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Caspase-9 monoclonal antibody (10-1-87)

ADI-905-686-100 100 µg 393.00 USD
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Product Details

Immunogen:Recombinant full length human Caspase-9.
UniProt ID:P55211
Source:Purified from mouse ascites.
Species reactivity:Human
Recommended Dilutions/Conditions:Western Blot (1µg/ml, ECL)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
Application Notes:Detects bands of ~47kDa (full length) and ~37/35kDa (cleaved) by Western blot.
Purity Detail:Protein G affinity purified.
Formulation:Liquid. In PBS, pH 7.2, containing 0.09% sodium azide and 50% glycerol.
Handling:Avoid freeze/thaw cycles.
Shipping:Blue Ice
Long Term Storage:-20°C
Scientific Background:The caspases are a family of cysteine proteases that cleave after certain aspartate residues, and are primarily recognized as mediators of apoptosis. caspases are synthesized as inactive zymogens that can be cleaved to form active enzymes following the induction of apoptosis by stress or death receptors. Initiator caspases (e.g. caspase-8 and -10) are activated by dimerization of the zymogen on a dedicated adaptor protein. These activated initiator caspases in-turn cleave downstream effector or executioner caspases (e.g. caspase-3, -6, and -7) in a cascade-like manner, which cleave key cellular proteins that lead to the morphological changes associated with apoptotic cell death.
Regulatory Status:RUO - Research Use Only
Caspase-9 monoclonal antibody (10-1-87) Western blot
Western blot analysis of MW marker (1), Jurkat (2), and Jurkat + staurosporine (3) cells probed with Caspase 9 mAb (10-1-87).
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Caspase-9 monoclonal antibody (10-1-87) Western blot

Product Literature References

Apaf-1 and caspase-9 are required for cytokine withdrawal-induced apoptosis of mast cells but dispensable for their functional and clonogenic death: V.S. Marsden, et al.; Blood 107, 1872 (2006), Abstract; Full Text
Granzyme M Mediates a Novel Form of Perforin-dependent Cell Death: J.M. Kelly, et al.; J. Biol. Chem. 279, 22236 (2004), Abstract; Full Text

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