γS-crystallin is an intrinsic component of the vertebrate eye lens, contributing significantly to its transparency and refractive properties. This protein belongs to the βγ-crystallin superfamily, which is characterized by its high stability and solubility, essential features for the maintenance of lens clarity throughout the life of an organism. The γS-crystallin gene is expressed during lens development, and its protein product is then meticulously packed within the lens fibers, contributing to the precise optical function of the eye. A delicate balance in the expression of γS-crystallin is crucial; it must be sufficient to sustain lens transparency but also carefully regulated to avoid aggregation that could lead to cataract formation. The stability of γS-crystallin is a testament to its evolutionary refinement, allowing it to withstand the protein-denaturing conditions that can occur over decades of an organism's lifespan.
The expression of γS-crystallin can be influenced by various cellular and molecular cues within the ocular environment. Research has identified several compounds that could play a role in the upregulation of this protein, although the exact mechanisms are not fully elucidated. Compounds such as hydrogen peroxide can create a state of oxidative stress, potentially triggering a protective cellular response that includes the synthesis of γS-crystallin. Other molecules like retinoic acid, which is crucial for eye development, might also signal the need for increased production of γS-crystallin during critical growth phases. Nutrient-derived molecules, including vitamins C and E, are known for their antioxidant properties and could support the expression of γS-crystallin to counterbalance oxidative stress in the lens. Trace elements like zinc and selenium are integral to various cellular functions, and their presence could signal the cellular machinery to produce proteins that are essential for maintaining lens transparency and integrity, including γS-crystallin. While the potential of these compounds to act as activators for γS-crystallin expression is grounded in their known biological roles, direct evidence linking them to the control of this specific protein's expression is an area ripe for further scientific exploration.
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| Product Name | CAS # | Catalog # | QUANTITY | Price | Citations | RATING |
|---|---|---|---|---|---|---|
Hydrogen Peroxide | 7722-84-1 | sc-203336 sc-203336A sc-203336B | 100 ml 500 ml 3.8 L | $30.00 $60.00 $93.00 | 27 | |
Hydrogen peroxide can provoke an oxidative environment, potentially triggering a cellular defense response that upregulates protective proteins such as γS-crystallin to combat potential oxidative damage in the lens. | ||||||
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, a metabolite of vitamin A, plays a pivotal role in eye development and could specifically stimulate γS-crystallin expression as part of the differentiation process in lens fiber cells. | ||||||
Tauroursodeoxycholic Acid, Sodium Salt | 14605-22-2 | sc-281165 | 1 g | $644.00 | 5 | |
This bile acid may exert a stabilizing effect on cellular proteins, potentially increasing the synthesis of γS-crystallin to assist in maintaining lens transparency and protein homeostasis. | ||||||
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, with its anti-inflammatory properties, could upregulate the transcription of genes encoding protective proteins like γS-crystallin as a response to inflammatory stress in the eye lens. | ||||||
D,L-Sulforaphane | 4478-93-7 | sc-207495A sc-207495B sc-207495C sc-207495 sc-207495E sc-207495D | 5 mg 10 mg 25 mg 1 g 10 g 250 mg | $150.00 $286.00 $479.00 $1299.00 $8299.00 $915.00 | 22 | |
DL-Sulforaphane can activate the expression of antioxidant defense genes and may specifically upregulate γS-crystallin as a part of this cellular protective response mechanism. | ||||||
Resveratrol | 501-36-0 | sc-200808 sc-200808A sc-200808B | 100 mg 500 mg 5 g | $60.00 $185.00 $365.00 | 64 | |
Resveratrol is known to activate the SIRT1 pathway, which might lead to the upregulation of γS-crystallin as a means to promote cellular resistance to stress and aging in the lens. | ||||||
Zinc | 7440-66-6 | sc-213177 | 100 g | $47.00 | ||
Zinc ions can act as a molecular signal to induce the synthesis of proteins including γS-crystallin, potentially contributing to lens clarity and anti-cataractous mechanisms. | ||||||
Selenium | 7782-49-2 | sc-250973 | 50 g | $61.00 | 1 | |
As an essential component of various antioxidant enzymes, selenium could stimulate the expression of γS-crystallin to enhance the antioxidative capacity of the lens. | ||||||
Quercetin | 117-39-5 | sc-206089 sc-206089A sc-206089E sc-206089C sc-206089D sc-206089B | 100 mg 500 mg 100 g 250 g 1 kg 25 g | $11.00 $17.00 $108.00 $245.00 $918.00 $49.00 | 33 | |
Quercetin, through its potent antioxidant activity, could trigger the upregulation of γS-crystallin to protect lens fibers against oxidative stress and to maintain lens function. | ||||||
L-Ascorbic acid, free acid | 50-81-7 | sc-202686 | 100 g | $45.00 | 5 | |
As a key water-soluble antioxidant, ascorbic acid may stimulate the expression of γS-crystallin to safeguard the lens against oxidative insults and support visual acuity. | ||||||