Synthetic peptide 17-aa, Human PUMA. Human control peptide sequence is also found in alternatively spliced PUMA-beta but not in gamma or delta forms.
The p53 tumor antigen is found in increased amounts in a wide variety of transformed cells. The protein is also detectable in many actively proliferating, nontransformed cells, but it is undetectable or present at low levels in resting cells. P53 tumor-suppressor protein functions to inhibit the growth of tumor cells. Although p53 is not required for the growth and differentiation of normal cells, it may play a role in several cellular processes including senescence and differentiation. Mice lacking p53 show a high incidence of tumor formation. P53 inhibits cell growth through inactivation of both cell cycle arrest and apoptosis. Several p53-induces genes play a role in the induction of apoptosis. Through global profiling of genes that were expressed soon after p53 expression, a novel gene termed PUMA (p53-upregulated modulator of apoptosis) as a target for p53 activation. PUMA/JFY1 (mouse 193-aa, human 193-aa, chromosome 19q) is expressed in most tissues. It is exclusively located in mitochondria and it induces cytochrome-C release. PUMA binds to BCL2 and BCLXL through a BH3 domain (141-149 aa). Exogenous expression of PUMA resulted in an extremely rapid and profound apoptosis that occurred much earlier than that resulting from exogenous expression of p53. PUMA is alternatively spliced to produce 2-4 transcripts PUMA alpha (193-aa, ~25kD), -beta (131-aa, ~16kD), gamma, and delta (101-aa). The gamma and delta forms were not detectable in endogenous cells. PUMA alpha and beta displayed similar apoptosis inducing ability.
Applications:ELISA: 1:10-50K for neat serum and 0.5-1ug/ml for affinity pure.
