| Product Name | CRYGS, 1-178aa, Human |
|---|---|
| Description | Crystallins are water soluble structural proteins found in the vertebrate eye. Mammalian crystallins are classified in three forms, designated alplha, beta and gamma. Crystallins, as the principal components of the lens, function to increase the refractive index of the eye during accommodation by forming high-molecular weight aggregates which maintain transparency. CRYGS, also known as beta-crystallin S, is exists as a monomer which does not aggregate. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation. Recombinant human CRYGS protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. |
| Synonyms | Beta-crystallin S, CRYG8 |
| Host | E.coli |
| Molecular Weight | 26.5 kDa(230aa), confirmed by MALDI-TOF (Molecular weight on SDS-PAGE will appear higher) |
| Amino Acid Sequence | MGSSHHHHHH SSGLVPRGSH MGSHMSKTGT KITFYEDKNF QGRRYDCDCD CADFHTYLSR CNSIKVEGGT WAVYERPNFA GYMYILPQGE YPEYQRWMGL NDRLSSCRAV HLPSGGQYKI QIFEKGDFSG QMYETTEDCP SIMEQFHMRE IHSCKVLEGV WIFYELPNYR GRQYLLDKKE YRKPIDWGAA SPAVQSFRRI VE |
| Tag | His-tag |
| Reactivity | Human |
| Applications | SDS-PAGE |
| Form | Liquid, in 20mM Tris-HCl buffer (pH8.0) containing 10% glycerol, 0.1M NaCl,1mM DTT |
| Concentration | 1.0 mg/ml (determined by Bradford assay) |
| Purity | > 95 % by SDS-PAGE |
| Storage | Can be stored at +4C short term (1-2 weeks). For long term storage, aliquot and store at -20C or -70C. Avoid repeated freezing and thawing cycles. |
| References |
Sun H., et al. (2005) J Med Genet. 42(9):706-10. Jester JV., et al. (2008) Semin Cell Dev Biol. 19(2):82-93. |
| Supplier | ARP |
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