collagen.
Certain compounds like beta-aminopropionitrile and D-penicillamine, known to interact with the enzymatic pathways of collagen cross-linking, present an indirect method of modulating the synthesis and organization of collagen. By disrupting the normal cross-linking process, they may inadvertently prompt a compensatory increase in collagen production, including the type produced by COL27A1. Phospholipids such as 1,2-Dioleoyl-sn-glycero-3-phosphocholine (DOPC) alter membrane fluidity, potentially influencing intracellular signaling cascades that govern protein synthesis. Such alterations in membrane dynamics can have cascading effects on the expression and stabilization of collagen, including those formed by COL27A1. Retinoic acid, with its gene expression modulation capabilities, can also upregulate or alter the synthesis of collagen proteins by influencing the transcriptional machinery. The oxidative environment within cells, marked by compounds like oxidized glutathione, and signaling molecules such as lysophosphatidic acid, spermidine, leptin, and genistein, can initiate a variety of responses that include the remodeling of extracellular matrix components.
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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 | |
Necessary for the hydroxylation of proline and lysine residues during collagen synthesis, ascorbic acid can promote COL27A1 activity by ensuring proper collagen maturation. | ||||||
ALK5 Inhibitor II | 446859-33-2 | sc-221234 sc-221234A sc-221234B sc-221234C sc-221234D sc-221234E sc-221234F | 1 mg 5 mg 10 mg 50 mg 100 mg 500 mg 1 g | $75.00 $150.00 $215.00 $650.00 $1224.00 $4296.00 $7818.00 | 8 | |
Although not a chemical, TGF-β is a significant enhancer of collagen synthesis, and chemicals that modulate TGF-β signaling can indirectly increase COL27A1 activity. | ||||||
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, an enzyme responsible for the cross-linking of collagen molecules, which may support the stabilization and function of COL27A1-related collagen structures. | ||||||
Manganese(II) sulfate monohydrate | 10034-96-5 | sc-203130 sc-203130A | 100 g 500 g | $40.00 $105.00 | ||
Manganese is a cofactor for prolidase, an enzyme involved in collagen synthesis, and may assist in the post-translational processing of collagen, including that encoded by COL27A1. | ||||||
3-Aminopropionitrile | 151-18-8 | sc-266473 | 1 g | $102.00 | ||
An inhibitor of lysyl oxidase, this compound can disrupt normal collagen cross-linking, indirectly affecting the turnover and potentially the synthesis of collagen types, including COL27A1. | ||||||
Penicillamine | 52-67-5 | sc-205795 sc-205795A | 1 g 5 g | $45.00 $94.00 | ||
Known to interfere with collagen cross-linking, it may upregulate collagen synthesis as a compensatory mechanism, potentially increasing COL27A1 activity. | ||||||
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 | |
By modulating gene expression, retinoic acid can influence the synthesis of various proteins, including collagens, and may affect the expression of COL27A1. | ||||||
Glutathione, oxidized | 27025-41-8 | sc-29093B sc-29093A sc-29093 | 250 mg 1 g 5 g | $57.00 $82.00 $270.00 | 3 | |
As an indicator of oxidative stress, GSSG can alter cell signaling pathways, which may include responses that upregulate collagen synthesis, potentially affecting COL27A1. | ||||||
Lysophosphatidic Acid | 325465-93-8 | sc-201053 sc-201053A | 5 mg 25 mg | $96.00 $334.00 | 50 | |
LPA can activate cellular signaling cascades that influence various biological processes, including the expression of extracellular matrix components like collagens. | ||||||
Spermidine | 124-20-9 | sc-215900 sc-215900B sc-215900A | 1 g 25 g 5 g | $56.00 $595.00 $173.00 | ||
Spermidine has been linked to autophagy and other cellular processes that could influence the turnover and synthesis of collagen, potentially affecting COL27A1. | ||||||