The chemicals identified as HAPLN3 Activators are understood to influence the extracellular matrix (ECM) composition and dynamics, subsequently affecting the expression or function of HAPLN3 indirectly. These compounds either contribute to the biosynthesis of ECM components or modulate enzymes and pathways that maintain the ECM, which HAPLN3 is a part of. For instance, vitamin C's role in collagen synthesis, copper's role as a cofactor for enzymes cross-linking collagen, and manganese's necessity for glycosaminoglycan synthesis all contribute to an ECM environment where HAPLN3 function is necessary. Similarly, glucosamine and chondroitin sulfate supplementation provides substrates for the assembly of proteoglycan aggregates, and the presence of hyaluronic acid signals the requirement for HAPLN3, which acts as an interfacing element.
In parallel, the modulation of signaling molecules and matrix components, such as lysophosphatidic acid and fibronectin fragments, impacts fibroblast behavior and ECM synthesis. These activities can result in enhanced demand for ECM structural integrity and complexity, thereby possibly leading to increased expression of HAPLN3 to fulfill the structural role within the matrix. Zinc, with its effect on matrix metalloproteinases, also reflects the tight regulation of ECM remodeling, where HAPLN3 may be implicated.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Retinoic Acid, all trans | 302-79-4 | sc-200898 sc-200898A sc-200898B sc-200898C | 500 mg 5 g 10 g 100 g | $66.00 $325.00 $587.00 $1018.00 | 28 | |
Retinoic acid modulates gene expression through the retinoic acid receptor (RAR) pathway, which can lead to the synthesis of extracellular matrix components, including potentially HAPLN3. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $46.00 | 5 | |
Vitamin C enhances the hydroxylation of proline residues during collagen synthesis, which may stabilize the extracellular matrix and could increase the need for HAPLN3 as a stabilizing linker. | ||||||
Copper(II) sulfate | 7758-98-7 | sc-211133 sc-211133A sc-211133B | 100 g 500 g 1 kg | $46.00 $122.00 $189.00 | 3 | |
Copper is a cofactor for lysyl oxidase, an enzyme that cross-links collagen and elastin in the extracellular matrix; stabilization of the matrix might require enhanced HAPLN3 activity for structural integrity. | ||||||
Manganese(II) chloride beads | 7773-01-5 | sc-252989 sc-252989A | 100 g 500 g | $19.00 $31.00 | ||
Manganese is essential for glycosaminoglycan synthesis, part of the proteoglycan complex with which HAPLN3 interacts; its presence can lead to a demand for HAPLN3. | ||||||
Sodium selenite | 10102-18-8 | sc-253595 sc-253595B sc-253595C sc-253595A | 5 g 500 g 1 kg 100 g | $49.00 $183.00 $316.00 $98.00 | 3 | |
Selenium is a cofactor for antioxidant enzymes that protect the extracellular matrix; a healthy matrix might upregulate the expression of link proteins like HAPLN3. | ||||||
Chondroitin Sulfate, Bovine | 9007-28-7 | sc-203888 | 5 g | $94.00 | 1 | |
Chondroitin sulfate is another component of the proteoglycan matrix; its abundance can signal a cellular need for more HAPLN3 to maintain matrix structure. | ||||||
Hyaluronic acid | 9004-61-9 | sc-337865 | 10 mg | $208.00 | ||
As a major component of the extracellular matrix, the presence of hyaluronic acid can signal a requirement for HAPLN3, which links proteoglycans to hyaluronan. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $48.00 | ||
Zinc influences matrix metalloproteinases and tissue inhibitors of metalloproteinases; balanced zinc levels can contribute to a stable extracellular matrix, which may require HAPLN3 function. | ||||||
Lysophosphatidic Acid | 325465-93-8 | sc-201053 sc-201053A | 5 mg 25 mg | $98.00 $341.00 | 50 | |
Lysophosphatidic acid can induce fibroblast proliferation and production of extracellular matrix components, possibly necessitating an increase in HAPLN3 expression for matrix assembly. | ||||||
Fibronectin | sc-29011 sc-29011A | 1 mg 5 mg | $143.00 $504.00 | 94 | ||
Fibronectin fragments can induce matrix assembly and fibroblast spreading, potentially influencing the cellular environment to favor the synthesis of linking proteins like HAPLN3. | ||||||