CRYGA Recombinant Rabbit mAb
Product Specifications
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. [provided by RefSeq, Jul 2008]
CAS Number
9000-83-3
Structure Composition
Store at -20°C. Supplied in 50mM Tris-Glycine (pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA. Stable for 12 months from date of receipt.
Product Name Alternative
CRYG1; CRYG5; CRY-g-A
Swiss Prot
P11844
Reactivity
Human, Mouse, Rat
Immunogen
Recombinant protein of human CRYGA
Conjugation
Unconjugated
Applications
WB
Dilution
WB: 1:1000
Purity
Affinity Purification
Modification
Unmodification
Molecular Weight
21 kDa
Storage Conditions
Store at 4°C short term. Aliquot and store at -20°C long term. Avoid freeze-thaw cycles.
Notes
For research use only, not for use in diagnostic procedure.
Specificity
IgG
Host or Source
Rabbit
Available Sizes
Frequently Asked Questions
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