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αA-Crystallin polyclonal antibody

ADI-SPA-221-D 50 µg 237.00 USD
ADI-SPA-221-F 200 µg 471.00 USD
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Product Details

Alternative Name:CRYAA, HSPB4
Immunogen:Synthetic peptide corresponding to the sequence near the C-terminus of human αA-Crystallin. The sequence is completely conserved in frog and chicken.
UniProt ID:P02489
GenBank ID:U05569
Source:Purified from rabbit serum.
Species reactivity:Human, Mouse
Applications:IF, IP, WB
Recommended Dilutions/Conditions:Western Blot (1:1,000, colorimetric)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Application Notes:Detects a band of ~20kDa by Western blot.
Purity Detail:Protein A affinity purified.
Formulation:Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
Shipping:Blue Ice
Long Term Storage:-20°C
Scientific Background:Alpha-crystallins, which are part of the small Heat shock family members, are major water-soluble proteins present in the lens of the mammalian eye. Phosphorylation of serine residues which occurs during development and in response to stress, is intimately linked with its function. Chaperone activity requires, and is modulated by, oligomerization and is limited to binding unfolded intermediates to prevent irreversible aggregation.
Regulatory Status:RUO - Research Use Only
αA-Crystallin polyclonal antibody Western blot
Western blot analysis of Crystallin, alpha-A pAb: Lane 1: Crystallin, alpha Native Bovine Protein, Lane 2: Crystallin, alpha A Native Bovine Protein, Lane 3: Crystallin, alpha B Native Bovine Protein (Negative Control), Lane 4: Crystallin, beta Native Bovine Protein (Negative Control).
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αA-Crystallin polyclonal antibody Western blot

Product Literature References

Glycation-mediated inter-protein crosslinking is promoted by chaperone-client complexes of α-crystallin: Implications for lens aging and presbyopia: S.K. Nandi, et al.; J. Biol. Chem. 295, 5701 (2020), Abstract; Full Text
p62/Sequestosome 1 levels increase and phosphorylation is altered in Cx50D47A lenses, but deletion of p62/sequestosome 1 does not improve transparency: O. Jara, et al.; Mol. Vis. 26, 204 (2020), Abstract; Full Text
A specific phosphorylation regulates the protective role of αA-crystallin in diabetes: A. Ruebsam, et al.; JCI Insight 3, e97919 (2018), Abstract;
Elevated retina-specific expression of the small heat shock protein,αA-crystallin, is associated with photoreceptor protection in experimental uveitis: N. Rao, et al. ; Invest. Ophthalmol. Vis. Sci. 49, 1161 (2008), Application(s): IP, IF using mouse cell lysates & tissue, Abstract;
alpha-Crystallin distribution in retinal pigment epithelium and effect of gene knockouts on sensitivity to oxidative stress: D. Hinton, et al. ; Mol. Vis. 13, 566 (2007), Application(s): WB, IF using human tissue culture & cell lysates, Abstract;
Small heat-shock proteins select &UDelta;F508-CFTR for endoplasmic reticulum-associated degradation: J. Brodsky, et al. ; Mol. Biol. Cell 18, 806 (2007), Application(s): IP, WB using human cell lysates, Abstract;

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