Product info:

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.

Alternative names:

CRYBB2; CCA2; CRYB2; CRYB2A; CTRCT3; D22S665

Species reactivity:

Mouse, Rat

Host:

Mouse

Cellular localisation:

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Isotype:

IgG

Immunogen:

Recombinant protein of human CRYBB2

Positive control:

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AA Sequence:

Email info@sobekbio.com for sequence

Purification:

Affinity purification

Molecular weight:

Calculated MW: 23kDa Observed MW: Refer to figures

Form:

Liquid

Applications:

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Dilution:

WB 1:200 - 1:2000 IHC 1:50 - 1:200

Storage buffer:

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Storage:

Store at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.

More info:

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Orders:

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