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Merck
CN

C4163

α-Crystallin from bovine eye lens

lyophilized powder

Synonym(s):

alpha-Crystallin

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About This Item

CAS Number:
UNSPSC Code:
12352202
NACRES:
NA.61
MDL number:
Form:
lyophilized powder
Assay:
≥70% (biuret)
Biological source:
bovine eye (lens)
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biological source

bovine eye (lens)

assay

≥70% (biuret)

form

lyophilized powder

technique(s)

cell culture | mammalian: suitable

UniProt accession no.

storage temp.

−20°C

Quality Level

Gene Information

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.

Biochem/physiol Actions

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.

Storage Class

11 - Combustible Solids

wgk

WGK 3

flash_point_f

Not applicable

flash_point_c

Not applicable

ppe

Eyeshields, Gloves, type N95 (US)

Regulatory Information

监管及禁止进口产品
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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.
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
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
Jakob Bunkenborg et al.
Proteomics, 16(4), 545-553 (2015-12-09)
Proteomic identifications hinge on the measurement of both parent and fragment masses and matching these to amino acid sequences via database search engines. The correctness of the identifications is assessed by statistical means. Here we present an experimental approach to

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