Anti-phospho-TP53 (pSer⁴⁶) antibody produced in rabbit

p53 is a nuclear protein which plays an essential role in the regulation of cell cycle specifically in the transition from G0 to G1. It is found in very low levels in normal cells however in a variety of transformed cell lines in high amounts and believed to contribute to transformation and malignancy. The open reading frame of p53 is 393 amino acids long, with the central region (consisting of amino acids from about 100 to 300) containing the DNA-binding domain. This proteolysis-resistant core is flanked by a C-terminal end mediating oligomerization and an N-terminal end containing a strong transcription activation signal. p53 binds as a tetramer to a PBS (p53-Binding Site) and activates the expression of downstream genes that inhibit growth and/or invasion. p53 binds as a tetramer to a p53-binding site (PBS) and to activate the expression of adjacent genes that inhibit growth and/or invasion. Deletion of one or both p53 alleles reduces the expression of tetramers, resulting in decreased expression of the growth inhibitory genes

Peptide sequence around phosphorylation site of serine 46 (M-L-S(p)-P-D), according to the protein TP53.

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Solution in phosphate-buffered saline containing 0.02% sodium azide and 50% glycerol