Beta-crystallin A4, Polyclonal Antibody

For Research Use Only. Not for use in diagnostic procedures.

Polyclonal

Rabbit

Purified by antigen-affinity chromatography.

Supplied in 0.1M Tris-buffered saline with 10% Glycerol (pH7.0). 0.01% Thimerosal was added as a preservative.

Store at -20 degree C for long term preservation (recommended). Store at 4 degree C for short term use.

Small volumes of anti-CRYBA4 antibody vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.

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 acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq]

Total protein Ab

Western Blot (WB), Immunofluorescence (IF)

Western blotting: 1:500-1:3000
Immunofluorescence: 1:100-1:200

Sample (30 ug of whole cell lysate)A: H1299B: HeLa12% SDS PAGEPrimary antibody diluted at 1: 1000

Immunofluorescence analysis of paraformaldehyde-fixed HeLa, using Beta-crystallin A4 antibody at 1: 200 dilution.

22,374 Da[Similar Products]

crystallin, beta A4

beta-crystallin A4

Beta-crystallin A4

CRBA4_HUMAN

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 acidic group member, is part of a gene cluster with beta-B1, beta-B2, and beta-B3. [provided by RefSeq, Jul 2008]

CRYBA4: a major structural protein of the eye lens. A member of the beta/gamma-crystallin family.

Chromosomal Location of Human Ortholog: 22q12.1

Molecular Function: structural constituent of eye lens

Biological Process: camera-type eye development; visual perception

Disease: Cataract 23

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