The Beta-Crystallin S Polyclonal Antibody (CAB7888) is a powerful tool for researchers studying beta-crystallin S, a key protein found in the lens of the eye and implicated in maintaining lens transparency and proper vision. This antibody, generated in rabbits, exhibits high specificity and sensitivity in detecting beta-crystallin S in human samples, making it an invaluable resource for studies involving eye development, cataract formation, and age-related vision problems.With its ability to recognize and bind to beta-crystallin S, this antibody enables precise visualization and analysis of the protein in various experimental systems, including Western blot assays. Its versatility and reliability make it well-suited for investigations into the molecular mechanisms underlying lens function and dysfunction, as well as potential therapeutic targets for vision-related disorders.
Beta-crystallin S is a crucial component of the lens structure, contributing to its optical properties and overall transparency. Dysregulation or mutations in this protein have been linked to the development of cataracts and other vision impairments, emphasizing the importance of studying its role in maintaining ocular health. By using the Beta-Crystallin S Polyclonal Antibody, researchers can further elucidate the function of beta-crystallin S and its involvement in vision-related conditions, ultimately paving the way for novel treatment strategies and preventive measures.
Product Name:
CRYGS Rabbit Polyclonal Antibody
SKU:
CAB7888
Size:
20uL, 100uL
Isotype:
IgG
Host Species:
Rabbit
Reactivity:
Human,Mouse,Rat
Immunogen:
Recombinant fusion protein containing a sequence corresponding to amino acids 1-178 of human CRYGS (NP_060011.1).
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.
Purification Method:
Affinity purification
Gene ID:
1427
Storage Buffer:
Store at -20℃. Avoid freeze / thaw cycles.Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3.
Western blot analysis of extracts of various cell lines, using CRYGS antibody (CAB7888) at 1:4000 dilution.Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (CABS014) at 1:10000 dilution.Lysates/proteins: 25μg per lane.Blocking buffer: 3% nonfat dry milk in TBST.Detection: ECL Basic Kit (AbGn00020).Exposure time: 1s.
