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C5163

Sigma-Aldrich

βL-Crystallin from bovine eye lens

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About This Item

CAS Number:
MDL number:
UNSPSC Code:
12352202
NACRES:
NA.61

biological source

bovine eye (lens)

Assay

≥95% (biuret)

form

powder

technique(s)

UV/Vis spectroscopy: suitable

impurities

Salt, essentially free

storage temp.

−20°C

General description

β-Crystallin is the most heterogeneous of the crystallin classes, with at least six different gene products, at least ten different post-translational modifications, and quaternary structure variants from dimers to octamers. However, all sequences are highly conserved through evolution.

Application

βL-Crystallin is one of the major lens proteins that aggregates under UV. A chaperone mixture of D-pathethine and N-acetyl carnosine has the ability to slow down the rate of photoaggregatin βL-Crystallin, and may be important in the prevention of cataract.

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

Regulatory Information

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J Horacio Espinoza et al.
Journal of photochemistry and photobiology. B, Biology, 167, 15-19 (2017-01-01)
The damage produced by UV-C radiation (100-280nm) in organisms and cells is a well known fact. The main reactions of proteins to UV-C radiation consist in the alteration of their secondary structures, exposure of hydrophobic residues, unfolding and aggregation. Furthermore

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