Product info:

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.

Alternative names:

CRYGB; CRYG2; CTRCT39

Species reactivity:

Mouse, Rat

Host:

Rabbit

Cellular localisation:

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Isotype:

IgG

Immunogen:

Recombinant fusion protein containing a sequence corresponding to amino acids 80-135 of human CRYGB (NP_005201.2).

Positive control:

Mouse eye, Rat eye

AA Sequence:

CLIPPHSGAYRMKIYDRDELRGQMSELTDDCISVQDRFHLTEIHSLNVLEGSWILY

Purification:

Affinity purification

Molecular weight:

Calculated MW: 20kDa Observed MW: 21kDa

Form:

Liquid

Applications:

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Dilution:

WB 1:500 - 1:2000

Storage buffer:

Buffer: PBS with 0.02% sodium azide, 50% glycerol, pH7.3.

Storage:

Store 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.

More info:

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Orders:

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