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CRYBB1


Official Full Name
crystallin beta B1
Organism
Homo sapiens
Gene ID
1414
Background
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, undergoes extensive cleavage at its N-terminal extension during lens maturation. It is also a member of a gene cluster with beta-A4, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]
Synonyms
CATCN3; CTRCT17

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SHG201085 shRNA set against Human CRYBB1(NM_001887.3) Inquiry
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Cat.No. Product Name Price
CDFH004292 Human CRYBB1 cDNA Clone(NM_001887.3) Inquiry
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CDCR050888 Mouse Crybb1 ORF clone (NM_023695.2) Inquiry
CDCR281799 Human CRYBB1 ORF Clone(NM_001887.3) Inquiry
CDCR377791 Rat Crybb1 ORF Clone(NM_012936.2) Inquiry
CDCS410498 Human CRYBB1 ORF Clone (BC036790) Inquiry
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