MilliporeSigma anti-AML1 (Ab-1), Polyclonal
Rabbit Polyclonal Antibody
Manufacturer: MilliporeSigma PC284100UG
Specifically detects AML1 Clone: in Human, Mouse samples, and it is validated for Gel Supershift, Immunoprecipitation, Immuno BlottingThe family of nuclear transcription factors represented by AML are important transactivators of tissue-specific genes of the hematopoietic lineage and the bone cell lineage. There are currently three different mammalian proteins that are members of this family, AML1, AML2, and AML3. The AML proteins in turn form heterodimers with another protein, CBFbeta and it is this complex which has the transcription factor activity. Within the complex the AML protein provides the DNA binding function. The AML gene was discovered in 1991 by cloning the t(8;21) translocation that is common to AML. Structurally the AML protein contains a transactivation domain at the C-terminus and has homology with the Drosophila Runt gene that is the DNA binding protein of the protein. In leukemias, AML1 undergoes a translocation and becomes fused to MTG8 (ETO) and forms a chimeric protein (83kDa). This chimera is in turn complexed with the CBFbeta gene product that also has undergone a translocation. In addition to MTG8, AML1 has also been shown to undergo translocation with TEL, and EVI. Splice variants have been reported for AML which include AML1a (30kDa), AML1b (54kDa), and AML1c. All forms contain the runt domain but vary in their transactivation ability. Additionally 6 major transcripts have been shown for AML due to the use of 2 promoters and differential use of 3 polyadenylation sites in addition to the splice variants.
|a synthetic peptide corresponding to amino acids at the N-terminus of human AML1|
|Gel Supershift, Immuno Blotting, Immunoblot, Immunoprecipitation|
|Recognizes the ∽58kDa AML1 protein in HeLa, Jurkat, and NIH2T3 cells. May not detect endogenous AML1.|
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