recommended for detection of Ser 89 phosphorylated p300 of human origin by WB, IP, IF, IHC(P) and ELISA
Modification
Phosphoralated
Modification Notes
Cyclic AMP-regulated gene expression frequently involves a DNA element designated the cAMP-regulated enhancer (CRE). Many transcription factors bind to this element, including the protein CREB which is activated as a result of phosphorylation by protein kinase A. It has been shown that protein kinase A-mediated CREB phosphorylation results in its binding to a nuclear protein designated CBP (for CREB-binding protein). These findings suggest that CBP has many of the properties expected of a CREB co-activator. Another high molecular weight transcriptional adapter protein, designated p300, is characterized by three cysteine- and histidine-rich regions, of which the most carboxy terminal region specifically binds the adenovirus E1A protein. p300 molecules lacking an intact E1A binding site bypass E1A repression even in the presence of high concentrations of E1A . Sequence analysis of CBP and p300 has revealed substantial homology, arguing that these proteins are members of a conserved family of co-activators. Human p300 may be phosphorylated on specific amino acid residues, including Ser 89.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFIHCELISA
WB:1:500~1:2000 IP:1:100~1:500 IF:1:200~1:500 IHC:1:50~1:200 Notes:Optimal dilutions/concentrations should be determined by the researcher.
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
recommended for detection of Ser 89 phosphorylated p300 of human origin by WB IP IF IHC(P) and ELISA
Tissue Specificity
recommended for detection of Ser 89 phosphorylated p300 of human origin by WB, IP, IF, IHC(P) and ELISA