CRYBB1 antibody (clone 2B2), anti-human
€435.00
In stock
SKU
AC-AT1642a
Catalog Number: AC-AT1642a
Size: 100 µg
Isotype: mouse IgG1 Kappa
Applications: WB, E
Request Information AC-AT1642a">Request Information
Size: 100 µg
Isotype: mouse IgG1 Kappa
Applications: WB, E
Request Information AC-AT1642a">Request Information
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.
Other Names:
Beta-crystallin B1, Beta-B1 crystallin, CRYBB1
Antigen Type:
Recombinant Protein
Gene Name: CRYBB1
Gene ID: 1414
NCBI Accession: NP_001878.1
Primary Accession: P53674
Other Accession: BC036790
Format: Clear, colorless solution in phosphate buffered saline, pH 7.2 .
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.
Other Names:
Beta-crystallin B1, Beta-B1 crystallin, CRYBB1
Antigen Type:
Recombinant Protein
Gene Name: CRYBB1
Gene ID: 1414
NCBI Accession: NP_001878.1
Primary Accession: P53674
Other Accession: BC036790
Format: Clear, colorless solution in phosphate buffered saline, pH 7.2 .
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