Recombinant humaan Crystalline beta B1/CRYBB1-eiwit

Crystallins are the major structural proteins of the vertebrate eye lens, where they maintain the transparency and refractive index of the lens. Crystallins are divided into alpha, beta, and gamma families. Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins. CRYBB1 is a beta basic group member and undergoes extensive cleavage at its N-terminal extension during lens maturation. Recombinant human CRYBB1 protein, fused to His-tag at C-terminus was expressed in E. coli and purified by using conventional chromatography techniques.

Crystallin beta B1, Beta-B1 crystallin, Beta-crystallin B1, CATCN3, CTRCT17

E.coli

Human

His-Tag

SDS-PAGE

1 mg/mL (determined by Bradford assay)

> 90% by SDS-PAGE

29.1 kDa (260aa) confirmed by MALDI-TOF

B-crystallin B1, CRYBB1, Beta-crystallin B1, CATCN3., Beta-crystallin B1 Beta crystallin B1, CRYBB 1, CRYBB1, Crystallin beta B1, Eye lens structural protein, OTTHuMP00000028719., ATGP0584-10 µg, ATGP0584-20 µg, ATGP0584-50 µg, ATGP0584-100 µg, ATGP0584-250 µg, ATGP0584-500 µg, ATGP0584-1 mg, ATGP0584-10, ATGP0584-20, ATGP0584-50, ATGP0584-100, ATGP0584-250, ATGP0584-500, ATGP0584-1

Hulsebos TJ., et al. (1995) Genomics. 29 (3) :712-8. ; ; Annunziata O., et al. (2005) Biochemistry. 44 (4) :1316-28. ;

Can be stored at 2°C to 8°C for 1 week. For long term storage, aliquot and store at -20C to -80C. Avoid repeated freezing and thawing cycles.

Liquid in. 20 mM Tris-HCl buffer (pH 8.0) containing 10% glycerol 1mM DTT

Neuroscience

NP_001878

P53674

Human