CRYGD Mouse Monoclonal Antibody [Kloon ID: LBI6E11]

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]

Carrier-free (BSA/glycerol-free) CRYGD mouse monoclonal antibody, clone LBI6E11

CACA; CCA3; CCP; cry-g-D; CRYG4; CTRCT4; PCC

Homo sapiens crystallin gamma D (CRYGD), mRNA.

1421

P07320

Unconjugated

WB 1:500

Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)

Lyophilized powder (original buffer 1X PBS, pH 7.3, 8% trehalose)

Druggable Genome

Stable for 1 year at -20°C from date of shipment. For maximum recovery of product, centrifuge the original vial after thawing and opening the cap. Aliquot will be stable at 4°C short term. For long-term storage, aliquot and store at -20°C or below. Stable for 12 months at -20°C. Avoid repeated freeze-thaw cycles.

CRYGD

https://www.ncbi.nlm.nih.gov/gene/?term=1421

https://www.uniprot.org/uniprot/P07320