Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.
Cleaved IL-1beta (Asp116) Antibody detects endogenous levels of the 17 kDa processed form of IL-1beta. The antibody does not recognize the uncleaved precursor of IL-1beta.
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence of the 17 kDa mature form of human IL-1beta. Antibodies are purified by protein A and peptide affinity chromatography.
Interleukin-1β (IL-1β), one of the major caspase-1 targets, is a multifunctional cytokine that is involved in a host of immune and proinflammatory responses (1). It is produced primarily by activated monocytes and macrophages. It signals through various adaptor proteins and kinases that lead to activation of numerous downstream targets (2-6). Human IL-1β is synthesized as a 31 kDa precursor. To gain activity, the precursor must be cleaved by caspase-1 between Asp116 and Ala117 to yield a 17 kDa mature form (7,8). Detection of the 17 kDa mature form of IL-1β is a good indicator of caspase-1 activity.
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