Key features and details
- Rabbit polyclonal to PML Protein
- Suitable for: WB, IHC-P, IHC-FoFr
- Reacts with: Mouse
- Isotype: IgG
Product nameAnti-PML Protein antibody
See all PML Protein primary antibodies
DescriptionRabbit polyclonal to PML Protein
Tested applicationsSuitable for: WB, IHC-P, IHC-FoFrmore details
Species reactivityReacts with: Mouse
Synthetic peptide derived from internal domain (400-500) of mouse PML protein
Storage instructionsShipped at 4°C. Upon delivery aliquot and store at -20°C. Avoid freeze / thaw cycles.
Storage bufferConstituent: Whole serum
Concentration information loading...
Our Abpromise guarantee covers the use of ab67761 in the following tested applications.
The application notes include recommended starting dilutions; optimal dilutions/concentrations should be determined by the end user.
|WB||1/500 - 1/5000. Predicted molecular weight: 98 kDa.|
|IHC-P||Use at an assay dependent concentration.|
|IHC-FoFr||Use at an assay dependent concentration. PubMed: 23518714|
FunctionKey component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum (By similarity). Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM2. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitinylation.
Involvement in diseaseNote=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon.
Sequence similaritiesContains 2 B box-type zinc fingers.
Contains 1 RING-type zinc finger.
DomainInteracts with PKM2 via its coiled-coil domain.
Binds arsenic via the RING-type zinc finger.
modificationsUbiquitinated; mediated by RNF4, SIAH1 or SIAH2 and leading to subsequent proteasomal degradation. 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination by RNF4 is polysumoylation-dependent.
Undergoes 'Lys-11'-linked sumoylation. Sumoylation on all three sites is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. The PML-RARA fusion protein requires the coiled-coil domain for sumoylation. Desumoylated by SENP2 and SENP6. Arsenic induces PML and PML-RARA oncogenic fusion proteins polysumoylation and their subsequent RNF4-dependent ubiquitination and proteasomal degradation, and is used as treatment in acute promyelocytic leukemia (APL).
Phosphorylated in response to DNA damage, probably by ATR.
Acetylation may promote sumoylation and enhance induction of apoptosis.
Cellular localizationNucleus > nucleoplasm. Cytoplasm. Nucleus > PML body. Nucleus > nucleolus. Endoplasmic reticulum membrane. Early endosome membrane. Sumoylated forms localize to the PML nuclear bodies. The B1 box and the RING finger are also required for this nuclear localization. Isoforms lacking a nuclear localization signal are cytoplasmic. Detected in the nucleolus after DNA damage. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein.
- Information by UniProt
- Acure promyelocytic leukemia, inducer of antibody
- MYL antibody
- Pml antibody
ab67761 staining PML in PyV-infected 3T3 cells or PML-/- MEFs (MOI of 10–20 pfu/cell), by Immunohistochemistry (PFA perfusion fixed frozen sections).
At 32 hpi, cells were frozen by high pressure and processed by cryo-substitution for immunoelectron microscopy. Sections were fixed with 0.5% paraformaldehyde for 15 min at 22°C. Sections were blocked in 1% milk/PBST (PBS/0.02% Tween 20) for 30 min at room temperature followed by incubation with primary antibody diluted 1/80 in 1% milk/PBST for 2 hr at 22°C. A gold-conjugated anti-rabbit IgG was used as the secondary antibody (1/20)
ab67761 has been referenced in 3 publications.
- Jiao X et al. Dachshund Depletion Disrupts Mammary Gland Development and Diverts the Composition of the Mammary Gland Progenitor Pool. Stem Cell Reports 12:135-151 (2019). PubMed: 30554919
- Chort A et al. Interferon beta induces clearance of mutant ataxin 7 and improves locomotion in SCA7 knock-in mice. Brain 136:1732-45 (2013). IHC-Fr, WB, IHC-P ; Mouse, Human . PubMed: 23518714
- Erickson KD et al. Virion assembly factories in the nucleus of polyomavirus-infected cells. PLoS Pathog 8:e1002630 (2012). IHC-FoFr . PubMed: 22496654