83-6035-53　CRYBA2 (Crystallin, beta A2) 50ul　244951

特徴

• Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous.
• The latter class constitutes the major proteins of the vertebrate eye, which function to maintain the transparency and refractive index of the lens.
• Since lens central fiber cells lose their nuclei during development, these crystallins are made and then retained throughout life, making them extremely stable proteins.
• Mammalian lens crystallins are divided into alpha, beta, and gamma families; beta and gamma crystallins are also defined as a superfamily.
• Alpha and beta families are further divided into acidic and basic groups.
• Seven protein regions exist in crystallins: four homologous motifs, a connecting peptide, and N- and C-terminal extensions.
• Beta-crystallins, the most heterogeneous, differ by the presence of the C-terminal extension (present in the basic group but absent in the acidic group).
• Beta-crystallins form aggregates of different sizes and are able to form homodimers through self-association or heterodimers with other beta-crystallins.
• This gene is a beta acidic group member.
• Three alternatively spliced transcript variants encoding identical proteins have been reported.
• [provided by RefSeq
• Applications:Suitable for use in Western Blot.
• Other applications not tested.
• Recommended Dilution:Optimal dilutions to be determined by the researcher.
• AA Sequence:MSSAPAPGPAPASLTLWDEEDFQGRRCRLLSDCANVCERGGLPRVRSVKVENGVWVAFEYPDFQGQQFILEKGDYPRWSAWSGSSSHNSNQLLSFRPVLCANHNDSRVTLFEGDNFQGCKFDLVDDYPSLPSMGWASKDVGSLKVSSGAWVAYQYPGYRGYQYVLERDRHSGEFCTYGELGTQAHTGQLQSIRRVQH
• Storage and Stability:May be stored at 4℃ for short-term only.
• Aliquot to avoid repeated freezing and thawing.
• Store at -20℃.
• Aliquots are stable for 12 months.
• For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.