Anti-MLL/HRX Antibody, CT., clone 9-12

The acute lymphoblastic leukaemia (ALL)-1 (also known as MLL, HRX, HTRX, and TRX1) gene on human chromosome 11q23 is the site of many locally clustered chromosomal alterations associated with several types of acute leukaemias, including deletions, partial duplications and translocations. Structurally variant proteins derived from the altered gene presumably cause the malignant transformation of early haemopoietic progenitor cells.

This monoclonal antibody targets the C-terminal proteolytic fragment of MLL (C180; MLL^C). A reduced target band detection by this antibody was seen lysate from G411NS human glioblastoma neural stem cells transfected with MLL shRNA (Gallo, M., et al. (2013). Cancer Res. 73(1):417-427).

Epitope: MLL C-terminal fragment

MBP-tagged recombinant human mixed lineage leukemia (MLL) protein C-terminal fragment (a.a. 3084-3959).

Anti-MLL/HRX, C-term., clone 9-12 is a high quality mouse monoclonal antibody that has been validated and published for use in Chromatin Immunoprecipitation (ChIP), Immunofluorescence, Immunoprecipitation, and Western Blotting applications.

Immnuofluorescence Analysis: A representative lot detected MLL expression in SOX2+ cells in paraffin-embedded high-grade human gliomas sections (Gallo, M., et al. (2013). Cancer Res. 73(1):417-427).

Chromatin Immnuoprecipitation (ChIP) Analysis: A representative lot detected MLL occupancy at the Hoxa10 and Meis promoters in mouse MLL-AF10 leukemia cells (Gallo, M., et al. (2013). Cancer Res. 73(1):417-427).

Chromatin Immnuoprecipitation (ChIP) Analysis: A representative lot detected an enhanced MLL occupancy at the Ink4a locus of 8-month-old than 2-month-old bEzTG mouse islets. The same age-dependent Ink4a locus enrichment was observed with H3K4me3, while the opposite trend was seen with Ezh and H3K27me3 enrichment at the same locus (Zhou, J.X., et al. (2013). J. Clin. Invest. 123(11):4849-4858).

Chromatin Immnuoprecipitation (ChIP) Analysis: A representative lot detected MLL occupancy at the HOXA10 promoter region in G179NS and G411NS human glioblastoma neural stem cells (Gallo, M., et al. (2013). Cancer Res. 73(1):417-427).

Chromatin Immnuoprecipitation (ChIP) Analysis: A representative lot detected MLL occupancy at the DNA replication origin (RD) as well as at both exon 1b and p16INK4a/p19ARF shared exon 2 in mouse embryonic fibroblast (MEF). An increased MLL enrichment at these sites was observed in senescent and Polycomb mutant MEFs (Agherbi, H., et al. (2009). PLoS One. 4(5):e5622).

Chromatin Immnuoprecipitation (ChIP) Analysis: A representative lot detected MLL occupancy at the Hoxa9 AB region using mouse embryonic fibroblast (MEF) chromatin preparation (Erfurth, F.E., et al. (2008). Proc. Natl. Acad. Sci. U.S.A. 105(21):7517-7522).

Immnuoprecipitation Analysis: A representative lot co-immunoprecipitated JmjD3 and RbBP5, but not Dnmt3a, with MLL from Min6 mouse insulinoma cell extract (Zhou, J.X., et al. (2013). J. Clin. Invest. 123(11):4849-4858).

Western Blotting Analysis: A representative lot detected higher MLL level in cultured glioblastoma neural stem (GNS) cells than neural stem (NS) cells, as well as MLL enrichment in the CD15+ fraction of freshly resected Glioblastoma (GBM) cells (Gallo, M., et al. (2013). Cancer Res. 73(1):417-427).

Western Blotting Analysis: A representative lot detected SET domain-containing C-terminal fragment of the MLL complex enzymatic subunit MLL (C180; MLL^C) in anti-FLAG immunoprecipitate from HeLaS cells stably expressing FLAG-tagged hDPY-30 (Cho, Y.W., et al. (2007). J. Biol. Chem. 282(28):20395-20406).

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Histones

Evaluated by Western Blotting in K562 nuclear extract.
Western Blotting Analysis: 0.1-1 µg/mL of this antibody detected MLL C-terminal fragment (C180; MLL^C) in K562 nuclear extract.

~180 kDa observed. 134.4 kDa (a.a. 2719-3969; human MLL cleavage product C180) and 431.8/427.7/432.1 kDa (human full-length MLL isoform 1/2 (14P-18B)/3) calculated.

Format: Purified

Protein G purified.

Purified mouse IgG1 in 0.1 M Tris-glycine, pH 7.4, 0.15 M NaCl, 0.05% sodium azide before the addition of glycerol to 30%. Liquid at -20ºC

Store for 2 years at -20ºC from date of shipment. For maximum recovery of product, centrifuge the vial prior to removing the cap.

Control
K562 nuclear extract

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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