|Application ||WB, IHC|
|Description||Rabbit Anti-Human PUMA (NT) Polyclonal|
|Target/Specificity||Detects the N-terminal domain of PUMA ~23kDa. Detects ~16kDa bands sometimes, possibly corresponding to PUMAβ.|
|Other Names||BBC3 Antibody, BCL2 binding component 3 Antibody, p53 up regulated modulator of apoptosis Antibody, PUMA/JFY1 Antibody|
|Immunogen||N-terminal amino acids of human PUMA|
|Purification||Protein A Purified|
|Storage Buffer||PBS, 0.02% sodium azide|
|Shipping Temperature||Blue Ice or 4ºC|
|Certificate of Analysis||2 µg/ml of SPC-165 was sufficient for detection of PUMA in 20 µg of human K562 cell lysate by colorimetric immunoblot analysis using Goat anti-rabbit IgG:HRP as the secondary antibody.|
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Provided below are standard protocols that you may find useful for product applications.
Apoptosis is related to many diseases and development. The p53 tumor-suppressor protein induces apoptosis through transcriptional activation of several genes. A novel p53 inducible pro-apoptotic gene was identified recently and designated PUMA (for p53 up-regulated modulator of apoptosis) and bbc3 (for Bcl-2 binding component 3) in human and mouse (1-3). PUMA/bbc3 is one of the pro-apoptotic Bcl-2 family members including Bax and Noxa, which are also transcriptional targets of p53. The PUMA gene encodes two BH3 domain-containing proteins termed PUMA-α and PUMA-β (1). PUMA proteins bind Bcl-2, localize to the mitochondria, and induce cytochrome c release and apoptosis in response to p53. PUMA may be a direct mediator of p53-induced apoptosis.
1. Nakano K., Vousden K.H. (2001) Mol Cell. 2001; 7(3): 683-94.
2. Yu J., Zhang L., Hwang P.M., Kinzler K.W., Vogelstein B. (2001) Mol Cell. 7(3): 673-82.
3. Han J., et al. (2001) Proc Natl Acad Sci U S A. 98(20): 11318-23.
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