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CRYBB2 Full-Length MS Protein Standard

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Product Description


NameCRYBB2 Full-Length MS Protein Standard
Cat#CPFL310125
Protein Namecrystallin, beta B2
SymbolCRYBB2
SynonymsCCA2; CRYB2; CRYB2A; CTRCT3; D22S665
AccessionNM_000496
Cytogenetic22q11.23
Amino Acid Labeled[U- 13C6, 15N4]-L-Arg and [U- 13C6, 15N2]-L-Lys
DescriptionCRYBB2 Full-Length MS Protein Standard (NP_000487), Labeled with [U- 13C6, 15N4]-L-Arginine and [U- 13C6, 15N2]-L-Lysine, was produced in human 293 cells (HEK293) with fully chemically defined cell culture medium to obtain incorporation efficiency at Creative-Proteomics. Crystallins are separated into two classes: taxon-specific, or enzyme, and ubiquitous. The latter class constitutes the major proteins of vertebrate eye lens and maintains 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 considered 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, none in the acidic group). Beta-crystallins form aggregates of different sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. This gene, a beta basic group member, is part of a gene cluster with beta-A4, beta-B1, and beta-B3. A chain-terminating mutation was found to cause type 2 cerulean cataracts.

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