Product Details

Uniprot No.

Target Names

Alternative Names

Acure promyelocytic leukemia, inducer of antibody; MYL antibody; Pml antibody; PML_HUMAN antibody; PP8675 antibody; Probable transcription factor PML antibody; Promyelocytic leukemia antibody; Promyelocytic leukemia inducer of antibody; Promyelocytic leukemia protein antibody; Protein PML antibody; RING finger protein 71 antibody; RNF 71 antibody; RNF71 antibody; TRIM 19 antibody; Tripartite motif protein TRIM19 antibody; Tripartite motif-containing protein 19 antibody

Species Reactivity

Human

Immunogen

A synthesized peptide derived from human PML

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

4E8

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, IHC, IF, FC

Recommended Dilution

Application	Recommended Dilution
IHC	1:50-1:200
IF	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunohistochemistry (IHC) Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

PML, or promyelocytic leukemia protein, serves as a critical tumor suppressor and the defining component of PML nuclear bodies—dynamic subnuclear structures that regulate diverse cellular processes including apoptosis, senescence, DNA damage response, and antiviral defense. The protein gained its name from its involvement in acute promyelocytic leukemia, where chromosomal translocation creates the oncogenic PML-RARα fusion protein. Beyond oncology, PML research extends into viral pathogenesis, cellular stress responses, and stem cell biology, making it a target of significant interest across multiple disciplines.

This recombinant monoclonal antibody, clone 4E8, offers the consistency and reproducibility that demanding research applications require. Generated against a synthetic peptide derived from human PML and produced using recombinant technology in rabbit host, this antibody provides sequence-defined specificity with minimal lot-to-lot variation—particularly valuable for longitudinal studies or multi-site collaborations where experimental reproducibility is paramount.

Validation across multiple platforms demonstrates this antibody's versatility in your experimental workflows. Immunohistochemistry performed on paraffin-embedded human cervical cancer tissue using a Leica Bond system shows clear target detection at 1:100 dilution with citrate buffer antigen retrieval. Immunofluorescence staining in A-549 lung carcinoma cells reveals the expected nuclear localization pattern characteristic of PML bodies. Flow cytometry analysis using 786-O renal carcinoma cells confirms reliable detection in suspension-based applications, with clear separation from isotype control.

Whether investigating PML's role in leukemogenesis, exploring nuclear body dynamics, or examining stress-induced cellular responses, this antibody provides researchers with a dependable tool for visualizing and quantifying PML across tissue sections, cultured cells, and flow cytometry applications.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Related Products

Target Background

Function

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. Isoform PML-4 has a multifaceted role in the regulation of apoptosis and growth suppression: activates RB1 and inhibits AKT1 via interactions with PP1 and PP2A phosphatases respectively, negatively affects the PI3K pathway by inhibiting MTOR and activating PTEN, and positively regulates p53/TP53 by acting at different levels (by promoting its acetylation and phosphorylation and by inhibiting its MDM2-dependent degradation). Isoform PML-4 also: acts as a transcriptional repressor of TBX2 during cellular senescence and the repression is dependent on a functional RBL2/E2F4 repressor complex, regulates double-strand break repair in gamma-irradiation-induced DNA damage responses via its interaction with WRN, acts as a negative regulator of telomerase by interacting with TERT, and regulates PER2 nuclear localization and circadian function. Isoform PML-6 inhibits specifically the activity of the tetrameric form of PKM. The nuclear isoforms (isoform PML-1, isoform PML-2, isoform PML-3, isoform PML-4 and isoform PML-5) in concert with SATB1 are involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Isoform PML-2 is required for efficient IFN-gamma induced MHC II gene transcription via regulation of CIITA. Cytoplasmic PML is involved in the regulation of the TGF-beta signaling pathway. PML also regulates transcription activity of ELF4 and can act as an important mediator for TNF-alpha- and IFN-alpha-mediated inhibition of endothelial cell network formation and migration.; Exhibits antiviral activity against both DNA and RNA viruses. The antiviral activity can involve one or several isoform(s) and can be enhanced by the permanent PML-NB-associated protein DAXX or by the recruitment of p53/TP53 within these structures. Isoform PML-4 restricts varicella zoster virus (VZV) via sequestration of virion capsids in PML-NBs thereby preventing their nuclear egress and inhibiting formation of infectious virus particles. The sumoylated isoform PML-4 restricts rabies virus by inhibiting viral mRNA and protein synthesis. The cytoplasmic isoform PML-14 can restrict herpes simplex virus-1 (HHV-1) replication by sequestering the viral E3 ubiquitin-protein ligase ICP0 in the cytoplasm. Isoform PML-6 shows restriction activity towards human cytomegalovirus (HHV-5) and influenza A virus strains PR8(H1N1) and ST364(H3N2). Sumoylated isoform PML-4 and isoform PML-12 show antiviral activity against encephalomyocarditis virus (EMCV) by promoting nuclear sequestration of viral polymerase (P3D-POL) within PML NBs. Isoform PML-3 exhibits antiviral activity against poliovirus by inducing apoptosis in infected cells through the recruitment and the activation of p53/TP53 in the PML-NBs. Isoform PML-3 represses human foamy virus (HFV) transcription by complexing the HFV transactivator, bel1/tas, preventing its binding to viral DNA. PML may positively regulate infectious hepatitis C viral (HCV) production and isoform PML-2 may enhance adenovirus transcription. Functions as an E3 SUMO-protein ligase that sumoylates (HHV-5) immediate early protein IE1, thereby participating in the antiviral response. Isoforms PML-3 and PML-6 display the highest levels of sumoylation activity.

Gene References into Functions

these findings uncover a novel mechanism by which PML loss may contribute to mTOR activation and cancer progression via dysregulation of basal DDIT4 gene expression. PMID: 28332630
STAT3 is responsible, at least in part, for the transcriptional upregulation of PML in breast cancer. Moreover, PML targeting hampers breast cancer initiation and metastatic seeding. Mechanistically, this biological activity relies on the regulation of the stem cell gene SOX9 through interaction of PML with its promoter region. PMID: 27553708
Data suggest that intracellular host defenses are counteracted by ICP0, which targets PML for degradation from the outset of nuclear infection to promote viral-DNA release from PML-nuclear bodies and the onset of HSV-1 lytic replication. (ICP0 = immediate early infected polypeptide-0; PML = promyelocytic leukemia protein; HSV-1 = herpes simplex virus-1) PMID: 29309427
the PML(NLS-) protein was detectable in the cytoplasm of neutrophils from patients with acute promyelocytic leukemia. PMID: 28849126
The PML sumo interaction motif differentially affects nuclear body formation by each individual isoform. PMID: 28851805
inhibiting CK2 can enhance sensitivity of Cisplatin to Non-small cell lung carcinoma cells through PML PMID: 28744813
Results show that PolySUMO5 conjugation on K160 of PML results in recruitment of proteins to form PML-nuclear bodies. SUMO5 conjugation on PML is gradually replaced by SUMO2/3 conjugation, which leads to RNF4-mediated disruption of PML-NBs. PMID: 27211601
the ND10 bodies become viral replication compartments, and ICP0, a viral E3 ligase, degrades both PML and SP100. The amounts of PML and SP100 and the number of ND10 structures increase in cells exposed to IFN-beta. PMID: 28439026
These results therefore indicate that EGCG targets PML/RARalpha oncoprotein for degradation and potentiates differentiation of promyelocytic leukemia cells in combination with ATRA via PTEN. PMID: 28766684
study revealed molecular mechanism of responsiveness of the PML-RARA mutations to AS2O3 treatment; mutation S214L disrupted PML-arsenic binding, nuclear body formation, basal SUMOylation and degradation; mutation A216T showed moderate defect in AS2O3 response;, mutants L217F and S220G behave similarly to wild-type; findings suggest distinct mutants of PML-RARA confer varying degree of AS2O3 resistance PMID: 28028657
Silencing of PML-RAR and RARalpha2 results in similar increases in the constitutive expression of several granulocytic differentiation markers. PMID: 27419624
Our findings unveil a novel essential oncogenic activity of PML/RARA in Acute promyelocitic leukemia PMID: 27626703
PML loss promotes tumor development, providing a growth advantage to tumor cells that use autophagy as a cell survival strategy during stress conditions. PMID: 27545895
WDR4 is an oncoprotein that negatively regulates PML via ubiquitination to promote lung cancer progression by fostering an immunosuppressive and prometastatic tumor microenvironment PMID: 28691927
Sumoylation of PML with SUMO2 by UBC9/UBE2I can lead to formation of polymeric SUMO chains. Data suggest that coordination of growing poly-SUMO chain with "back side" binding site on UBC9/UBE2I appears to be required for SUMO chain elongation on PML. (PML = promyelocytic leukemia protein; SUMO2 = small ubiquitin-like modifier 2; UBC9/UBE2I = ubiquitin-conjugating enzyme UBC9/UBE2I) PMID: 28784659
Data show that the cytoplasmic localization of promyelocytic leukaemia (PML) is mediated by its nuclear export in a chromosomal maintenance 1 (CRM1)-dependent manner. PMID: 26549027
this study, we first observed that PML-positive intranuclear aggregates also appeared in controls and were not specific for the Neuronal Intranuclear Hyaline Inclusion Disease cases. PMID: 28863453
TRIB3 promotes acute promyelocytic leukemia progression through stabilization of the oncoprotein PML-RARalpha and inhibition of p53-mediated senescence. PMID: 28486108
Data suggest that the binding of Z-10 to RXRalpha inhibited the interaction of RXRalpha with PML-RARalpha, leading to Z-10's selective induction of PML-RARalpha degradation. PMID: 28129653
PML protein prevents the loss of HPV genome following infection implying that the host cell may be able to recognize chromatinized HPV genome or the associated capsid proteins. PMID: 27860076
findings demonstrate that the PML protein, which mediates an intrinsic immune response against human cytomegalovirus, specifically serves as an E3 ligase for SUMO modification of IE1p72. PMID: 28250117
During infection, PML undergoes oxidation-mediated multimerization, associates with the nuclear matrix, and becomes de-SUMOylated due to the pore-forming activity of the Listeria toxin listeriolysin O (LLO). PMID: 28074026
Data suggest PML (promyelocytic leukemia protein) positively regulates STAT1 and STAT2 isgylation, a ubiquitination-like protein modification; PML exhibits potent angiostatic activity, doing so in part by forming a positive feedforward loop with STAT1/2 and a negative feedback loop with STAT3. (STAT = signal transducer and activator of transcription) PMID: 28432122
PML(nuclear localization signal -) was detected in primary acute promyelocytic leukemia (APL), but not non-APL cells. PML was localized to the nucleus, interacted with importin alpha in vivo, and co-localized in the PML nuclear bodies. PML(NLS-) was primarily localized in the cytoplasm and the interaction with importin alpha was lost PMID: 28075463
These data suggest that CACUL1 is a novel regulator that negatively controls p53 activity through the regulation of PML SUMOylation. PMID: 27889610
An HSV-1 protein, ICP0, can recognize individual host factors and target them differently for destruction. We identified elements that are important for the ICP0 E3 ubiquitin ligase to differentially recognize two of its substrates, isoforms PML I and PML II. PMID: 27681131
In line with these observations, rhesus monkey rhadinovirus infection resulted in rapid degradation of SP100, followed by degradation of PML and the loss of ND10 structures, whereas the protein levels of ATRX and DAXX remained constant. PMID: 27356898
Taken together, these data show that the PML II isoform, through its various actions, has an overall negative effect on the human adenovirus 5 lifecycle. PMID: 27217299
PML-RARa bcr1 fusion is not responsible for colorectal tumor development. PMID: 22167334
PML nuclear bodies change in number and size in cells actively replicating Merkel cell polyomavirus proviral DNA. PMID: 27580912
High PML expression is associated with hepatocellular carcinoma. PMID: 27517564
This study demonstrated an important phosphorylated site of PML, which contributed to explore the role of PML in mitosis. PMID: 27609478
PML acts as an effector of antiviral effects of IFN-beta. PMID: 27162364
The activity of the PML internal ribosome entry site is induced by TNFalpha in a manner that involves MNK1 activation. PMID: 26383972
The association of RNF168 with PML NBs resulted in increased ubiquitylation. PMID: 26675234
Data suggest that hematopoietically expressed homeobox protein (HHEX) downmodulation by promyelocytic leukemia-retinoic acid receptor alpha fusion oncoprotein (PML-RARalpha) is a key event during acute promyelocytic leukemia (APL) pathogenesis. PMID: 27052408
The authors show that PML can inhibit HIV-1 and other lentiviruses as part of the IFN-I-mediated response. PMID: 27000403
PML contributes to the intrinsic restriction of HIV-1 infections in a cell type-dependent manner. PMID: 26703718
Suggest a novel role of PCGF2 in arsenic trioxide-mediated degradation of PML-RARA that PCGF2 might act as a negative regulator of UBE2I via direct interaction. PMID: 27030546
Indicate the important role of PML/c-Myc axis in the maintenance of glioblastoma tumor stem cells. Arsenic trioxide disrupts glioma stem cells via promoting PML degradation to inhibit tumor growth. PMID: 26510911
Our work provides a novel view of the physiologic function of PML, which participates in telomeres surveillance in normal cells. Our data further imply that a diminished PML function may contribute to cell senescence, genomic instability and tumorigenesis PMID: 26119943
Mutations affect both the rearranged and the unrearranged PML alleles in refractory acute promyelocytic leukaemia. PMID: 26728337
Methylated arsenic metabolites bind to PML protein but do not induce cellular differentiation and PML-RARalpha protein degradation in acute promyelocytic leukemia. PMID: 26213848
Novel insight into the functional difference of acquired mutations of PML-RARA both in vitro and in the clinical setting. PMID: 26537301
Authors performed mutational analysis to define a PML interaction motif within the E1B-55K polypeptide. Results showed that E1B-55K/PML binding is not required for p53, Mre11 and Daxx interaction. PMID: 25772236
These data suggest that targeting PML by human herpesvirus 5 IE1 represents a strategy to antagonize both intrinsic and innate immune mechanisms. PMID: 26559840
The results corroborated that PML-II plays a critical role in generating nuclear Lipid droplets in specific cell types. PMID: 26728854
Studies of the dynamics of the response of PML nuclear body components and IFI16 to invading herpes simplex virus 1 genomes demonstrated that human Daxx (hDaxx) and IFI16 respond more rapidly than PML. PMID: 26468536
PML is upregulated in obesity and liver steatosis. PMID: 25999785
(PML) nuclear bodies (APBs) at telomeres promote telomere maintenance by inducing a DNA damage response in ALT-positive tumor cells through changing the telomeric chromatin state to trigger ATM phosphorylation. PMID: 25908860

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Involvement in disease

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.

Subcellular Location

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. Note=Isoform PML-1 can shuttle between the nucleus and cytoplasm. Isoform PML-2, isoform PML-3, isoform PML-4, isoform PML-5 and isoform PML-6 are nuclear isoforms whereas isoform PML-7 and isoform PML-14 lacking the nuclear localization signal are cytoplasmic isoforms. Detected in the nucleolus after DNA damage. Acetylation at Lys-487 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. Sequestered in the cytoplasm by interaction with rabies virus phosphoprotein.

Database Links

HGNC: 9113

OMIM: 102578

KEGG: hsa:5371

STRING: 9606.ENSP00000268058

UniGene: Hs.526464

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Code	CSB-RA171352A0HU
Size	US$210
	Order now
Image	IHC image of CSB-RA171352A0HU diluted at 1:100 and staining in paraffin-embedded human cervical cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Immunofluorescence staining of A-549 cell with CSB-RA171352A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L). Overlay Peak curve showing 786-O cells stained with CSB-RA171352A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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PML Recombinant Monoclonal Antibody

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Target Background