PML sirna

PML siRNA (Human)

Cat. Num. AAA827040

• Gene Names: PML; MYL; RNF71; PP8675; TRIM19
• Reactivity: Human
• Applications: RNA Interference (RNAi)
• Purity: > 97%
• Synonyms: PML; PML siRNA (Human); MYL; PP8675; RNF71; TRIM19; Protein PML; Promyelocytic leukemia protein; RING finger protein 71; Tripartite motif-containing protein 19; PML sirna

• Host: Synthetic
• Reactivity: Human
• Specificity: PML siRNA (Human) is a target-specific 19-23 nt siRNA oligo duplexes designed to knock down gene expression.
• Purity/Purification: > 97%
• Form/Format: Lyophilized powder
• Sequence Length: 633

• Applicable Applications for PML sirna: RNA Interference (RNAi)
• Quality Control: Oligonucleotide synthesis is monitored base by base through trityl analysis to ensure appropriate coupling efficiency. The oligo is subsequently purified by affinity-solid phase extraction. The annealed RNA duplex is further analyzed by mass spectrometry to verify the exact composition of the duplex. Each lot is compared to the previous lot by mass spectrometry to ensure maximum lot-to-lot consistency.
• Directions for Use: We recommends transfection with 100 nM siRNA 48 to 72 hours prior to cell lysis. Before resuspending, briefly centrifuge the tube to ensure the lyophilized siRNA is at the bottom of the tube. Resuspend the siRNA oligos to an appropriate concentration with DEPC water. For each vial, suitable for 250 transfections in 24 well plate (20 pmol for each well).
• Components: We offer pre-designed sets of 3 different target-specific siRNA oligo duplexes of human PML gene. Each vial contains 5 nmol of lyophilized siRNA. The duplexes can be transfected individually or pooled together to achieve knockdown of the target gene, which is most commonly assessed by qPCR or western blot. Our siRNA oligos are also chemically modified (2'-OMe) at no extra charge for increased stability and enhanced knockdown in vitro and in vivo.
• Preparation and Storage: Shipped at 4 degree C. Store at -20 degree C for one year.

Related Product Information for PML sirna

siRNA to inhibit PML expression using RNA interference

NCBI and Uniprot Product Information

• NCBI GI #: 4505903
• NCBI GeneID: 5371
• NCBI Accession #: NP_002666.1
• NCBI GenBank Nucleotide #: NM_002675.3
• UniProt Accession #: P29590; P29591; P29592; P29593; Q00755; Q15959; Q59FP9; Q8WUA0; Q96S41; Q9BPW2; Q9BWP7; E9PBR7
• Molecular Weight: 47,575 Da
• NCBI Official Full Name: protein PML isoform 6
• NCBI Official Synonym Full Names: promyelocytic leukemia
• NCBI Official Symbol: PML
• NCBI Official Synonym Symbols: MYL; RNF71; PP8675; TRIM19
• NCBI Protein Information: protein PML
• UniProt Protein Name: Protein PML
• Protein Family: Protein
• UniProt Gene Name: PML
• UniProt Synonym Gene Names: MYL; PP8675; RNF71; TRIM19
• UniProt Entry Name: PML_HUMAN

NCBI Description

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. [provided by RefSeq, Jul 2008]

Uniprot Description

PML: a zinc-finger protein that can regulate transcription and can localize to nuclear bodies. Cytoplasmic forms regulate glycolysis by inhibiting the tetrameric form of PKM2. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Interacts with SIRT1, TOPBP1, TRIM27 and TRIM69. Sumoylated forms interact with SATB1 and localize to the PML nuclear bodies. Sumoylation on three sites is required for nuclear body formation. Sumoylation on Lys-160 is a prerequisite for sumoylation on Lys-65. The B1 box and the RING finger are also required for localization to nuclear bodies. May play an important role in recruitment of ELF4 into PML nuclear bodies. A chromosomal aberration involving PML can cause acute promyelocytic leukemia (APL). Seven alternatively-spliced human isoforms have been reported.

Protein type: Tumor suppressor; Transcription factor; Oncoprotein; Nucleolus; Ubiquitin conjugating system

Chromosomal Location of Human Ortholog: 15q22

Cellular Component: nucleoplasm; PML body; nuclear membrane; nuclear matrix; early endosome membrane; cytoplasm; nucleolus; nucleus; cytosol

Molecular Function: protein binding; protein homodimerization activity; DNA binding; SUMO binding; zinc ion binding; protein heterodimerization activity; ubiquitin protein ligase binding; transcription coactivator activity; SMAD binding; cobalt ion binding

Biological Process: retinoic acid receptor signaling pathway; proteasomal ubiquitin-dependent protein catabolic process; viral reproduction; apoptosis; positive regulation of apoptosis involved in mammary gland involution; regulation of MHC class I biosynthetic process; PML body organization and biogenesis; SMAD protein nuclear translocation; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest; entrainment of circadian clock by photoperiod; negative regulation of cell proliferation; positive regulation of histone deacetylation; regulation of transcription, DNA-dependent; transforming growth factor beta receptor signaling pathway; response to gamma radiation; negative regulation of mitotic cell cycle; protein complex assembly; circadian regulation of gene expression; maintenance of protein localization in nucleus; cell cycle arrest; negative regulation of telomere maintenance via telomerase; defense response to virus; DNA damage response, signal transduction by p53 class mediator resulting in induction of apoptosis; response to UV; caspase activation; regulation of protein amino acid phosphorylation; cell fate commitment; transcription, DNA-dependent; protein stabilization; cytokine and chemokine mediated signaling pathway; common-partner SMAD protein phosphorylation; regulation of circadian rhythm; negative regulation of telomerase activity; negative regulation of angiogenesis; endoplasmic reticulum calcium ion homeostasis; DNA damage response, signal transduction resulting in induction of apoptosis; response to cytokine stimulus; response to hypoxia; innate immune response; myeloid cell differentiation; negative regulation of translation in response to oxidative stress; negative regulation of cell growth; negative regulation of transcription, DNA-dependent; positive regulation of defense response to virus by host; induction of apoptosis by oxidative stress; protein targeting