CRYBA4, Polyclonal Antibody

Beta-crystallin A4; Beta-A4 crystallin; CRYBA4

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

Polyclonal

Rabbit Ig

Rabbit

This CRYBA4 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 98-127 amino acids from the C-terminal region of human CRYBA4.

Peptide Affinity Purified Rabbit Polyclonal Antibody (Pab)

Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is purified through a protein A column, followed by peptide affinity purification.

Vial Concentration: 0.5 (lot specific)

Maintain refrigerated at 2-8 degree C for up to 6 months. For long term storage store at -20 degree C in small aliquots to prevent freeze-thaw cycles.

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].

Western Blot (WB), ELISA (EIA)

WB~~1:1000

CRYBA4 Antibody (C-term) western blot analysis in mouse stomach tissue lysates (35ug/lane).This demonstrates the CRYBA4 antibody detected the CRYBA4 protein (arrow).

22374

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

Zhou, G., et al. Mol. Vis. 16, 1019-1024 (2010) :
Zhang, X., et al. Mol. Vis. 15, 2911-2918 (2009) :
Billingsley, G., et al. Am. J. Hum. Genet. 79(4):702-709(2006)
Collins, J.E., et al. Genome Biol. 5 (10), R84 (2004) :
Mackay, D.S., et al. Am. J. Hum. Genet. 71(5):1216-1221(2002)

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