Recombinant Human α-Crystallin A Chain/CRYAA

Instruction Manual!

Product name:	Recombinant Human α-Crystallin A Chain/CRYAA
Source:	E. coli
Purity:	Greater than 95% as determined by reducing SDS-PAGE.
Buffer Formulation:	Lyophilized from a 0.2 μm filtered solution of PBS, 2mM EDTA, pH 8.0.
Applications:	Applications:SDS-PAGE; WB; ELISA; IP.
Storage:	Avoid repeated freeze/thaw cycles. Store at 2-8 oC for one month. Aliquot and store at -80 oC for 12 months.
UOM:	100ug/50ug/200ug/1mg/1g

Source	E. coli
Description	Recombinant Human alpha-Crystallin A Chain is produced by our E.coli expression system and the target gene encoding Met1-Ser173 is expressed with a 6His tag at the C-terminus.
Names	Alpha-Crystallin A Chain; Heat Shock Protein Beta-4; HspB4; Alpha-Crystallin A Chain, Short Form; CRYAA; CRYA1; HSPB4
Accession #	P02489
Formulation	Lyophilized from a 0.2 μm filtered solution of PBS, 2mM EDTA, pH 8.0.
Shipping	The product is shipped at ambient temperature.
Reconstitution	Always centrifuge tubes before opening. Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100 μg/ml. Dissolve the lyophilized protein in ddH2O. Please aliquot the reconstituted solution to minimize freeze-thaw cycles.
Storage	Lyophilized protein should be stored at < -20°C, though stable at room temperature for 3 weeks. Reconstituted protein solution can be stored at 4-7°C for 2-7 days. Aliquots of reconstituted samples are stable at < -20°C for 3 months.
Purity	Greater than 95% as determined by reducing SDS-PAGE.
Endotoxin	Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.
Amino Acid Sequence	MDVTIQHPWFKRTLGPFYPSRLFDQFFGEGLFEYDLLPFLSSTISPYYRQSLFRTVLDSGISEVR SDRDKFVIFLDVKHFSPEDLTVKVQDDFVEIHGKHNERQDDHGYISREFHRRYRLPSNVDQSALS CSLSADGMLTFCGPKIQTGLDATHAERAIPVSREEKPTSAPSSLEHHHHHH
Background	Alpha-Crystallin A Chain (CRYAA) belongs to the small heat shock protein (HSP20) family and can be induced by heat shock. The expression of CRYAA is preferentially restricted to the lens cell. CRYAA may contribute to the transparency and refractive index of the lens. CRYAA has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. Two additional functions of CRYAA are an autokinase activity and participation in the intracellular architecture.