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C4413 Sigma-Aldrich

γ-Crystallin from bovine eye lens

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Properties

Related Categories Biochemicals and Reagents, Crystallin, Proteins and Derivatives, Structural Proteins
biological source   bovine eye (lens)
form   solid
impurities   Salt, essentially free
storage temp.   −20°C
Gene Information   bovine ... CRYGB(281720), CRYGC(281722), CRYGD(281723)

Description

Biochem/physiol Actions

γ-Crystallin is a natural substrate for the small heat-shock protein and molecular chaperone α-crystallin. γ-Crystallin competes with Cu2+ and Zn2+ for binding to α-crystallin, reducing the latter′s chaperone capacity.

Preparation Note

Further purified from the BO-5 fraction of Chiou, S., et al., to remove βs-crystallin.

Safety & Documentation

Safety Information

Personal Protective Equipment 
RIDADR 
NONH for all modes of transport
WGK Germany 
3

Documents

Certificate of Analysis (COA)

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Protocols & Articles
Peer-Reviewed Papers
15

References

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