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antisense sequence against pir 19521  (Genechem)

 
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    Structured Review

    Genechem antisense sequence against pir 19521
    Antisense Sequence Against Pir 19521, supplied by Genechem, used in various techniques. Bioz Stars score: 86/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
    https://www.bioz.com/product/antisense+sequences/19521+against+antisense+pir+sequence/pm41109384-72-7-25
    Average 86 stars, based on 1 article reviews
    antisense sequence against pir 19521 - by Bioz Stars, 2026-11
    86/100 stars

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    Related Articles

    Expressing:

    Article Title: piR-19521 facilitates cancer stem cell-like properties by enhancing ALX4 transcription via an enhancer RNA-like mechanism in colorectal cancer.
    Article Snippet: Piwi-interacting RNAs (piRNAs) are critical regulators of stemness maintenance in germline cells and have emerging roles in tumorigenesis.. Our previous study identified piR-19521 as up-regulated in colorectal cancer (CRC), with higher levels correlating with poorer differentiation, implicating a potential role in colorectal cancer stem cells (CR-CSCs).. Here, we explored piR-19521's function in CR-CSC-like properties.

    Sequencing:

    Article Title: piR-19521 facilitates cancer stem cell-like properties by enhancing ALX4 transcription via an enhancer RNA-like mechanism in colorectal cancer.
    Article Snippet: Piwi-interacting RNAs (piRNAs) are critical regulators of stemness maintenance in germline cells and have emerging roles in tumorigenesis.. Our previous study identified piR-19521 as up-regulated in colorectal cancer (CRC), with higher levels correlating with poorer differentiation, implicating a potential role in colorectal cancer stem cells (CR-CSCs).. Here, we explored piR-19521's function in CR-CSC-like properties.

    Control:

    Article Title: piR-19521 facilitates cancer stem cell-like properties by enhancing ALX4 transcription via an enhancer RNA-like mechanism in colorectal cancer.
    Article Snippet: Piwi-interacting RNAs (piRNAs) are critical regulators of stemness maintenance in germline cells and have emerging roles in tumorigenesis.. Our previous study identified piR-19521 as up-regulated in colorectal cancer (CRC), with higher levels correlating with poorer differentiation, implicating a potential role in colorectal cancer stem cells (CR-CSCs).. Here, we explored piR-19521's function in CR-CSC-like properties.

    Construct:

    Article Title: piR-19521 facilitates cancer stem cell-like properties by enhancing ALX4 transcription via an enhancer RNA-like mechanism in colorectal cancer.
    Article Snippet: Piwi-interacting RNAs (piRNAs) are critical regulators of stemness maintenance in germline cells and have emerging roles in tumorigenesis.. Our previous study identified piR-19521 as up-regulated in colorectal cancer (CRC), with higher levels correlating with poorer differentiation, implicating a potential role in colorectal cancer stem cells (CR-CSCs).. Here, we explored piR-19521's function in CR-CSC-like properties.



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    Image Search Results


    tiRNA-Met directly interacted with SNRPA and promoted its ubiquitination. A , B Silver-stained SDS-PAGE gel images showed proteins immunoprecipitated by tiRNA-Met and its antisense RNA in MDA-MB-231 ( A ) and BT-549 ( B ) cell lines. C Western blot analysis of products from RNA pull-down assays using tiRNA-Met sense and antisense confirmed that tiRNA-Met directly associated with SNRPA. D , E RIP followed by RT-qPCR demonstrated specific binding of tiRNA-Met to SNRPA in MDA-MB-231 ( D ) and BT-549 ( E ) cells. F RNA pull-down and western blot assays revealed that tiRNA-Met bound to the RRM2 domain of SNRPA. G The mRNA expression levels of SNRPA remained unchanged in MDA-MB-231 and BT-549 cells transfected with tiRNA-Met mimics or inhibitor. H Overexpression of tiRNA-Met reduced SNRPA protein levels in both cell lines, while inhibition of tiRNA-Met increased SNRPA protein levels. I MDA-MB-231 cells treated with cycloheximide (Chx; 5 μM) and then transfected with tiRNA-Met mimics exhibited a reduced half-life of endogenous SNRPA protein, as shown by western blot; β-actin served as a loading control. J Treatment with MG132 (20 μg/ml) led to a progressive increase in SNRPA protein levels over time; β-actin was used as a reference. K Immunoprecipitation assays indicated that the binding of SNRPA to ubiquitinated proteins was elevated in MDA-MB-231 cells transfected with tiRNA-Met mimics. All data are presented as means ± SD; ns, P > 0.05; * P < 0.05; ** P < 0.01; **** P < 0.0001

    Journal: Cellular & Molecular Biology Letters

    Article Title: The novel tRNA-derived fragment, tiRNA-Met, inhibits the malignant progression of triple-negative breast cancer by regulating RANBP3L via a targeted interaction with SNRPA

    doi: 10.1186/s11658-025-00738-2

    Figure Lengend Snippet: tiRNA-Met directly interacted with SNRPA and promoted its ubiquitination. A , B Silver-stained SDS-PAGE gel images showed proteins immunoprecipitated by tiRNA-Met and its antisense RNA in MDA-MB-231 ( A ) and BT-549 ( B ) cell lines. C Western blot analysis of products from RNA pull-down assays using tiRNA-Met sense and antisense confirmed that tiRNA-Met directly associated with SNRPA. D , E RIP followed by RT-qPCR demonstrated specific binding of tiRNA-Met to SNRPA in MDA-MB-231 ( D ) and BT-549 ( E ) cells. F RNA pull-down and western blot assays revealed that tiRNA-Met bound to the RRM2 domain of SNRPA. G The mRNA expression levels of SNRPA remained unchanged in MDA-MB-231 and BT-549 cells transfected with tiRNA-Met mimics or inhibitor. H Overexpression of tiRNA-Met reduced SNRPA protein levels in both cell lines, while inhibition of tiRNA-Met increased SNRPA protein levels. I MDA-MB-231 cells treated with cycloheximide (Chx; 5 μM) and then transfected with tiRNA-Met mimics exhibited a reduced half-life of endogenous SNRPA protein, as shown by western blot; β-actin served as a loading control. J Treatment with MG132 (20 μg/ml) led to a progressive increase in SNRPA protein levels over time; β-actin was used as a reference. K Immunoprecipitation assays indicated that the binding of SNRPA to ubiquitinated proteins was elevated in MDA-MB-231 cells transfected with tiRNA-Met mimics. All data are presented as means ± SD; ns, P > 0.05; * P < 0.05; ** P < 0.01; **** P < 0.0001

    Article Snippet: Biotin-labeled tiRNA-Met sense and antisense sequences were obtained from Genescript (Nanjing, China).

    Techniques: Ubiquitin Proteomics, Staining, SDS Page, Immunoprecipitation, Western Blot, Quantitative RT-PCR, Binding Assay, Expressing, Transfection, Over Expression, Inhibition, Control