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About This Item
Form:
powder
Assay:
≥95% (biuret)
Biological source:
bovine eye (lens)
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
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
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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