C4163
α-Crystallin from bovine eye lens
lyophilized powder
Synonym(e):
alpha-Crystallin
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About This Item
Empfohlene Produkte
Biologische Quelle
bovine eye (lens)
Qualitätsniveau
Assay
≥70% (biuret)
Form
lyophilized powder
Methode(n)
cell culture | mammalian: suitable
Lagertemp.
−20°C
Angaben zum Gen
bovine ... CRYAA(281718) , CRYAB(281719)
Anwendung
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. Wirkung
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.
Lagerklassenschlüssel
11 - Combustible Solids
WGK
WGK 3
Flammpunkt (°F)
Not applicable
Flammpunkt (°C)
Not applicable
Persönliche Schutzausrüstung
Eyeshields, Gloves, type N95 (US)
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Axel Leppert et al.
Protein science : a publication of the Protein Society, 31(8), e4378-e4378 (2022-07-29)
Molecular chaperones are essential to maintain proteostasis. While the functions of intracellular molecular chaperones that oversee protein synthesis, folding and aggregation, are established, those specialized to work in the extracellular environment are less understood. Extracellular proteins reside in a considerably
Raju Timsina et al.
Experimental eye research, 202, 108337-108337 (2020-11-01)
It is well-studied that the significant factor in cataract formation is the association of α-crystallin, a major eye lens protein, with the fiber cell plasma membrane of the eye lens. The fiber cell plasma membrane of the eye lens consists
Binding of Alpha-Crystallin to Cortical and Nuclear Lens Lipid Membranes Derived from a Single Lens.
Timsina, et al.
International Journal of Molecular Sciences, 23 (2023)
Laxman Mainali et al.
Current eye research, 46(2), 185-194 (2020-06-23)
Purpose/Aim: The amount of membrane-bound α-crystallin increases significantly with age and cataract formation, accompanied by a corresponding decline in the level of α-crystallin in the lens cytoplasm. The purpose of this research is to evaluate the binding affinity of α-crystallin
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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