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]

Specificity:

crystallin gamma C

Alternative names:

CCL; CRYG3; CTRCT2

Species reactivity:

Human, Mouse, Rat

Host:

Mouse

Ig type:

PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Immunogen:

Full length human recombinant protein of human CRYGC (NP_066269) produced in HEK293T cell.

Purification & Purity:

Purified from mouse ascites fluids or tissue culture supernatant by affinity chromatography (protein A/G)

Molecular weight:

20.7 kDa(Predicted)

Applications:

WB

Usage:

WB 1:2000

Storage:

PBS (PH 7.3) containing 1% BSA, 50% glycerol and 0.02% sodium azide.

Precautions:

For research use only, not for use in diagnostic procedure.

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