Application

Anti-ATRX Antibody, clone 39f, Cat. No. MABE1798, is a highly specific mouse monoclonal antibody that targets ATRX and has been tested in Immunocytochemistry and Western Blotting .

Immunocytochemistry Analysis: A representative lot detected ATRX in HeLa cells (McDowell, T.L., et. al. (1999). Proc Natl Acad Sci USA. 96(24):13983-8).

Western Blotting Analysis: A representative lot detected ATRX in EBV-transformed lymphocytes (McDowell, T.L., et. al. (1999). Proc Natl Acad Sci USA. 96(24):13983-8).

Western Blotting Analysis: A representative lot detected ATRX in depletion in fibroblasts (Lukashchuk, V., et. al. (2008). J Virol. 82(24):12543-54).

General description

Transcriptional regulator ATRX (UniProt: P46100; also known as EC:3.6.4.12, ATP-dependent helicase ATRX, X-linked helicase II, X-linked nuclear protein, XNP, Znf-HX, ATRX) is encoded by the ATRX (also known as RAD54L, XH2) gene (Gene ID: 546) in human. ATRX is ubiquitously distributed and is involved in transcriptional regulation and chromatin remodeling. ATRX has a PHD zinc finger motif and an ATPase/helicase domain of the SWI/SNF type. It facilitates DNA replication in multiple cellular environments and is required for efficient replication of a subset of genomic loci. ATRX binds to DNA tandem repeat sequences in both telomeres and euchromatin and is shown to bind quadruplex structures in vitro. ATRX associates with pericentromeric heterochromatin during interphase and mitosis, probably by interacting with CBX5/HP1 alpha. It interacts with DAXX to form the chromatin remodeling complex ATRX:DAXX, which has ATP-dependent DNA translocase activity and catalyzes the replication-independent deposition of histone H3.3 in pericentric DNA repeats outside S-phase and telomeres. ATRX is believed to be involved in telomere maintenance via recombination in ALT (alternative lengthening of telomeres) cell lines. ATRX is phosphorylated at serine residues during mitosis and phosphorylation is most evident at pro-metaphase stage. Phosphorylation of ATRX is necessary for release of the protein from the nuclear matrix and that it may facilitate progression to mitosis. Dephosphorylation of ATRX seems to coincide with exit of the cells from M phase. Mutations in ATRX gene are known to cause severe psychomotor and mental retardation, facial dysmorphism, and urogenital abnormalities. (Ref.: Berube, NG et al. (2000). Hum. Mol. Gen. 9(4):539-547).

Immunogen

Recombinant fragment corresponding to 235 amino acids from the N-terminal half of human ARTX.

Other Notes

Concentration: Please refer to lot specific datasheet.

Physical form

Format: Purified

Quality

Evaluated by Western Blotting in HEK293 cell lysate.

Western Blotting Analysis: A 1:500 dilution of this antibody detected ATRX in 10 µg of HEK293 cell lysate.

Specificity

Clone 39f specifically recognizes human ARTX. This clone binds to an epitope beetween amino acid 85-319 in the N-terminal half of human ATRX.

Target description

~282 kDa observed; 282.59 kDa calculated. Uncharacterized bands may be observed in some lysate(s).