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anti-Human PML Antibodies:
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Human Polyclonal PML Primary Antibody for ICC, IF - ABIN252967
Wimmer, Schreiner, Everett, Sirma, Groitl, Dobner: SUMO modification of E1B-55K oncoprotein regulates isoform-specific binding to the tumour suppressor protein PML. in Oncogene 2010
Show all 21 Pubmed References
Human Polyclonal PML Primary Antibody for ICC, IF - ABIN4346484
Campagna, Herranz, Garcia, Marcos-Villar, González-Santamaría, Gallego, Gutierrez, Collado, Serrano, Esteban, Rivas: SIRT1 stabilizes PML promoting its sumoylation. in Cell death and differentiation 2010
Show all 3 Pubmed References
Human Polyclonal PML Primary Antibody for ICC, IF - ABIN252968
Kuroki, Ariumi, Ikeda, Dansako, Wakita, Kato: Arsenic trioxide inhibits hepatitis C virus RNA replication through modulation of the glutathione redox system and oxidative stress. in Journal of virology 2009
Show all 2 Pubmed References
Human Polyclonal PML Primary Antibody for ELISA, ICC - ABIN6264315
Wu, Shao, Zhou, Sun, Wang, Yan, Liu, Wu, Ye, Huang, Zhou et al.: Autophagy and Ubiquitin-Mediated Proteolytic Degradation of PML/Rarα Fusion Protein in Matrine-Induced Differentiation Sensitivity Recovery of ATRA-Resistant APL (NB4-LR1) Cells: in Vitro and in Vivo ... in Cellular physiology and biochemistry : international journal of experimental cellular physiology, biochemistry, and pharmacology 2018
Mouse (Murine) Monoclonal PML Primary Antibody for ICC, IF - ABIN2668256
Evdokimov, Sharma, Lockett, Lualdi, Kuehn: Loss of SUMO1 in mice affects RanGAP1 localization and formation of PML nuclear bodies, but is not lethal as it can be compensated by SUMO2 or SUMO3. in Journal of cell science 2008
these findings uncover a novel mechanism by which PML loss may contribute to mTOR (show FRAP1 Antibodies) activation and cancer progression via dysregulation of basal DDIT4 (show DDIT4 Antibodies) gene expression.
This study establishes PML as an important regulator of NF-kappaB (show NFKB1 Antibodies) and demonstrates that PML-RARalpha (show RARA Antibodies) dysregulates NF-kappaB (show NFKB1 Antibodies).
STAT3 (show STAT3 Antibodies) 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 (show SOX9 Antibodies) through interaction of PML with its promoter region.
Respiratory syncytial virus induces NRF2 (show GABPA Antibodies) degradation through a PML-RNF4 (show RNF4 Antibodies) pathway.
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 (show JUN Antibodies) infected polypeptide-0; PML = promyelocytic leukemia protein; HSV-1 = herpes simplex virus-1)
the PML(NLS (show ALDH1A2 Antibodies)-) protein was detectable in the cytoplasm of neutrophils from patients with acute promyelocytic leukemia.
The PML sumo interaction motif differentially affects nuclear body formation by each individual isoform.
inhibiting CK2 (show CSNK2A1 Antibodies) can enhance sensitivity of Cisplatin to Non-small cell lung carcinoma cells through PML
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 (show SUMO2 Antibodies)/3 conjugation, which leads to RNF4 (show RNF4 Antibodies)-mediated disruption of PML-NBs (show NBN Antibodies).
the ND10 bodies become viral replication compartments, and ICP0, a viral E3 ligase, degrades both PML and SP100 (show SP100 Antibodies). The amounts of PML and SP100 (show SP100 Antibodies) and the number of ND10 structures increase in cells exposed to IFN-beta (show IFNB1 Antibodies).
PML mediates the binding of PER2 (show PER2 Antibodies) to BMAL1 (show ARNTL Antibodies) in the BMAL1 (show ARNTL Antibodies)/CLOCK heterodimer and is an important component in the organization of a functional clock complex in the nucleus.
Promyelocytic leukemia protein Pml -/- cells showed a higher proliferation rate, compared to Pml +/+ cells.
PML protein organizes heterochromatin domains where it regulates histone H3.3 (show H3F3A Antibodies) deposition by ATRX (show ATRX Antibodies) and DAXX (show DAXX Antibodies).
Data indicate that promyelocytic leukemia protein knockout (Pml-/-) animals fail to properly activate oxidative stress-responsive p53 (show TP53 Antibodies) targets, whereas the NRF2 (show NFE2L2 Antibodies) response is amplified and accelerated.
data support a model in which activation of myogenic differentiation results in PML NB loss, chromatin reorganization and DAXX (show DAXX Antibodies) relocalization, and provides a paradigm for understanding the consequence of PML loss in other cellular contexts, such as during cancer development and progression
a regulatory role of ZNF451 (show ZNF451 Antibodies)-1 in fine-tuning physiological PML levels
PML loss promotes tumor development, providing a growth advantage to tumor cells that use autophagy as a cell survival strategy during stress conditions.
The data demonstrate a dual role of PML in protection and recovery after brain injury.
This study designates PML protein and PML-NBs (show NLRP2 Antibodies) to be major cellular components involved in the control of Herpes simplex virus 1 (HSV-1) latency, probably during the entire life of an individual.
Study found that Promyelocytic leukemia protein (PML) is broadly expressed across the gray matter, with the highest levels in the cerebral and cerebellar cortices. PML bodies are broadly involved in activity-dependent nuclear phenomena in adult neurons
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.
RING finger protein 71
, probable transcription factor PML
, promyelocytic leukemia protein
, promyelocytic leukemia, inducer of
, protein PML
, tripartite motif protein TRIM19
, tripartite motif-containing protein 19
, promyelocytic leukemia
, probable transcription factor PML-like