Cat. # | Size | Qty. | Price |
---|---|---|---|
58525S | 100 µl |
|
REACTIVITY | H |
SENSITIVITY | Endogenous |
MW (kDa) | 90 |
Source/Isotype | Rabbit IgG |
Product Information
Application | Dilution |
---|---|
Western Blotting | 1:1000 |
For western blots, incubate membrane with diluted primary antibody in 5% w/v nonfat dry milk, 1X TBS, 0.1% Tween® 20 at 4°C with gentle shaking, overnight.
NOTE: Please refer to primary antibody product webpage for recommended antibody dilution.
NOTE: Prepare solutions with reverse osmosis deionized (RODI) or equivalent grade water.
Load 20 µl onto SDS-PAGE gel (10 cm x 10 cm).
NOTE: Loading of prestained molecular weight markers (#59329, 10 µl/lane) to verify electrotransfer and biotinylated protein ladder (#7727, 10 µl/lane) to determine molecular weights are recommended.
NOTE: Volumes are for 10 cm x 10 cm (100 cm2) of membrane; for different sized membranes, adjust volumes accordingly.
* Avoid repeated exposure to skin.
posted June 2005
revised June 2020
Protocol Id: 263
Human
Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of human Pyrin/MEFV protein. Antigen mapping indicates that this antibody and Pyrin/MEFV (E2E8U) Rabbit mAb #40649 have different epitopes.
Pyrin is encoded by the MEFV gene that is frequently mutated in patients with familial Mediterranean fever (FMF), an autoinflammatory disorder that causes recurrent fevers, usually also accompanied by pain in the abdomen, chest, and joints. It is expressed mainly in cells of the innate immune system, such as granulocytes, eosinophils, monocytes, and dendritic cells (1,2). Pyrin can form inflammasomes with ASC and Casp1, and this is regulated by RhoA guanosine triphosphatase (GTPase). RhoA activation leads to PKN1/2-mediated phosphorylation of Ser208 and Ser242 on Pyrin (Ser205 and Ser241 on mouse Pyrin, respectively). The chaperone 14-3-3 proteins bind to the phosphorylated Pyrin and keep it in an inactive state. Agents that inactivate RhoA, such as certain bacterial toxins, cause a decrease in PKN1/2 activity and Pyrin phosphorylation. This in turn releases Pyrin from the inhibitory 14-3-3 proteins, and allows Pyrin to form an active inflammasome (3-6).
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