C4163
α-Crystallin from bovine eye lens
lyophilized powder
Synonym(s):
alpha-Crystallin
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About This Item
Recommended Products
biological source
bovine eye (lens)
Assay
≥70% (biuret)
form
lyophilized powder
technique(s)
cell culture | mammalian: suitable
storage temp.
−20°C
Gene Information
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.
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 Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Certificates of Analysis (COA)
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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.
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
Pasupulati Anil Kumar et al.
IUBMB life, 61(5), 485-495 (2009-04-25)
Cataract, loss of eye lens transparency, is the leading cause of blindness worldwide. alpha-Crystallin, initially known as one of the major structural proteins of the eye lens, is composed of two homologous subunits alphaA- and alphaB-crystallins. It is convincingly established
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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