Immunohistochemistry was performed on formalin-fixed, paraffin-embedded human brain tumor tissue sections. To expose target antigens, heat-induced epitope retrieval was performed by heating tissues at 120°C for 5 minutes in sodium citrate buffer pH 6.0. Tissues were blocked in 3% hydrogen peroxide for 5 minutes at room temperature and probed with a CRYAB monoclonal antibody (Product # MA5-15383) at a dilution of 1:500 for 80 minutes at room temperature. Tissues were washed extensively with TBST. Detection was performed using an HRP-conjugated anti-mouse IgG secondary antibody and colorimetric substrate. Tissues were counterstained with hematoxylin and visualized by light microscopy. Data courtesy of the Innovators Program.
|Tested species reactivity||Human|
|Host / Isotype||Mouse / IgG2a|
|Immunogen||Purified recombinant fragment of CRYAB (aa1-175) expressed in E. Coli.|
|Contains||0.03% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Immunohistochemistry (Paraffin) (IHC (P))||1/200 - 1/1000|
|Western Blot (WB)||1/500 - 1/2000|
* 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.
MA5-15383 targets CRYAB in IHC and WB applications and shows reactivity with Human samples.
The MA5-15383 immunogen is purified recombinant fragment of CRYAB (aa1-175) expressed in E. Coli.
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.