Mouse Anti-CPSF3 Recombinant Antibody (CBFYC-2165) (V2LY-1206-LY988)

Name: Mouse Anti-CPSF3 Recombinant Antibody (CBFYC-2165)
SKU: V2LY-1206-LY988
Rating: 5 (1 reviews)

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Published Data

Mouse Anti-CPSF3 Recombinant Antibody (CBFYC-2165) (V2LY-1206-LY988) in Immunoblot

The mRNA expression level of splicing factors CPSF3, SRSF1 and HNRNPA3 in CHP-134 and GI-ME-N cell lines. Significance was calculated with an unpaired t-test. Results are the mean values ± SD; n = 3 independent experiments (each with three technical replicates). Immunoblot showing the protein expression levels of MYCN and E2F1 in the CHP-134 and GI-ME-N cell lines. GAPDH served as a loading control for this experiment. ...View More

Bate-Eya, L. T., Albayrak, G., Carr, S. M., Shrestha, A., Kanapin, A., Samsonova, A., & La Thangue, N. B. (2024). Sustained cancer-relevant alternative RNA splicing events driven by PRMT5 in high-risk neuroblastoma. Molecular Oncology.

Distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Mouse Anti-CPSF3 Recombinant Antibody (CBFYC-2165) (V2LY-1206-LY988) in IF

(Left) DAPI, anti-CPSF3 and anti-α tubulin staining in axons and cell bodies of sympathetic neurons. Scale bar=10μm. (Right) RT-PCR of mRNA isolated from axons and cell bodies of sympathetic neurons cultured in compartmentalised chambers. The absence of cell body material in axonal samples was assessed using primers amplifying Histone H4 transcripts. Noncontiguous lanes from the same experiment and gels are shown side by side, as indicated by lines in the figure. ...View More

Andreassi, C., Luisier, R., Crerar, H., Darsinou, M., Blokzijl-Franke, S., Lenn, T., ... & Riccio, A. (2021). Cytoplasmic cleavage of IMPA1 3' UTR is necessary for maintaining axon integrity. Cell Reports, 34(8).

Distributed under Open Access license CC BY 4.0, without modification.

Datasheet

SDS

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Datasheet Target References Q & As Review & reward Protocols Associated Products

Basic Information

Host Animal

Mouse

Clone

CBFYC-2165

Application

WB, IP, IF, ELISA

Immunogen

Amino acids 418-562 mapping within an internal region of human CPSF3.

Host Species

Mouse

Specificity

Human, Mouse, Rat, Dog, Cattle, Pig, Horse

Antibody Isotype

IgG1, κ

Clonality

Monoclonal Antibody

Application Notes

Application	Note
WB	1:100-1:1,000
IP	1-2 µg per 100-500 µg of total protein (1 ml of cell lysate)
IF(ICC)	1:50-1:500
ELISA	1:100-1:1,000

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

Format

Liquid

Buffer

0.1% gelatin

Preservative

0.09% 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.

More Infomation

Target

Full Name

cleavage and polyadenylation specific factor 3, 73kDa

Entrez Gene ID

Human	51692
Mouse	54451
Rat	298916

UniProt ID

Human	Q9UKF6
Mouse	Q9QXK7
Rat	Q499P4

Function

Component of the cleavage and polyadenylation specificity factor (CPSF) complex that play a key role in pre-mRNA 3'-end formation, recognizing the AAUAAA signal sequence and interacting with poly(A) polymerase and other factors to bring about cleavage and poly(A) addition. Has endonuclease activity, and functions as mRNA 3'-end-processing endonuclease. Also involved in the histone 3'-end pre-mRNA processing. U7 snRNP-dependent protein that induces both the 3'-endoribonucleolytic cleavage of histone pre-mRNAs and acts as a 5' to 3' exonuclease for degrading the subsequent downstream cleavage product (DCP) of mature histone mRNAs. Cleavage occurs after the 5'-ACCCA-3' sequence in the histone pre-mRNA leaving a 3'hydroxyl group on the upstream fragment containing the stem loop (SL) and 5' phosphate on the downstream cleavage product (DCP) starting with CU nucleotides. The U7-dependent 5' to 3' exonuclease activity is processive and degrades the DCP RNA substrate even after complete removal of the U7-binding site. Binds to the downstream cleavage product (DCP) of histone pre-mRNAs and the cleaved DCP RNA substrate in a U7 snRNP dependent manner. Required for the selective processing of microRNAs (miRNAs) during embryonic stem cell differentiation via its interaction with ISY1 (By similarity).

Required for the biogenesis of all miRNAs from the pri-miR-17-92 primary transcript except miR-92a (By similarity).

Only required for the biogenesis of miR-290 and miR-96 from the pri-miR-290-295 and pri-miR-96-183 primary transcripts, respectively (By similarity).

Biological Process

mRNA 3'-end processing Source: Reactome
mRNA 3'-end processing by stem-loop binding and cleavage Source: UniProtKB
mRNA cleavage Source: ProtInc
mRNA export from nucleus Source: Reactome
mRNA polyadenylation Source: GO_Central
mRNA splicing, via spliceosome Source: Reactome
Termination of RNA polymerase II transcription Source: Reactome

Cellular Location

Nucleus

PTM

Sumoylated on Lys-462, Lys-465 and Lys-545, preferentially by SUMO3.

Li, N., Jiang, S., Fu, R., Lv, J., Yao, J., Mai, J., ... & Lu, M. (2021). Cleavage and polyadenylation-specific factor 3 induces cell cycle arrest via PI3K/Akt/GSK-3β signaling pathways and predicts a negative prognosis in hepatocellular carcinoma. Biomarkers in Medicine, 15(5), 347-358.

Ross, N. T., Lohmann, F., Carbonneau, S., Fazal, A., Weihofen, W. A., Gleim, S., ... & Beckwith, R. E. (2020). CPSF3-dependent pre-mRNA processing as a druggable node in AML and Ewing’s sarcoma. Nature chemical biology, 16(1), 50-59.

Kakegawa, J., Sakane, N., Suzuki, K., & Yoshida, T. (2019). JTE-607, a multiple cytokine production inhibitor, targets CPSF3 and inhibits pre-mRNA processing. Biochemical and biophysical research communications, 518(1), 32-37.

Ning, Y., Liu, W., Guan, X., Xie, X., & Zhang, Y. (2019). CPSF3 is a promising prognostic biomarker and predicts recurrence of non‑small cell lung cancer. Oncology Letters, 18(3), 2835-2844.

Swale, C., Bougdour, A., Gnahoui-David, A., Tottey, J., Georgeault, S., Laurent, F., ... & Hakimi, M. A. (2019). Metal-captured inhibition of pre-mRNA processing activity by CPSF3 controls Cryptosporidium infection. Science translational medicine, 11(517), eaax7161.

Wall, R. J., Rico, E., Lukac, I., Zuccotto, F., Elg, S., Gilbert, I. H., ... & Horn, D. (2018). Clinical and veterinary trypanocidal benzoxaboroles target CPSF3. Proceedings of the National Academy of Sciences, 115(38), 9616-9621.

Palencia, A., Bougdour, A., Brenier‐Pinchart, M. P., Touquet, B., Bertini, R. L., Sensi, C., ... & Hakimi, M. A. (2017). Targeting Toxoplasma gondii CPSF 3 as a new approach to control toxoplasmosis. EMBO molecular medicine, 9(3), 385-394.

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Please try the standard protocols which include: protocols, troubleshooting and guide.

Enzyme-linked Immunosorbent Assay (ELISA)
Flow Cytometry
Immunofluorescence (IF)
Immunohistochemistry (IHC)
Immunoprecipitation (IP)
Western Blot (WB)
Enzyme Linked Immunospot (ELISpot)
Proteogenomic
Other Protocols

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Isotype control

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

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