The HSPB4 Antibody from MyBioSource.com is a Rabbit Polyclonal antibody to CRYAA, CRYAA2, and crystallin alpha A2. This antibody recognizes Human, Mouse, and Rat antigen. The HSPB4 Antibody has been validated for the following applications: ELISA, and Western Blot.
Description
Function: Contributes to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions.
Subunit Structure: Heteropolymer composed of three CRYAA and one CRYAB subunits. Inter-subunit bridging via zinc ions enhances stability, which is crucial as there is no protein turn over in the lens. Can also form homodimers and higher homooligomers. Age-dependent C-terminal truncation affects oligomerization.
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 seems to 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.
Similarity: Belongs to the small heat shock protein (HSP20) family