Capases are a highly conserved family of cysteine proteases and are synthesized as inactive zymogens, which are cleaved at Asp-x sites during apoptosis, generating large and small subunits that heterodimerize to form the active enzyme. Caspase-1 is a member of the ICE/CED-3 family of caspases and is detected in the pro-form as a protein of 45 kDa.
Caspase-1 generates the bioactive form of the pro-inflammatory cytokine IL-1β from its biologically inactive precursor. Overexpression of caspase-1 in cells induces apoptosis, which can be inhibited by cytokine response modifier A (CrmA). Caspase-1 mRNA is predominantly expressed in the spleen and lung and to a lesser extent in skeletal muscle, kidney, testis and heart and within these tissues macrophages preferentially express caspase-1. Caspase-1 deficient mice have no gross abnormalities, however, macrophages from caspase-1-deficient mice are defective in IL-β processing and release.
- For ELISA, Flow Cytometry, Western Blot
Recognizes an epitope within the p20 fragment of mouse caspase-1. Detects a band of ~45kDa by Western blot. Does not cross-react with mouse caspase-11 or -12.
Type: Primary
Antigen: CASP1
Clonality: Monoclonal
Clone:
Conjugation:
Epitope:
Host: Rat
Isotype:
Reactivity: Mouse
