Render Target: SSR
Render Timestamp: 2024-12-19T21:39:23.017Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-11-18 16:03:13.381
Product last modified at: 2024-11-19T09:00:32.473Z
Cell Signaling Technology Logo
1% for the planet logo
PDP - Template Name: Monoclonal Antibody
PDP - Template ID: *******c5e4b77
R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.

Pyrin/MEFV (F9C4G) Rabbit mAb #62008

Filter:
  • WB
  • IP

    Supporting Data

    REACTIVITY M
    SENSITIVITY Endogenous
    MW (kDa) 105
    Source/Isotype Rabbit IgG
    Application Key:
    • WB-Western Blotting 
    • IP-Immunoprecipitation 
    Species Cross-Reactivity Key:
    • M-Mouse 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000
    Immunoprecipitation 1:50

    Storage

    Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/mL BSA, 50% glycerol, and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.

    Protocol

    Specificity / Sensitivity

    Pyrin/MEFV (F9C4G) Rabbit mAb recognizes endogenous levels of total Pyrin/MEFV protein.

    Species Reactivity:

    Mouse

    Source / Purification

    Monoclonal antibody is produced by immunizing animals with recombinant protein specific to the carboxy terminus of mouse Pyrin/MEFV protein.

    Background

    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).
    For Research Use Only. Not For Use In Diagnostic Procedures.
    Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.
    All other trademarks are the property of their respective owners. Visit our Trademark Information page.