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Product Description
CRYGD Antibody | 19-828 | ProSci
Host: Rabbit
Reactivity: Human, Mouse, Rat
Homology: N/A
Immunogen: Recombinant fusion protein containing a sequence corresponding to amino acids 18-117 of human CRYGD (NP_008822.2) .
Research Area: Neuroscience
Tested Application: WB
Application: WB: 1:500 - 1:2000
Specificiy: N/A
Positive Control 1: BT-474
Positive Control 2: HepG2
Positive Control 3: SW620
Positive Control 4: Raji
Positive Control 5: Mouse liver
Positive Control 6: N/A
Molecular Weight: Observed: 26kDa
Validation: N/A
Isoform: N/A
Purification: Affinity purification
Clonality: Polyclonal
Clone: N/A
Isotype: IgG
Conjugate: Unconjugated
Physical State: Liquid
Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.
Concentration: N/A
Storage Condition: Store at -20˚C. Avoid freeze / thaw cycles.
Alternate Name: Gamma-crystallin D, Gamma-D-crystallin, Gamma-crystallin 4, CRYGD, CRYG4
User Note: Optimal dilutions for each application to be determined by the researcher.
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. Four gamma-crystallin genes (gamma-A through gamma-D) and three pseudogenes (gamma-E, gamma-F, gamma-G) are tandemly organized in a genomic segment as a gene cluster. Whether due to aging or mutations in specific genes, gamma-crystallins have been involved in cataract formation.
