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Crystallins are separated into two classes taxon-specific, or enzyme, and ubiquitous. Additionally we are shipping Crystallin, beta B1 Antibodies (32) and Crystallin, beta B1 Kits (5) and many more products for this protein.
Showing 10 out of 17 products:
fundamental transcriptional regulatory mechanism of the betaB1-crystallin gene has been well conserved between humans and zebrafish
The ontogeny and localization of the alphaA-crystallin (show CRYAA Proteins) and betaB1-crystallin during embryonic lens development and regeneration indicated a different development program, although they have identical origins, the ectoderm.
Our findings highlight the importance of the C-terminus in betaB1-crystallin in maintaining the crystalline function and stability, and provide a novel insight into the molecular mechanism underlying the pathogenesis of human autosomal dominant congenital cataract.
CRYBB1 partial duplication ad complete duplication of CRYBA4 (show CRYbA4 Proteins) identified in a family with autosomal dominant congenital cataract.
Molecular dynamic simulation studies indicated that the mutation decreased the subunit binding energy and modified the distribution of surface electrostatic potentials. More importantly, the mutation separated two interacting loops in the C-terminal domain, which shielded the hydrophobic core from solvent in native betaB1-crystallin.
Congenital microcornea-cataract syndrome-causing mutation X253R increases betaB1-crystallin hydrophobicity to promote aggregate formation
Despite the disruption of betaB1-crystallin assembly, the thermal stability of betaB1-crystallin was increased by the mutation accompanied by the reduction of thermal aggregation at high temperatures
study identified a novel heterozygous p.Ser129Arg mutation in CRYBB1 in a congenital cataract-microcornea syndrome family of Chinese origin
Analyses of 20 Chinese families with hereditary nuclear congenital cataract revealed 3 novel mutations. Two of these mutations (V146M and I21N) affected betaB2-crystallin (CRYBB2 (show CRYbB2 Proteins)). One mutation (R233H) was detected in betaB1-crystallin (CRYBB1).
Variant alleles of the CRYBB1 and CRYBB2 (show CRYbB2 Proteins) genes were found, none are considered pathogenic.
Mutation G220X is associated with autosomal dominant cataract.
Removal of the N-terminal extension of beta B1-crystallin has major effects on the physical properties of the protein by increasing the self-association potential and by blocking heteromolecular associations with beta A3-crystallin (show CRYBA1 Proteins).
Tissue expression analysis indicated that that swine SDHB (show SDHB Proteins), SNRPA (show SNRPA Proteins) and CRYBB1 genes were differentially expressed in tissues including fat, lung, muscle, small intestine, kidney, large intestine, spleen and liver.
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.
crystallin, beta B1
, crystallin B1
, beta B1 crystallin
, beta-B1 crystallin
, beta-crystallin B1
, eye lens structural protein
, beta crystallin subunit beta B1