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ALX-201-191 Revised 07-May-08
αA-Crystallin (human) (recombinant)
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SYNONYMS CRYAA (human) (recombinant)
PRODUCT LINE Stress & Heat Shock Proteins
PRODUCT CATEGORY Small Heat Shock Proteins / Related Products
Ordering Information
Product Numbers: Format: Size: Unit Price: Quantity: Add To Cart
ALX-201-191-C100   100 µg 125.00 USD Add To Cart
Product Specification
MW: ~19.9kDa.
SOURCE/HOST: Produced in E. coli.
CONCENTRATION: 1mg/ml
PURITY: ≥95% (SDS-PAGE)
FORMULATION: Liquid. In 20mM TRIS-HCl, pH 7.5, containing 50mM sodium chloride and 1mM EDTA.
SHIPPING: SHIPPED ON BLUE ICE
LONG TERM STORAGE: -20°C
HANDLING: Avoid freeze/thaw cycles.
Product Images
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General Information
α-crystallins are composed of two gene products: αA and αB, for acidic and basic, respectively. α-crystallins can be induced by heat shock and are members of the family of small heat shock proteins (sHSP also known as the HSP20). They act as molecular chaperones and form large soluble heteroaggregates of 30-40 αA and αB subunits in a 3:1 ratio. α-crystallins also have an autokinase activity and participation in the intracellular architecture. αA-crystallin is preferentially expressed in the lens cell.
General Literature References
Alpha-crystallin regions affected by adenosine 5'-triphosphate identified by hydrogen-deuterium exchange: A. Hasan, et al.; Biochemistry 41, 15876 (2002) Abstract
A positive charge preservation at position 116 of alpha A-crystallin is critical for its structural and functional integrity: S. Bera, et al.; Biochemistry 41, 12421 (2002) Abstract
Suppression of DTT-induced aggregation of abrin by alphaA- and alphaB-crystallins: a model aggregation assay for alpha-crystallin chaperone activity in vitro: G.B. Reddy, et al.; FEBS Lett. 522, 59 (2002) Abstract
The R116C mutation in alpha A-crystallin diminishes its protective ability against stress-induced lens epithelial cell apoptosis: U.P. Andley, et al.; J. Biol. Chem. 277, 10178 (2002) Abstract; Full Text
Further Categories Containing This Product:
Recombinant Proteins / Fusion Proteins
 
 

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