AlphaA Crystallin/CRYAA Products

Description

Lens proteins consist almost entirely of crystallins (about 95%). Crystallins are also found vertebrate skeletal muscle tissue. In the lens, their structural function is to assist in maintaining the proper refractive index of the lens. The mammalian lens contains 3 major classes of crystallins: alpha, beta, and gamma. Alpha-crystallin is the largest of the crystallins and is composed of 2 primary gene products--alpha-A and alpha-B. There are at least 5 different proteins comprising the beta-crystallins. The gamma-crystallins are monomeric, but there are at least 5 gamma crystallins identified in bovine and rat lens. Alpha-Crystallin comprises 40% of total lens protein composition. In addition to maintaining proper refractive index, it also functions in a chaperone like manner by preventing the formation of aggregates possibly leading to cataract formation. It is believed that the phosphorylated states of the alpha-crystallin occur in response to cellular stress and may serve a structural control function and play a role in protein maintenance. Alpha-B crystallin has been linked to Alexander®s disease where it accumulates in brain cells of those afflicted.

Bioinformatics

Entrez	1409 Human 24273 Rat
Uniprot	NP_000385 Human NP_000385.1 Human P02489 Human
Product By Gene ID	1409
Alternate Names	CRYA1crystallin, alpha-1 crystallin, alpha A Heat shock protein beta-4 HSPB4alpha-crystallin A chain human alphaA-crystallin (CRYA1), 10HspB4

Research Areas for AlphaA Crystallin/CRYAA

Find related products by research area and learn more about each of the different research areas below.

Membrane Trafficking and Chaperones
Vision