Date published: 2026-6-4

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γD-crystallin Activators

The category of chemicals classified as γD-crystallin activators encompasses a range of compounds that, through various physicochemical mechanisms, can support the function and structural integrity of γD-crystallin. This protein is paramount in maintaining the transparency and refractive power of the eye lens, and its proper functioning is facilitated by factors that promote its stability and prevent aggregation. The assortment of chemicals within this classification does not possess a singular chemical structure or property; rather, they are defined by their capability to interact with γD-crystallin in a manner that promotes its activity. This interaction is critical, given that γD-crystallin must remain stable and functional over the lifetime of an organism, without the opportunity for renewal or replacement.

The compounds typically associated with the activation of γD-crystallin include a variety of molecular entities such as inorganic salts, osmoprotectants, cryoprotectants, and certain amino acids. Each of these compounds performs its function through a distinct pathway. Inorganic salts, for example, may fine-tune the ionic balance necessary for the proper folding of γD-crystallin, while osmoprotectants like trehalose and glycerol are known for their role in safeguarding the protein from environmental stresses that can lead to denaturation or precipitation. Amino acids such as arginine and proline are reputed to act as chemical chaperones, contributing to the solubility and stabilization of the protein, thereby averting the opacity that can disrupt lens clarity. Furthermore, antioxidants are significant in this category as they can protect γD-crystallin from oxidative damage that might otherwise lead to conformational changes and loss of function. Collectively, these activators are instrumental in sustaining the native state and activity of γD-crystallin, which is essential for the longevity and clarity of the ocular lens.

Items 1 to 10 of 11 total

Display:

Product NameCAS #Catalog #QUANTITYPriceCitationsRATING

Zinc

7440-66-6sc-213177
100 g
$48.00
(0)

Zinc ions can stabilize γD-crystallin structure, maintaining lens transparency and proper refractive function.

L-Ascorbic acid, free acid

50-81-7sc-202686
100 g
$46.00
5
(1)

Acts as an antioxidant, protecting γD-crystallin from oxidative stress which can lead to protein aggregation.

Glycerol

56-81-5sc-29095A
sc-29095
100 ml
1 L
$56.00
$153.00
12
(5)

Used as a stabilizer in protein solutions, can aid in the proper folding and stability of γD-crystallin.

Dimethyl Sulfoxide (DMSO)

67-68-5sc-202581
sc-202581A
sc-202581B
100 ml
500 ml
4 L
$31.00
$117.00
$918.00
136
(6)

May stabilize protein conformation and prevent aggregation of γD-crystallin under stress conditions.

D-(+)-Trehalose Anhydrous

99-20-7sc-294151
sc-294151A
sc-294151B
1 g
25 g
100 g
$30.00
$167.00
$260.00
2
(0)

Functions as a protein stabilizer, potentially reducing aggregation of γD-crystallin in the eye lens.

L-Arginine

74-79-3sc-391657B
sc-391657
sc-391657A
sc-391657C
sc-391657D
5 g
25 g
100 g
500 g
1 kg
$20.00
$31.00
$61.00
$219.00
$352.00
2
(0)

Can act as a chemical chaperone, potentially enhancing the solubility and stability of γD-crystallin.

L-Proline

147-85-3sc-397196
sc-397196A
sc-397196B
sc-397196C
25 g
100 g
1 kg
5 kg
$38.00
$133.00
$208.00
$978.00
(0)

Might contribute to the osmoprotection of γD-crystallin, enhancing its structural integrity.

Sodium Chloride

7647-14-5sc-203274
sc-203274A
sc-203274B
sc-203274C
500 g
2 kg
5 kg
10 kg
$19.00
$30.00
$60.00
$110.00
15
(3)

At certain concentrations, can influence the solubility and stability of lens crystallins including γD-crystallin.

Magnesium chloride

7786-30-3sc-255260C
sc-255260B
sc-255260
sc-255260A
10 g
25 g
100 g
500 g
$28.00
$35.00
$48.00
$125.00
2
(1)

Magnesium ions can support the proper folding and function of lens crystallins such as γD-crystallin.

Calcium chloride anhydrous

10043-52-4sc-207392
sc-207392A
100 g
500 g
$66.00
$262.00
1
(1)

Calcium may influence protein structure by affecting ionic interactions within γD-crystallin.