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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"e;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.
CTPP2, MFM2, HSPB5, CMD1II, CRYA2, CTRCT16
alpha-crystallin B chain, heat shock protein beta-5, heat-shock 20 kD like-protein, renal carcinoma antigen NY-REN-27, rosenthal fiber component, CRYA2, CTPP2, HSPB5, CRYAB