MAB3738
Anti-PML Antibody, clone 36.1-104
ascites fluid, clone 36.1-104, Chemicon®
Synonym(s):
Promyelocytic Leukemia Protein, Tripartite Motif Protein 19
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About This Item
UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Product Name
Anti-PML Antibody, clone 36.1-104, ascites fluid, clone 36.1-104, Chemicon®
biological source
mouse
conjugate
unconjugated
antibody form
ascites fluid
antibody product type
primary antibodies
clone
36.1-104, monoclonal
species reactivity
mouse
should not react with
human
manufacturer/tradename
Chemicon®
technique(s)
immunocytochemistry: suitable
immunoprecipitation (IP): suitable
western blot: suitable
isotype
IgG2b
NCBI accession no.
UniProt accession no.
shipped in
dry ice
target post-translational modification
unmodified
Gene Information
human ... PML(5371)
Analysis Note
Control
POSITIVE CONTROL: Mouse embryo fibroblasts (MEF1 cells).
POSITIVE CONTROL: Mouse embryo fibroblasts (MEF1 cells).
Application
Anti-PML Antibody, clone 36.1-104 is a Mouse Monoclonal Antibody for detection of PML also known as Promyelocytic Leukemia Protein & has been validated in ICC, IP & WB.
Research Category
Epigenetics & Nuclear Function
Epigenetics & Nuclear Function
Research Sub Category
Transcription Factors
Transcription Factors
Western blot (1:500)
Immunoprecipitation
Immunocytochemistry (1:100)
Optimal working dilutions must be determined by end user.
Immunoprecipitation
Immunocytochemistry (1:100)
Optimal working dilutions must be determined by end user.
Biochem/physiol Actions
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.
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
General description
106 kDa
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).
Immunogen
His-tagged PML fusion protein corresponding to amino acids 1-581 of mouse PML.
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Physical form
Ascites fluid containing no preservatives.
Unpurified
Preparation Note
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.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
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Storage Class
10 - Combustible liquids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Tracy Dagher et al.
The Journal of experimental medicine, 218(2) (2020-10-20)
Interferon α (IFNα) is used to treat JAK2V617F-driven myeloproliferative neoplasms (MPNs) but rarely clears the disease. We investigated the IFNα mechanism of action focusing on PML, an interferon target and key senescence gene whose targeting by arsenic trioxide (ATO) drives
Arkadiy K Golov et al.
PloS one, 10(10), e0139855-e0139855 (2015-10-06)
The extremely high concentration of macromolecules in a eukaryotic cell nucleus indicates that the nucleoplasm is a crowded macromolecular solution in which large objects tend to gather together due to crowding forces. It has been shown experimentally that crowding forces
Marie-Odile Baudement et al.
Genome research, 28(11), 1733-1746 (2018-10-06)
The mammalian cell nucleus contains numerous discrete suborganelles named nuclear bodies. While recruitment of specific genomic regions into these large ribonucleoprotein (RNP) complexes critically contributes to higher-order functional chromatin organization, such regions remain ill-defined. We have developed the high-salt-recovered sequences-sequencing
Sonia Missiroli et al.
Cell reports, 16(9), 2415-2427 (2016-08-23)
The precise molecular mechanisms that coordinate apoptosis and autophagy in cancer remain to be determined. Here, we provide evidence that the tumor suppressor promyelocytic leukemia protein (PML) controls autophagosome formation at mitochondria-associated membranes (MAMs) and, thus, autophagy induction. Our in vitro and
Ming Chen et al.
Nature genetics, 50(2), 206-218 (2018-01-18)
Lipids, either endogenously synthesized or exogenous, have been linked to human cancer. Here we found that PML is frequently co-deleted with PTEN in metastatic human prostate cancer (CaP). We demonstrated that conditional inactivation of Pml in the mouse prostate morphs
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