The CRYBB1 Antibody (CAB2590) is a high-quality antibody developed for reliable detection and analysis of target proteins. 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.
This antibody is validated for use in WB, ELISA applications and has demonstrated reactivity against Human, Mouse samples.
Product Name:
CRYBB1 Antibody
SKU:
CAB2590
Size:
100μL, 20μL
Reactivity:
Human, Mouse
Conjugate:
Unconjugated
Immunogen:
Recombinant protein (or fragment).This information is considered to be commercially sensitive.
Tested Applications:
WBELISA
Recommended Dilution:
WB
1:500 - 1:1000
ELISA
Recommended starting concentration is 1 μg/mL. Please optimize the concentration based on your specific assay requirements.
Synonyms:
CATCN3, CTRCT17, CRYBB1
Positive Sample:
Mouse eye
Calculated MW:
28kDa
Observed MW:
28kDa
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.
Purification Method
Affinity purification
Gene ID
1414
RRID
AB_2764475
Buffer Information
Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS containing 50% glycerol, preserved with proclin300 or sodium azide, pH 7.3.
Western blot analysis of various lysates, using CRYBB1 Rabbit pAb (CAB2590) at 1:1000 dilution. Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25μg per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (AbGn00020). Exposure time: 180s.
