|Tested species reactivity||Bovine, Rat|
|Host / Isotype||Rabbit / IgG|
|Immunogen||Purified alpha-A Crystallin from bovine lens.|
|Purification||Antigen affinity chromatography|
|Storage buffer||PBS with 30mg/ml BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||-20° C, Avoid Freeze/Thaw Cycles|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||10 ug/ml|
|Western Blot (WB)||0.1 ug/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
PA1-009 detects alpha-A crystallin from bovine and rat samples. This antibody does not detect the unphosphorylated form of the protein.
PA1-009 has been successfully used in Western blot and immunohistochemistry procedures. By Western blot, this antibody detects an ~20 kDa protein representing alpha-A crystallin from bovine lens samples. Immunohistochemical staining of alpha-A crystallin in rat thymus samples results in staining of epithelial reticular cells.
The PA1-009 immunogen is purified alpha-A Crystallin from bovine lens.
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 and quote;s disease where it accumulates in brain cells of those afflicted.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.