C4163
α-Crystallin from bovine eye lens
lyophilized powder
Synonym(e):
alpha-Crystallin
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About This Item
Empfohlene Produkte
Biologische Quelle
bovine eye (lens)
Qualitätsniveau
Assay
≥70% (biuret)
Form
lyophilized powder
Methode(n)
cell culture | mammalian: suitable
Lagertemp.
−20°C
Angaben zum Gen
bovine ... CRYAA(281718) , CRYAB(281719)
Anwendung
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.
Biochem./physiol. Wirkung
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.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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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
Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.
Timsina, et al.
International Journal of Molecular Sciences, 23 (2023)
Axel Leppert et al.
Protein science : a publication of the Protein Society, 31(8), e4378-e4378 (2022-07-29)
Molecular chaperones are essential to maintain proteostasis. While the functions of intracellular molecular chaperones that oversee protein synthesis, folding and aggregation, are established, those specialized to work in the extracellular environment are less understood. Extracellular proteins reside in a considerably
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)
P Anil Kumar et al.
Molecular vision, 11, 561-568 (2005-08-10)
A decline in the chaperone-like activity of eye lens alpha-crystallin in diabetic conditions has been reported. In this study, we investigated whether curcumin, a dietary antioxidant, can manipulate the chaperone-like activity of alpha-crystallin in diabetic rat lens. A group of
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