The CRYGS Antibody (CAB7888) is a high-quality antibody developed for reliable detection and analysis of target proteins. 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.
This antibody is validated for use in WB, ELISA applications and has demonstrated reactivity against Human, Mouse, Rat samples.
Product Name:
CRYGS Antibody
SKU:
CAB7888
Size:
100μL, 20μL
Reactivity:
Human, Mouse, Rat
Conjugate:
Unconjugated
Immunogen:
Recombinant protein (or fragment).This information is considered to be commercially sensitive.
Tested Applications:
WBELISA
Recommended Dilution:
WB
1:500 - 1:2000
ELISA
Recommended starting concentration is 1 μg/mL. Please optimize the concentration based on your specific assay requirements.
Synonyms:
CRYG8, CTRCT20, CRYGS
Positive Sample:
Mouse eye, Rat eye
Calculated MW:
21kDa
Observed MW:
21kDa
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
RRID
AB_2769054
Buffer Information
Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS containing 50% glycerol, preserved with proclin300 or sodium azide, pH 7.3.
Western blot analysis of various lysates using CRYGS Rabbit pAb (CAB7888) at 1:4000 dilution. Secondary antibody: HRP-conjugated Goat anti-Rabbit IgG (H+L) (AS014) 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.
