CRYGS 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. Gamma-crystallins are a homogeneous group of highly symmetrical, monomeric proteins typically lacking connecting peptides and terminal extensions. They are differentially regulated after early development. This gene encodes a protein initially considered to be a beta-crystallin but the encoded protein is monomeric and has greater sequence similarity to other gamma-crystallins. This gene encodes the most significant gamma-crystallin in adult eye lens tissue. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.

Other Names:
Beta-crystallin S, Gamma-S-crystallin, Gamma-crystallin S, CRYGS, CRYG8

Target/Specificity:
This CRYGS antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 133-162 amino acids from the C-terminal region of human CRYGS.

Antigen Region:
133-162

Antigen Type: Synthetic Peptide

Gene Name: CRYGS
Gene ID: 1427
Primary Accession: P22914
NCBI Accession: NP_060011.1
Other Accession: NP_060011.1
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.