Anti-PML Isoform II Antibody, clone 1A8.1

Evaluated by Western Blotting in lysate from PML-2 transfected HEK293 cells.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected the exogenously expressed human PML-2 in 10 µg of lysate from transfected HEK293 cells.

Anti-PML Isoform II Antibody, clone 1A8.1 is an antibody against PML Isoform II for use in Western Blotting, Immunocytochemistry.

Immunocytochemistry Analysis: 40 µg/mL from a representative lot immunostained 10% neutral-buffered formalin-fixed HEK293 cells transfected with human PML isoform II by non-fluorescent immunocytochemistry (Courtesy of Professor Ygal Haupt, Peter MacCallum Cancer Centre, East Melbourne, Australia).
Immunocytochemistry Analysis: 10 µg/mL from a representative lot immunostained 4% paraformaldehyde-fixed HEK293 cells transfected with human PML isoform II by fluorescent immunocytochemistry (Courtesy of Professor Ygal Haupt, Peter MacCallum Cancer Centre, East Melbourne, Australia).

Research Category
Epigenetics & Nuclear Function

Research Sub Category
Chromatin Biology

Clone 1A8.1 was raised against an C-terminal region sequence unique to PML isoform II (PML-2), but not present in the other 11 PML spliced isoforms reported by UniProt (P29590).

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Protein PML (UniProt P29590; also known as Promyelocytic leukemia protein, RING finger protein 71, Tripartite motif-containing protein 19) is encoded by the PML (also known as MYL, PP8675, RNF71, TRIM19) gene (Gene ID 5371) in human. The human PML gene/protein adopted its name when it was originally discovered as an RARα fusion protein caused by chromosomal translocation in acute promyelocytic leukemia (APL) patients. In normal cells, the PML protein interacts with multiple protein partners in the nucleus to form PML nuclear bodies (PML-NBs) that mediate a variety of cellular functions including senescence, apoptosis, protein degradation, telemere stasbility, and antiviral defense. At least 12 PML isoforms are generated by alternative splicings, including six nuclear isoforms (PML-I to PML-VI) and the cytoplasmic isoform PML-VII (a.k.a. PML-VIIB), other spliced isoforms without exon 6-coding sequence (a.a. 467-552) are likewise expected to be cytoplasmic due to the abscence of nuclear localization signal (NLS) encoded by exon 6. All isoforms share the same N-terminal region (a.a. 1-419) containing the RBCC/tripartite motif and may have related functions due to their common functional RBCC/TRIM domain, while increasing evidences also suggest that each PML isoform possesses distinct functions mediated by its specific C-terminal sequence. Isoform PML-1 (a.k.a. PML-I, TRIM19alpha; UniProt P29590-1) and PML-2 (a.k.a. PML-II or TRIM19kappa; UniProt P29590-8) share the same N-terminal 570-a.a. sequence (encoded by exons 1 to 7a), however PML-1 derives its remaining C-terminal sequence (a.a. 571-882) from exons 8a & 9, while PML-II derives its (a.a. 571-829) from exon 7b with a different reading frame as that of PML-V.

~110 kDa observed. 90.72 kDa calculated. Uncharacterized band(s) may appear in some lysates.

Epitope: C-terminal region.

KLH-conjugated linear peptide corresponding to a C-terminal sequence of human PML Isoform II.

Concentration: Please refer to lot specific datasheet.

Format: Purified

Protein G Purified

Purified mouse monoclonal IgG1κ antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Stable for 1 year at 2-8°C from date of receipt.