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C4163

Sigma-Aldrich

α-Crystallin from bovine eye lens

lyophilized powder

Synonyme(s) :

alpha-Crystallin

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About This Item

Numéro CAS:
11046-99-4
Numéro MDL:
MFCD00070939
Code UNSPSC :
12352202
Nomenclature NACRES :
NA.61

Source biologique

bovine eye (lens)

Pureté

≥70% (biuret)

Forme

lyophilized powder

Technique(s)

cell culture | mammalian: suitable

Numéro d'accès UniProt

P02470
P02510

Température de stockage

−20°C

Informations sur le gène

bovine ... CRYAA(281718) , CRYAB(281719)

Application

α-Crystallin is a lens protein that contains two homologous subunits: αA- and αB-crystallins. α-Crystallin displays chaperone-like activity and plays an important role in maintaining lens transparency. It has been noted that in diabetic conditions of rats there is a decline in the chaperone activity of α-Crystallin. Research has shown that a dietary antioxidant, curcumin, can prevent this loss of chaperone activity.

Actions biochimiques/physiologiques

α-Crystallin is a small heat-shock protein that has chaperone-like activity, preventing protein aggregation in vitro. Point mutations in α-crystallin genes are believed to be responsible for hereditary cataract development.

Code de la classe de stockage

11 - Combustible Solids

Classe de danger pour l'eau (WGK)

WGK 3

Point d'éclair (°F)

Not applicable

Point d'éclair (°C)

Not applicable

Équipement de protection individuelle

Eyeshields, Gloves, type N95 (US)

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Consulter la Bibliothèque de documents

Raju Timsina et al.
Current eye research, 47(6), 843-853 (2022-02-19)
This research aims to probe the interaction of α-crystallin with a model of human, porcine, and mouse lens-lipid membranes. Cholesterol/model of human lens-lipid (Chol/MHLL), cholesterol/model of porcine lens-lipid (Chol/MPLL), and cholesterol/model of mouse lens-lipid (Chol/MMLL) membranes with 0-60 mol% Chol were
Delay of diabetic cataract in rats by the antiglycating potential of cumin through modulation of α-crystallin chaperone activity.
Kumar PA., et al.
The Journal of Nutrition, 20, 553-562 (2009)
Raju Timsina et al.
Experimental eye research, 206, 108544-108544 (2021-03-22)
The concentration of α-crystallin decreases in the eye lens cytoplasm, with a corresponding increase in membrane-bound α-crystallin during cataract formation. The eye lens's fiber cell plasma membrane consists of extremely high cholesterol (Chol) content, forming cholesterol bilayer domains (CBDs) within
Raju Timsina et al.
Experimental eye research, 202, 108337-108337 (2020-11-01)
It is well-studied that the significant factor in cataract formation is the association of α-crystallin, a major eye lens protein, with the fiber cell plasma membrane of the eye lens. The fiber cell plasma membrane of the eye lens consists
Laxman Mainali et al.
Current eye research, 46(2), 185-194 (2020-06-23)
Purpose/Aim: The amount of membrane-bound α-crystallin increases significantly with age and cataract formation, accompanied by a corresponding decline in the level of α-crystallin in the lens cytoplasm. The purpose of this research is to evaluate the binding affinity of α-crystallin
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