CRYBA4 Antibody - BSA Free

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.

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

We have publications tested in 1 confirmed species: Human.

We have publications tested in 1 application: WB.

Showing Publication 1 - 1 of 1.

Publication using NBP1-32741	Applications	Species
Li D, Jing Q, Jiang Y The identification and characterization of the p.G91 deletion in CRYBA1 in a Chinese family with congenital cataracts BMC Med. Genet. 2019-09-05 [PMID: 31488069] (WB, Human)	WB	Human

Array NBP1-32741

• CRYBA4 Antibodies
• CRYBA4 Lysate
• CRYBA4 Proteins