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γ-Crystallin (bovine), (native)

 
ADI-SPP-240-J 1 mg 119.00 USD
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Product Specification

Alternative Name:CRYGD
 
MW:~19kDa
 
Source:Isolated from bovine eye lens.
 
Formulation:Liquid. In PBS containing 0.09% sodium azide.
 
Purity:≥90% (SDS-PAGE; Western blot)
 
Purity Detail:Purified by multi-step chromatography.
 
Applications:WB
 
Application Notes:Western blot control.
 
Shipping:Shipped on Dry Ice
 
Long Term Storage:-80°C
 
Scientific Background:The crystallins are structural proteins most highly expressed in lens fiber cells of the vertebrate eye. The crystallins are divided into two subfamilies: the alpha-crystallins (alphaA and alphaB) which are members of the small heat shock protein superfamily, also functioning as molecular chaperones; and the evolutionarily-linked superfamily of beta- and gamma-crystallins which comprise the majority of soluble protein in the lens, and contribute to the transparency and refractive properties of lens structure. There are four major gamma-crystallin classes: terrestrial (gammaA-F); aquatic (fish-gammaM); gamma-S; and gamma-N, a beta-gamma-hybrid crystallin. The beta- and gamma-crystallins share structural homology in the presence of four modified Greek key beta-gamma-motifs, but differ in that monomeric gamma-crystallins lack N-terminal extensions present in beta-crystallins that promote oligomerization. Alterations in gamma-crystallin gene expression leads to aggregation of misfolded protein in the lens, and has been linked to the development of congenital cataracts in humans. The predicted molecular weight of bovine gamma-crystallin is approximately 20-21 kDa.
 
SPP-240 SDS-PAGE
SDS-PAGE analysis: Lane 1: MW marker, Lane 2: 1µg, Lane 3: 2µg, Lane 4: 5µg gamma-Crystallin.
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SPP-240 SDS-PAGE

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Heat Shock Proteins & the Cellular Stress Response Catalog
Heat Shock Proteins & the Cellular Stress Response Catalog
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