Recombinant Human alpha A Crystallin/CRYAA protein (His tag)
Be the first to review this product! Submit a review
|
(0 Publication)
Recombinant Human alpha A Crystallin/CRYAA protein (His tag) is a Human Full Length protein, in the 1 to 173 aa range, expressed in Escherichia coli, with >95%, suitable for SDS-PAGE.
View Alternative Names
CRYA1, HSPB4, CRYAA, Alpha-crystallin A chain, Heat shock protein beta-4, Heat shock protein family B member 4, HspB4
- SDS-PAGE
Unknown
SDS-PAGE - Recombinant Human alpha A Crystallin/CRYAA protein (His tag) (AB268427)
SDS-PAGE analysis of ab268427.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Alpha A Crystallin acts like a molecular chaperone. It helps prevent the aggregation of misfolded proteins which is important in maintaining cellular protein homeostasis. Alpha A Crystallin can combine with alpha B Crystallin in lens fiber cells to form a hetero-oligomeric complex. This ability to bind unfolded proteins and assist in refolding processes highlights its importance in cell stress responses especially in situations where proteins could potentially denature and lose function.
Pathways
Alpha A Crystallin participates significantly in the oxidative stress response and apoptotic pathways. It interacts with proteins involved in these processes such as caspases to inhibit cell death and curb the deleterious effects of reactive oxygen species. In the apoptotic pathway alpha A Crystallin's role in regulating cell survival highlights its association with proteins like Hsp70 another heat shock protein that serves as a stabilizing agent during cellular stress.
Specifications
Form
Liquid
General info
Function
Contributes to the transparency and refractive index of the lens (PubMed : 18302245). In its oxidized form (absence of intramolecular disulfide bond), acts as a chaperone, preventing aggregation of various proteins under a wide range of stress conditions (PubMed : 18199971, PubMed : 19595763, PubMed : 22120592, PubMed : 31792453). Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed : 28935373).
Sequence similarities
Belongs to the small heat shock protein (HSP20) family.
Post-translational modifications
O-glycosylated; contains N-acetylglucosamine side chains.. Deamidation of Asn-101 in lens occurs mostly during the first 30 years of age, followed by a small additional amount of deamidation (approximately 5%) during the next approximately 38 years, resulting in a maximum of approximately 50% deamidation during the lifetime of the individual.. Phosphorylation on Ser-122 seems to be developmentally regulated. Absent in the first months of life, it appears during the first 12 years of human lifetime. The relative amount of phosphorylated form versus unphosphorylated form does not change over the lifetime of the individual.. Acetylation at Lys-70 may increase chaperone activity.. Undergoes age-dependent proteolytical cleavage at the C-terminus. Alpha-crystallin A(1-172) is the most predominant form produced most rapidly during the first 12 years of age and after this age is present in approximately 50% of the lens molecules.. In young individuals and during the first approximately 30 years of life, less than half molecules contain an intramolecular disulfide bond (oxidized form), while in the remaining fraction the cysteines are in the free sulfhydryl form (reduced form). With aging, the amount of oxidized form increases up to 90% and it becomes a major constituent of high molecular weight aggregates, concomitant with an age-dependent loss of its chaperone activity. The reduced form is undetectable in cataractous lenses.
Subcellular localisation
Nucleus
Target data
Complementary Products
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com