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αA-Crystallin polyclonal antibody

ADI-SPA-221

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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.

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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).

Product Details

Alternative Name	CRYAA, HSPB4
Application	IF, IP, WB
Application Notes	Detects a band of ~20kDa by Western blot.
Formulation	Liquid. In PBS, pH 7.2, containing 50% glycerol and 0.09% sodium azide.
GenBank ID	U05569
Host	Rabbit
Immunogen	Synthetic peptide corresponding to the sequence near the C-terminus of human αA-Crystallin. The sequence is completely conserved in frog and chicken.
Purity Detail	Protein A affinity purified.
Recommendation 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.
Source	Purified from rabbit serum.
Species Reactivity	Bovine, Human, Mouse
UniProt ID	P02489
Worry-free Guarantee	This antibody is covered by our Worry-Free Guarantee.

Handling & Storage

Long Term Storage	-20°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

Novel mTORC2/HSPB4 Interaction: Role and Regulation of HSPB4 T148 Phosphorylation: Sluzala, Z. B., Shan, Y., et al.; Cells 13, (2024), Abstract
Thiol-Mediated Enhancement of Nε-Acetyllysine Formation in Lens Proteins: Panja, S., Nahomi, R. B., et al.; ACS Chem. Biol. 19, 1495 (2024), Abstract
Promotion of Protein Solubility and Reduction in Stiffness in Human Lenses by Aggrelyte-1: Implications for Reversing Presbyopia.: Panja, S., Gaikwad, H., et al.; Int. J. Mol. Sci. 24, (2023), Application(s): WB, Abstract
Aggrelyte-2 promotes protein solubility and decreases lens stiffness through lysine acetylation and disulfide reduction: Implications for treating presbyopia: Panja, S., Nahomi, R. B., et al.; Aging Cell 22, e13797 (2023), Abstract
AAV2-Mediated Expression of HspB1 in RGCs Prevents Somal Damage and Axonal Transport Deficits in a Mouse Model of Ocular Hypertension.: Nam, M. H., Nahomi, R. B., et al.; Transl. Vis. Sci. Technol. 11, 8 (2022), Reactant(s): Mouse, Abstract
Glycation-mediated protein crosslinking and stiffening in mouse lenses are inhibited by carboxitin in vitro.: Nandi, S. K., Rankenberg, J., et al.; Glycoconj. J. 38, 347 (2021), Reactant(s): Mouse, Abstract
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), Reactant(s) Mouse, 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
The absence of SIRT3 and SIRT5 promotes the acetylation of lens proteins and improves the chaperone activity of α-crystallin in mouse lenses.: Nandi, S. K., Nahomi, R. B., et al.; Exp. Eye Res. 182, 1 (2019), Reactant(s): Mouse, Abstract
A specific phosphorylation regulates the protective role of αA-crystallin in diabetes: A. Ruebsam, et al.; JCI Insight 3, e97919 (2018), Abstract