Further Information
CCA2, CRYB2, CRYB2A, CTRCT3, D22S665, beta-crystallin B2, CTA-221G9.7, beta-B2 crystallin, beta-crystallin Bp, eye lens structural protein
WB: 1:500 - 1:2000
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.
PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
batch dependent
Unconjugated
Optimal dilutions/concentrations should be determined by the end user. The information provided is a guideline for product use. This product is for research use only.
Recombinant fusion protein containing a sequence corresponding to amino acids 1-205 of human CRYBB2 (NP_000487.1).
1415
crystallin beta B2
CRYBB2
Homo sapiens
Liquid
PREDICTED MOLECULAR WEIGHT:
Observed: 27kDa
Affinity purification
Other
P43320
Optimal dilutions for each application to be determined by the researcher.