Crystallin Beta A4, Recombinant Protein

CRYBA4 Human; Crystallin Beta A4 Human Recombinant; Beta-crystallin A4; Beta-A4 crystallin; CRYBA4; MCOPCT4

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

E Coli

Greater than 95.0% as determined by SDS-PAGE.

The CRYBA4 protein (1mg/ml) 20mM Tris-HCl buffer (pH8.0), 20% glycerol, 0.1M NaCl and 1mM DTT.
Sterile filtered colorless solution.

Store at 4 degree C if entire vial will be used within 2-4 weeks. Store, frozen at -20 degree C for longer periods of time. For long term storage it is recommended to add a carrier protein (0.1% HSA or BSA).Avoid multiple freeze-thaw cycles.

Small volumes of CRYBA4 recombinant protein 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.

Description: CRYBA4 Human Recombinant produced in E Coli is a single, non-glycosylated polypeptide chain containing 216 amino acids (1-196 a.a.) and having a molecular mass of 24.5kDa.CRYBA4 is fused to a 20 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Introduction: Beta-crystallin A4 (CRYBA4) is a member of the beta/gamma-crystallin family which are the dominant structural components of the vertebrate eye lens. Beta-crystallins construct aggregates of various sizes and are able to self-associate to form dimers or to form heterodimers with other beta-crystallins. The CRYBA4 gene being a beta acidic group member is part of a gene cluster with beta-B1, beta-B2, and beta-B3.

HEAT SHOCK PROTEINS; Recombinant Proteins; Crystallin

22,374 Da

crystallin, beta A4

beta-crystallin A4; beta crystallin A4 chain transcript PS; beta-A4 crystallin; crystallin, beta polypeptide A4; eye lens structural protein

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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