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Mouse Anti-DCPS Recombinant Antibody (1E6) (V2LY-0125-LY1227)


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Summary

Host Animal
Mouse
Specificity
Human, Mouse, Rat
Clone
1E6
Antibody Isotype
IgG1, κ
Application
WB, IP, IF, ELISA

Basic Information

Immunogen
Amino acids 273-311 near the C-terminus of human DcpS.
Host Species
Mouse
Specificity
Human, Mouse, Rat
Antibody Isotype
IgG1, κ
Clonality
Monoclonal Antibody
Application Notes
ApplicationNote
WB1:100-1:1,000
IP1-2 μg per 100-500 μg of total protein (1 mL of cell lysate)
IF(ICC)1:50-1:500
ELISA1:100-1:1,000

Formulations & Storage [For reference only, actual COA shall prevail!]

Format
Liquid
Buffer
Gelatin & PBS
Preservative
Sodium Azide
Concentration
0.2 mg/mL
Purity
>95% as determined by analysis by SDS-PAGE
Storage
Store at +4°C short term (1-2 weeks). Aliquot and store at -20°C long term. Avoid repeated freezethaw cycles.

Target

Full Name
decapping enzyme, scavenger
Entrez Gene ID
Human28960
Mouse69305
Rat266605
UniProt ID
HumanQ96C86
MouseQ9DAR7
RatQ8K4F7
Function
Decapping scavenger enzyme that catalyzes the cleavage of a residual cap structure following the degradation of mRNAs by the 3'->5' exosome-mediated mRNA decay pathway. Hydrolyzes cap analog structures like 7-methylguanosine nucleoside triphosphate (m7GpppG) with up to 10 nucleotide substrates (small capped oligoribonucleotides) and specifically releases 5'-phosphorylated RNA fragments and 7-methylguanosine monophosphate (m7GMP). Cleaves cap analog structures like tri-methyl guanosine nucleoside triphosphate (m3(2,2,7)GpppG) with very poor efficiency. Does not hydrolyze unmethylated cap analog (GpppG) and shows no decapping activity on intact m7GpppG-capped mRNA molecules longer than 25 nucleotides. Does not hydrolyze 7-methylguanosine diphosphate (m7GDP) to m7GMP (PubMed:22985415).

May also play a role in the 5'->3 mRNA decay pathway; m7GDP, the downstream product released by the 5'->3' mRNA mediated decapping activity, may be also converted by DCPS to m7GMP (PubMed:14523240).

Binds to m7GpppG and strongly to m7GDP. Plays a role in first intron splicing of pre-mRNAs. Inhibits activation-induced cell death.
Biological Process
Cellular response to menadione Source: UniProtKB
Deadenylation-dependent decapping of nuclear-transcribed mRNA Source: GO_Central
Exonucleolytic catabolism of deadenylated mRNA Source: Reactome
mRNA cis splicing, via spliceosome Source: UniProtKB
Negative regulation of programmed cell death Source: UniProtKB
Nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
Cellular Location
Cytoplasm; Nucleus. Predominantly localized in the nucleus. Nucleocytoplasmic shuttling protein that can transiently enter the cytoplasm in mammalian cells in a XPO1/CRM1-dependent manner.
Involvement in disease
Al-Raqad syndrome (ARS):
A syndrome characterized by delayed psychomotor development, moderate to severe intellectual disability, poor or absent speech, microcephaly, congenital hypotonia, and severe growth delay.
More Infomation

Salamon, I., Palsule, G., Luo, X., Roque, A., Tucai, S., Khosla, I., ... & Kiledjian, M. (2022). mRNA-decapping associated DcpS enzyme controls critical steps of neuronal development. Cerebral Cortex, 32(7), 1494-1507.

Fuchs, A. L., Wurm, J. P., Neu, A., & Sprangers, R. (2020). Molecular basis of the selective processing of short mRNA substrates by the DcpS mRNA decapping enzyme. Proceedings of the National Academy of Sciences, 117(32), 19237-19244.

Ferenc-Mrozek, A., Bojarska, E., Stepinski, J., Darzynkiewicz, E., & Lukaszewicz, M. (2020). Effect of the His-tag location on decapping scavenger enzymes and their hydrolytic activity toward cap analogs. ACS omega, 5(19), 10759-10766.

Wulf, M. G., Buswell, J., Chan, S. H., Dai, N., Marks, K., Martin, E. R., ... & Schildkraut, I. (2019). The yeast scavenger decapping enzyme DcpS and its application for in vitro RNA recapping. Scientific reports, 9(1), 1-9.

Mei, Z. Z., Sun, H., Ou, X., Li, L., Cai, J., Hu, S., ... & Jiang, Y. (2019). The natural antisense transcript NATTD regulates the transcription of decapping scavenger (DcpS) enzyme. The International Journal of Biochemistry & Cell Biology, 110, 103-110.

Pietrow, P., Ferenc-Mrozek, A., Piecyk, K., Bojarska, E., Darzynkiewicz, E., & Jankowska-Anyszka, M. (2019). Decapping Scavenger Enzyme Activity toward N2-Substituted 5′ End mRNA Cap Analogues. ACS omega, 4(17), 17576-17580.

Yamauchi, T., Masuda, T., Canver, M. C., Seiler, M., Semba, Y., Shboul, M., ... & Maeda, T. (2018). Genome-wide CRISPR-Cas9 screen identifies leukemia-specific dependence on a pre-mRNA metabolic pathway regulated by DCPS. Cancer cell, 33(3), 386-400.

Cherry, J. J., DiDonato, C. J., Androphy, E. J., Calo, A., Potter, K., Custer, S. K., ... & Tones, M. A. (2017). In vitro and in vivo effects of 2, 4 diaminoquinazoline inhibitors of the decapping scavenger enzyme DcpS: context-specific modulation of SMN transcript levels. PloS one, 12(9), e0185079.

Gopalsamy, A., Narayanan, A., Liu, S., Parikh, M. D., Kyne Jr, R. E., Fadeyi, O., ... & Jones, L. H. (2017). Design of potent mRNA decapping scavenger enzyme (DcpS) inhibitors with improved physicochemical properties to investigate the mechanism of therapeutic benefit in spinal muscular atrophy (SMA). Journal of medicinal chemistry, 60(7), 3094-3108.

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For research use only. Not intended for any clinical use.

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