| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Protein PML;Pml; |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Host | |
| Immunogen | A synthetic peptide corresponding to a sequence at the N-terminus of mouse PML Protein, different from the related human sequence by six amino acids. |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
This antibody is intended for detection of Pml (Protein PML) in biological samples using common immunoassay formats. It is typically selected based on target identity, species reactivity, clonality/clone information, and detection modality.
Vendor notes: Boster Bio Anti-PML Protein Antibody Picoband® catalog # PB10085. Tested in IHC, WB applications. This antibody reacts with Mouse. The brand Picoband indicates this is a premium antibody that guarantees superior quality, high affinity, and strong signals with minimal background in Western blot applications. Only our best-performing antibodies are designated as Picoband, ensuring unmatched performance.
Key elements and design rationale
- Antibody format: Rabbit Polyclonal Rabbit IgG
- Immunogen / epitope context: A synthetic peptide corresponding to a sequence at the N-terminus of mouse PML Protein, different from the related human sequence by six amino acids.
- Molecular weight context: reported MW: 72 kDa, 97 kDa; calculated MW: 98242 MW
- Reactivity: Mouse
- Applications: IHC, WB
As a polyclonal antibody, the reagent recognizes multiple epitopes on the target, which can improve detection robustness but may increase sensitivity to sample-dependent epitope changes.
Biological background
Protein PML; Protein PML. The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. This phosphoprotein localizes to nuclear bodies where it functions as a transcription factor and tumor suppressor. Its expression is cell-cycle related and it regulates the p53 response to oncogenic signals. The gene is often involved in the translocation with the retinoic acid receptor alpha gene associated with acute promyelocytic leukemia (APL). Extensive alternative splicing of this gene results in several variations of the protein's central and C-terminal regions; all variants encode the same N-terminus. Alternatively spliced transcript variants encoding different isoforms have been identified. Functional note: Functions via its association with PML-nuclear bodies (PML-NBs) in a wide range of important cellular processes, including tumor suppression, transcriptional regulation, apoptosis, senescence, DNA damage response, and viral defense mechanisms. Acts as the scaffold of PML-NBs allowing other proteins to shuttle in and out, a process which is regulated by SUMO-mediated modifications and interactions. Positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2- dependent degradation). Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum. Regulates RB1 phosphorylation and activity. Acts as both a negative regulator of PPARGC1A acetylation and a potent activator of PPAR signaling and fatty acid oxidation. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates PER2 nuclear localization and circadian function. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. Required for normal development of the brain cortex during embryogenesis. Plays a role in granulopoiesis or monopoiesis of myeloid progenitor cells. May play a role regulating stem and progenitor cell fate in tissues as diverse as blood, brain and breast. Shows antiviral activity towards lymphocytic choriomeningitis virus (LCMV) and the vesicular stomatitis virus (VSV). . Reported localization: Nucleus . Nucleus, nucleoplasm. Cytoplasm. Nucleus, PML body. Nucleus, nucleolus . Endoplasmic reticulum membrane; Peripheral membrane protein; Cytoplasmic side. Early endosome membrane ; Peripheral membrane protein ; Cytoplasmic side . Detected in the nucleolus after DNA damage. Acetylation at Lys-497 is essential for its nuclear localization. Within the nucleus, most of PML is expressed in the diffuse nuclear fraction of the nucleoplasm and only a small fraction is found in the matrix-associated nuclear bodies (PML-NBs). The transfer of PML from the nucleoplasm to PML-NBs depends on its phosphorylation and sumoylation. The B1 box and the RING finger are also required for the localization in PML-NBs. Also found in specific membrane structures termed mitochondria-associated membranes (MAMs) which connect the endoplasmic reticulum (ER) and the mitochondria (By similarity). . Expression/tissue context: Milk lipid globules.
Research relevance and current trends
- Cancer: Researchers commonly examine how Pml (Protein PML) relates to this theme using model systems and orthogonal readouts.
- Cancer Metabolism: Researchers commonly examine how Pml (Protein PML) relates to this theme using model systems and orthogonal readouts.
- Domain Families: Researchers commonly examine how Pml (Protein PML) relates to this theme using model systems and orthogonal readouts.
Common research applications
- Western blotting: compare relative Pml (Protein PML) levels across conditions; band patterns may reflect isoforms and processing.
- IHC/IHC-F: assess spatial distribution of Pml (Protein PML) across tissue regions and cell types using matched controls.
Notes for experimental interpretation
- Specificity notes: No cross reactivity with other proteins.
- Cross-reactivity: No cross-reactivity with other proteins
- Isoforms and PTMs: Apparent size and signal patterns can differ across splice isoforms, proteolytic processing, and post-translational modifications.
- Controls: Include an isotype control (as relevant), no-primary control for imaging, and orthogonal validation such as KD/KO samples when available.
Customization & Add-ons: Can’t find the antibody you need—or require a custom format for your assay? We can help you source the best match or support custom antibody solutions for diverse research needs, including species and isotype selection, conjugations and labeling (e.g., HRP/AP, biotin, fluorophores), purification grade options (Protein A/G, affinity purified), formulation preferences (buffer selection, carrier-free, glycerol-free), custom concentrations and aliquoting, low-endotoxin options for cell-based work, and application-focused QC/validation support (project dependent). Click Talk to a Scientist to submit a request, email us at support@biohippo.com, or explore our Research Services for additional support—our team will follow up with feasibility details and next steps.
