This webpage contains legacy information. The product is either no longer available from the supplier or has been delisted at Labome.
product summary
company name :
EMD Millipore
other brands :
Oncogene Research Products, Calbiochem, Novagen, Merck, Upstate Biotechnology, Chemicon, LINCO, Novabiochem, Guava
product type :
antibody
product name :
PML Antibody, clone 36.1-104
catalog :
MAB3738
quantity :
100 μL
clonality :
monoclonal
host :
mouse
conjugate :
nonconjugated
clone name :
36.1-104

The same clone is also sold as:
reactivity :
human, mouse
application :
western blot, immunocytochemistry, immunoprecipitation, immunohistochemistry - paraffin section, immunocytochemistry knockout validation
citations: 16
Published Application/Species/Sample/DilutionReference
  • immunocytochemistry knockout validation; mouse; loading ...; fig 1a
  • western blot; human; loading ...; fig 5c
Guarnerio J, Mendez L, Asada N, Menon A, Fung J, Berry K, et al. A non-cell-autonomous role for Pml in the maintenance of leukemia from the niche. Nat Commun. 2018;9:66 pubmed publisher
  • immunohistochemistry - paraffin section; mouse; loading ...; fig 1a
Niwa Kawakita M, Ferhi O, Soilihi H, Le Bras M, Lallemand Breitenbach V, de Thé H. PML is a ROS sensor activating p53 upon oxidative stress. J Exp Med. 2017;214:3197-3206 pubmed publisher
  • immunocytochemistry; human; 1:100; fig 6
  • immunocytochemistry; mouse; 1:100; fig 6
Kargaran P, Yasaei H, Anjomani Virmouni S, Mangiapane G, Slijepcevic P. Analysis of alternative lengthening of telomere markers in BRCA1 defective cells. Genes Chromosomes Cancer. 2016;55:864-76 pubmed publisher
  • immunocytochemistry; mouse; fig 3
  • western blot; mouse; fig 1
Golov A, Gavrilov A, Razin S. The Role of Crowding Forces in Juxtaposing β-Globin Gene Domain Remote Regulatory Elements in Mouse Erythroid Cells. PLoS ONE. 2015;10:e0139855 pubmed publisher
  • western blot; mouse; 1:500; fig 4b
Pencik J, Schlederer M, Gruber W, Unger C, Walker S, Chalaris A, et al. STAT3 regulated ARF expression suppresses prostate cancer metastasis. Nat Commun. 2015;6:7736 pubmed publisher
  • immunocytochemistry; mouse
Münch S, Weidtkamp Peters S, Klement K, Grigaravicius P, Monajembashi S, Salomoni P, et al. The tumor suppressor PML specifically accumulates at RPA/Rad51-containing DNA damage repair foci but is nonessential for DNA damage-induced fibroblast senescence. Mol Cell Biol. 2014;34:1733-46 pubmed publisher
  • immunohistochemistry - paraffin section; mouse; 1:50
Milman P, Woulfe J. Novel variant of neuronal intranuclear rodlet immunoreactive for 40 kDa huntingtin associated protein and ubiquitin in the mouse brain. J Comp Neurol. 2013;521:3832-46 pubmed publisher
  • western blot; mouse
Evdokimov E, Sharma P, Lockett S, Lualdi M, Kuehn M. 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. J Cell Sci. 2008;121:4106-13 pubmed publisher
Cohen C, Corpet A, Roubille S, Maroui M, Poccardi N, Rousseau A, et al. Promyelocytic leukemia (PML) nuclear bodies (NBs) induce latent/quiescent HSV-1 genomes chromatinization through a PML NB/Histone H3.3/H3.3 Chaperone Axis. PLoS Pathog. 2018;14:e1007313 pubmed publisher
Guo S, Cheng X, Lim J, Liu Y, Kao H. Control of antioxidative response by the tumor suppressor protein PML through regulating Nrf2 activity. Mol Biol Cell. 2014;25:2485-98 pubmed publisher
Talluri S, Francis S, Dick F. Mutation of the LXCXE binding cleft of pRb facilitates transformation by ras in vitro but does not promote tumorigenesis in vivo. PLoS ONE. 2013;8:e72236 pubmed publisher
Berscheminski J, Groitl P, Dobner T, Wimmer P, Schreiner S. The adenoviral oncogene E1A-13S interacts with a specific isoform of the tumor suppressor PML to enhance viral transcription. J Virol. 2013;87:965-77 pubmed publisher
Neault M, Mallette F, Vogel G, Michaud Levesque J, Richard S. Ablation of PRMT6 reveals a role as a negative transcriptional regulator of the p53 tumor suppressor. Nucleic Acids Res. 2012;40:9513-21 pubmed publisher
Cho G, Lim Y, Golden J. SUMO interaction motifs in Sizn1 are required for promyelocytic leukemia protein nuclear body localization and for transcriptional activation. J Biol Chem. 2009;284:19592-600 pubmed publisher
Song M, Salmena L, Carracedo A, Egia A, Lo Coco F, Teruya Feldstein J, et al. The deubiquitinylation and localization of PTEN are regulated by a HAUSP-PML network. Nature. 2008;455:813-7 pubmed publisher
Miller R, Cirulli V, Diaferia G, Ninniri S, Hardiman G, Torbett B, et al. Switching-on survival and repair response programs in islet transplants by bone marrow-derived vasculogenic cells. Diabetes. 2008;57:2402-12 pubmed publisher
product information
Catalog Number :
MAB3738
Subcategory :
Epigenetics & Nuclear Function
Product Name :
Anti-PML Antibody, clone 36.1-104
Product Type :
Antibodies
Clonality :
Monoclonal Antibody
Gene ID :
P29590
Host Name :
Mouse
Antigen :
PML
Clone :
36.1-104
Conjugate :
Ascites
Isotype :
IgG2b
Product Description :
Anti-PML Antibody, clone 36.1-104
Cross Reactivity :
Mouse
Background :
PML protein is a tripartite motif (TRIM)-containing nuclear protein that may function as, among other things, a transcription factor, a coactivator of nuclear receptors (Ruggerio, 2000), a regulator of apoptosis (Guo, 2000), a mediator of interferon-induced antiviral response (Regand and Chelbi-Aliz, 2001), and as a suppressor of growth and oncogenic transformation (Mu, 1997). PML is localized to the nucleoplasm and in distinct subnuclear structures referred to as Promyelocytic Leukemia Bodies (also known as Nuclear Domain 10). Localization of PML to Promyelocytic Leukemia Bodies requires modification of PML protein by the Small Ubiquitin Modifier (SUMO) and is required for proper formation and integrity of these subnuclear structures. At least 14 splice variants of PML ranging in molecular weight from 48-97 kDa (predicted) have been described in the literature. The functional significance of the various splice variants is not well understood. In patients with Acute Promyelocytic Leukemia, the PML gene is involved in at least two specific chromosomal translocations that result in the expression of chimeric proteins with the Retinoic Acid Receptor alpha (RARalpha DNA- and Hormone-binding domains; Pandolfi, 2001). All isoforms of PML, as well as the PML-RARalpha chimeric proteins expressed in Type A and Type B APL contain an identical N-terminus but vary in the C-terminal portion of the protein (Jenson, 2001).
ALT Names :
Promyelocytic Leukemia Protein; Tripartite Motif Protein 19
Immunogen :
His-tagged PML fusion protein corresponding to amino acids 1-581 of mouse PML.
Specificity :
Recognizes mouse PML (Promyelocytic Leukemia protein). On western blots of protein extracts from mouse embryo fibroblast (MEF1 cells), MAB3738 recognizes a band migrating at approximately 106 kDa corresponding to PML.
Package Size :
100 μL
Uses :
Immunocytochemistry;Immunoprecipitation;Western Blotting
Storage :
Maintain for 1 year at -20°C from date of shipment. Aliquot to avoid repeated freezing and thawing. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
company information
EMD Millipore
290 Concord Road
Billerica, Massachusetts 01821
bioscienceshelp@emdchemical.com
https://www.emdmillipore.com
888-854-3417
headquarters: United States
EMD Millipore is the Life Science division of Merck KGaA of Darmstadt, Germany

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