CRYBA4 polyclonal (C-term), anti-human, mouse

Background:
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].

Other Names:
Beta-crystallin A4, Beta-A4 crystallin, CRYBA4

Target/Specificity:
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.

Antigen Region:
98-127

Antigen Type: Synthetic Peptide

Gene Name: CRYBA4
Gene ID: 1413
Primary Accession: P53673
NCBI Accession: NP_001877.1
Other Accession: NP_001877.1
Format: 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.