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. Source: Recombinant protein corresponding to aa1-252 of human CRYBB1, fused to His-tag at C-terminal expressed in E. coli. Molecular Weight: ~29.1kD Amino Acid Sequence: MSQAAKASAS ATVAVNPGPD TKGKGAPPAG TSPSPGTTLA PTTVPITSAK AAELPPGNYR LVVFELENFQ GRRAEFSGEC SNLADRGFDR VRSIIVSAGP WVAFEQSNFR GEMFILEKGE YPRWNTWSSS YRSDRLMSFR PIKMDAQEHK ISLFEGANFK GNTIEIQGDD APSLWVYGFS DRVGSVKVSS GTWVGYQYPG YRGYQYLLEP GDFRHWNEWG AFQPQMQSLR RLRDKQWHLE GSFPVLATEP PKRSHHHHHH Storage and Stability: May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for 6 months after receipt at -20C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.
